Pubmed abstracts for Protein-Protein Interaction search result :

Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.51600385
Single chain C1s proenzyme was activated to two chain C1s with self activated C1r . 0.51600385^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.58474979
In order to define the boundaries of the C1r domain ( s ) responsible for Ca2+ binding and Ca2+ dependent interaction with C1s and to assess the contribution of individual modules to these functions , the CUB , EGF , and CUB EGF fragments were expressed in eucaryotic systems or synthesized chemically . 0.58474979^^^ These data demonstrate that the C1r CUB EGF module pair ( residues 1 175 ) is the minimal segment required for high affinity Ca2+ binding and Ca2+ dependent interaction with C1s and indicate that Ca2+ binding induces a more compact folding of the CUB EGF pair . . 0.57446553^^^ Ca2+ dependent interaction of intact C1r with C1s was studied using surface plasmon resonance spectroscopy , yielding KD values of 10 . 9 29 . 7 nM . 0.50213176^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Analysis of C components immunochemically demonstrated a marked reduction of C1q and C1s inhibitor , undetectable C1r , C1s and an elevated B . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Synthetic inhibitors of trypsin , plasmin , kallikrein , thrombin , C1r , and C 1 esterase . p Carbethoxyphenyl episol guanidinocaproate and p ( p ' guanidinobenzoyloxy ) phenyl derivatives were prepared , and their inhibitory effects on trypsin , plasmin , plasma kallikrein , thrombin , C1r and C 1 esterase were examined . ^^^ Among the various inhibitors tested , p nitrophenyl p ' guanidinobenzoate , N , N dimethylamino p ( p ' guanidinobenzoyloxy ) benzoyl glycolate and N , N dimethylamino p ( p ' guanidinobenzoyloxy ) benzilcarbonyloxy glycolate were the most effective inhibitors of trypsin , plasmin , plasma kallikrien and thrombin , and they strongly inhibited the esterolytic activities of C1r and C 1 esterase . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Formation of complexes composed of C1r , C1s , and C 1 inactivator in human serum on activation of C 1 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Studies have been performed with platelets using C 1 haemolytic assays and platelet aggregation induced by anti C1q , anti C1s and aggregated IgG in the presence of C 1 subcomponents C1q , C1r and C1s . ^^^ The addition of C1q restored the reactivity of the platelets to aggregated IgG while the addition of C1r or C1s was without effect . ^^^ Furthermore , the addition of C1r or C1s to C1q inhibited the action of C1q in platelet aggregation induced by IgG . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r and C1s were disproportionally high compared with the C1q levels . ^^^ Furthermore , crossed immunoelectrophoresis revealed abnormal complexes composed of C1r and C1s , and complexes composed of C1r , C1s and C 1 IA . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Binding of C 1 via C1q in this manner leads to activation of C1r , C1s , and thus of the classical C pathway . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
All of the C1q , C1r , and C1s detected in normal serum was found to be in the C 1 complex . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Proenzymic C1s associated with catalytic amounts of C1r . ^^^ Proenzymic C1s isolated from human plasma by euglobulin precipitation and DEAE cellulose chromatography is associated with trace amounts of C1r ( 0 . 5 1 % on a molar basis ) . ^^^ From the kinetic experiments and from the inhibition characteristics , the activation of C1s can be attributed to the presence of C1r , which appears to undergo activation and then to activate secondarily C1s . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Hemolytic titrations of C 1 , C 4 , C 2 , C 3 , and C 5 showed a complete inhibition of C 4 , C 2 and C 3 , and a partial inhibition of C 1 ( C1q , C1r , C1s , Ca++ ) and C 5 , by this drug . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The peptic fragment blocked the reconstitution of C 1 haemolytic activity by competing with intact subcomponent C1q in the utilization of a mixture of the other two subcomponents , C1r and C1s . 4 . ^^^ The peptic fragment was unable to block efficiently the reconstitution of C 1 haemolytic activity unless it was added to the mixture of subcomponents C1r and C1s before the attempt to reconstitute C 1 haemolytic activity , in solution , or on the surface of antibody coated erythrocytes . 7 . ^^^ Evidence was obtained that suggested that subcomponent C1q bound the subcomponent C1r C1s complex more efficiently when the subcomponent C1q was bound to antibody than when it was free in solution . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The inability of C 1 to induce particle agglutination might be caused by the C 1 subunits C1r and C1s sterically inhibiting the subunit C1q to bridge between the particles . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The C1r was found to reconstitute C 1 complex when it reacted with rabbit C1q and C1s in the presence of Ca2+ , since C1s was able to bind to C1q bound on sensitized sheep erythrocytes only in the presence of C1r . ^^^ This result indicates that a part of the H chain of C1s not contributing to the structural integrity of an active site may be involved in the binding of C1s to C1r . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
However , the peptide esterase inhibitors Trasylol , hirudin , leupeptin , and C 1 esterase inhibitor had no effect on the esterase activity of C1r . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The inhibitor binds rapidly to subcomponent C1s , and more slowly to subcomponent C1r . ^^^ Formation of the C1r C 1 inhibitor complex causes rapid dissociation of subcomponents C1r and C1s from the antibody antigen component C 1 aggregate . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The isolated complexes were shown to contain antigen , antibody , C1q , C1r , C1s and C 3 . ^^^ The isolated material was found to contain IgM , IgG , C1q , C1r , C1s , C3c and C3d . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Activation can be achieved by incubation with human C1r , resulting in cleavage of the C1s chain into two chains of 65000 and 27000 mol . wt . and the generation of an isoleucine N terminal residue on the smaller chain . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The role of C1s , C1r and properdin in the initiation of the C3b dependent feedback mechanism of the complement system . ^^^ The influence of activated C1s , C1r and properdin in the fluid phase initiation of the C3b dependent feedback mechanism of the human complement was studied . ^^^ When a normal serum was incubated with C1r before incubation with C1s , only C 3 was converted , whereas factor B remained in the unaltered native state . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Epithelial and mesenchymal cells synthesized and secreted all three subcomponents of the first component of complement ( C 1 ) : C1q , C1r , and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Modulation of the antigenicity of C1r and C1s by C 1 inactivator . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r and C1s associated with a lupus erythematosus like disease . ^^^ Complete absence of C1r and almost complete absence of C1s were found in 4 of 8 living siblings . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The activation of subcomponents C1r and C1s in the first component of complement , C 1 , when bound to antibody antigen complexes was investigated . ^^^ Activation was followed both by the splitting of the peptide chains of subcomponents C1r and C1s and by the development of proteolytic activity . ^^^ For the maximum rate of activation to occur , all components must be present in approximate molar proportions of antibody : C1q : C1r : C1s of 13 : 1 : 5 : 5 . ^^^ For activation of subcomponent C1s , subcomponents C1r or C1r , but not C1r inactivated with iPr2P F ( di isopropyl phosphorofluorideate ) , are effective . ^^^ For activation of subcomponent C1r , subcomponents C1s , C1s or C1s inactivated with iPr2P F are effective . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Interaction of C 1 inhibitor with the C1r and C1s subcomponents in human C 1 . 1 . ^^^ C 1 inhibitor bound to both subcomponents ( C1r and C1s in C 1 and formed stable complexes of respective apparent molecular weights 197 , 000 and 185 , 000 , as determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis . ^^^ The binding reaction proceeded more readily with C1s than with C1r and was correlated with the inhibition of C1s esterase activity . 3 . ^^^ At physiological ionic strength , binding of C 1 inhibitor to subcomponents C1r and C1s caused release of these subcomponents from the C 1 immune aggregates complex , indicating that C 1 inhibitor binding decreased the inter subcomponent binding forces in C 1 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Fractionation of C 1 by DEAE Cellulose chromatography under the conditions that led to the original identification of C1q , C1r , and C1s resulted in recovery of 2 P 2 in the fractions containing C1r . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Affinity chromatography of serum on Sepharose tryptophan modified IgG resulted in the binding of only C1r and C1s . ^^^ By the use of purified C 1 proteins and Sepharose IgG in binding studies it was confirmed that both C1q and C1r bind independently to sites on IgG and hold C1s and C1t by Ca++ dependent bonds . ^^^ Both C1t and C1r independently enhanced the C 1 activity of C1q C1s mixtures ; maximal activity required all four subcomponents . ^^^ The evidence suggests that the spatial sequence of the components of the Sepharose IgG Serum C 1 complex is : Sepharose IgG : C1q : C1t : C1s : C1r : IgG Sepharose . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r had a high affinity for active C1s or proenzyme C1s in the presence of calcium and was able to activate C1s and to form C 1 in conjunction with C1q and C1s . ^^^ Activation of C1s by C1r was inhibited by calcium , C 1 inactivator , polyanethol sulfonate , and DFP . ^^^ Activation of C1s by C1r occurred only after a preliminary incubation of C1r for a brief time at 37 degrees C before addition of C1s . ^^^ The ability of C1r to form C 1 in conjunction with C1q and C1s was , however , progressively lost on incubation at 37 degrees C . ^^^ The binding of 125I C1r to sensitized sheep erythrocytes required the presence of C1q and calcium but not C1s , whereas the binding of 125I C1s required C1q , C1r and calcium . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Studies have been performed with platelets using C 1 haemolytic assays and platelet aggregation induced by anti C1q , anti C1s and aggregated IgG in the presence of C 1 subcomponents C1q , C1r and C1s . ^^^ Furthermore , the addition of C1r or C1s to C1q inhibited the action of C1q in platelet aggregation induced by IgG . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Highly purified subcomponents C1q , C1r and C1s were recovered at DEAE Sephadex chromatography from such purified C 1 material after EDTA treatment . ^^^ Tests on isolated C1q , C1r and C1s disclosed in addition to the well known interaction between heparin and C1q an equally strong or even stronger interaction between heparin and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r and C1s were recovered in the proenzyme form and their identity was established by SDS polyacrylamide gel electrophoresis before and after reduction and alkylation , and on the basis of their esterolytic activities toward different substrates . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The structure and enzymic activities of the C1r and C1s subcomponents of C 1 , the first component of human serum complement . ^^^ The subcomponents C1r and C1s and their activated forms C 1r and C 1s were each found to have mol . wts . in dissociating solvents of about 83000 . ^^^ The amino acid compositions of each were similar , but there were significant differences in the monosaccharide analyses of subcomponents C1r and C1s , whether activated or not . ^^^ Subcomponents C1r and C1s have only one polypeptide chain , but subcomponents C 1r and C 1s each contain two peptide chains of approx . mol . wts . 56000 ( `` a ' ' chain ) and 27000 ( `` b ' ' chain ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1q , C1r , C1s , C 3 , C 4 and C 1 IA were determined by electroimmunoassay in sera from 150 patients with chronic urticaria or angioedema . ^^^ Sera from 11 % of the patients contained C1r C1s complexes . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Interaction with complement subcomponents C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
In the case of proenzymic C1s , di isopropyl phosphorofluoridate ( 0 . 5 5 mM ) is added at all stages of the purification procedure , which includes euglobulin precipation followed by DEAE cellulose chromatography and affinity chromatography on anti C1r IgG Sepharose 6B . ^^^ The final step completely removes contaminant traces of C1r and / or C1r , ensuring that the final preparation of C1s is stable in the proenzyme form and suitable for activation studies . 2 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 was reconstituted in macromolecular proenzyme , nonactivated form by incubation of highly purified C1q , C1r , and 125I C1s together in the presence of calcium . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
We describe a 46 year old women with a seven year history of urticarial like symptoms and cutaneous vasculitis with marked deficiency of C1q in the presence of normal levels of C1r and C1s and high titers of low molecular weight ( 7S ) C1q precipitins . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The unactivated subcomponents were also isolated , and evidence is given that the three subcomponents C1q , C1r and C1s account wholly for the activity of component C 1 in serum . ^^^ The approximate molar proportions of the subcomponents in serum are C1q / C1r / C1s = 1 : 2 : 2 . ^^^ Optimum activity by haemolytic assay was found at approximate molar proportions C1q / C1r / C1s of 1 : 4 : 4 . ^^^ No activity was found when subcomponents were assayed singly or in pairs , except for subcomponents C1q and C1s , which in molar ratio 1 : 4 gave 15 20 % of the activity of the mixture C1q + C1r + C1s . ^^^ Subcomponents C1q + C1r + C1s and C1q + C1s in the presence of antibody antigen aggregates were activated and inactivated simultaneously , showing a peak of activity and subsequent loss of activity . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r values were well correlated to the levels of C1q ( r = 0 . 708 ) and of C1s ( r = 0 . 768 ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The alpha 2 peak was a complex composed of C 1 IA , C1s and C1r proteins . ^^^ The molecular species in the beta 1 region was shown to be a calcium dependent complex of C1r and C1s , probably in proenzyme form . the C1r C1s complex formed macromolecular C 1 on addition of purified C1q to serum . ^^^ During electrophoresis activation of C 1 subcomponents was initiated by a mechanism involving CIr with generation of CIs activity in eluted fractions corresponding to the position of macromolecular C 1 as well as in the beta region . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The substrate profile of D was dinstinct when compared to that of CIs , CIr , plasmin , urokinase , and trypsin . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Factor H was shown to complex with intact C 1 , to isolated C1q and to the C1r : C1s tetramer . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Based on analyses of molecular size , antigenicity , and 11 NH 2 terminal amino acid sequences of the L chain , we conclude that MASP is a novel protein different from C1r or C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 inhibitor ( C1I ) , a member of the serine protease inhibitor superfamily , is the principal regulator of the activation classical pathway of complement by reducing the proteolytic activity of activated C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Isolation and comparison of the proenzyme and activated forms of the human serum complement subcomponents C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
These results suggest that , in the case of rabbit C1s , the primary product of activation with C1r , C1s ( 1 ) , may be susceptible to further cleavage of its H chain without any loss of C1s activity , resulting in the formation of C1s ( 2 ) , though the active principle responsible for this conversion remains to be elucidated . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r was unable to cleave and activate proenzyme C1s unless first incubated at 37 degrees C in the absence of calcium before the addition of C1s . ^^^ Thus , C1r is converted from an inactive form into an enzyme , C1r , able to cleave and activate C1s by proteolytic cleavage in marked analogy to the activation of several other complement enzymes . ^^^ In other studies , cleavage of C1r was not accelerated by the addition of C1r ot C1s . ^^^ Proteolytic cleavage of the C1r molecule was found to occur on addition of aggregated IgG to a mixture of C1q , C1r , and C1s in the presence of calcium . ^^^ Neither C1q , C1s nor aggregated IgG alone , not C1r nor C1s induced C1r cleavage . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The role of C 1 esterase inhibitor in the activation of C1r , a subcomponent of the first component of complement from human plasma . ^^^ On thecolumn , the C 1 esterase inhibitor activity was found to coincide with Clr but not C1s ( another subcomponent of the first component ) C1r was isolated from the euglobulin fraction of human serum by DEAE cellulose column chromatograph . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The protein contains several domains : a signal peptide , a putative propeptide , a catalytic domain with an active center typical of a Zn ( 2+ ) metalloprotease , an EGF like domain and two internal repeats similar to repeated domains found in the C1s and C1r serine proteases of the complement cascade . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r is a Ca ( 2+ ) binding serine protease that interacts with two other plasma proteins , C1q and C1s , to form C 1 , the first component of the complement cascade . ^^^ The antibody reacts with native and heat denatured C1r , and with zymogen C1r , but does not cross react with C1s or C1q . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The use of the method is illustrated on distantly related domains shared by complement components C1S and C1R , calcium dependent serine proteinase and bone morphogenetic protein 1 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Apart from cleaving C1s , we demonstrate for the first time that : 1 ) at concentrations found in serum , the activated forms of the complement components C1r in addition to C1s can cleave the heavy chain of MHC class 1 antigens , 2 ) the cleavage by C1r and C1s is seemingly dependent upon a native configuration of the MHC class 1 antigen , since heat denaturation of the HLA antigens reduce the cleavage . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Recombinant human complement subcomponent C1s lacking beta hydroxyasparagine , sialic acid , and one of its two carbohydrate chains still reassembles with C1q and C1r to form a functional C 1 complex . ^^^ Furthermore , the mutated protein displays good hemolytic activity when reassembled with C1q and either human serum or recombinant C1r , demonstrating that these posttranslational modifications are not critical for any of the multiple interactions between C1s and C1q , C1r , C 2 , and C 4 required for reassembly of the C 1 complex , activation , and initiation of the classical complement pathway . ^^^ The 4 . 0S recombinant C1s dimerizes to yield 5 . 6S C1s2 in the presence of Ca2+ and forms the 9 . 1S C1s C1r C1r C1s tetramer upon the addition of human serum C1r and the 15 . 6S C 1 complex upon the addition of C1q to the tetramer . ^^^ The recombinant C1s is secreted and isolated as the unactivated zymogen , and it may be activated by human serum C1r which cleaves at Arg 422 Ile423 to yield the characteristic heavy and light chains . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Interestingly , patients with evidence of HUVS fairly consistently had zymogen ( C1r C1s ) 2 complexes in their serum , while patients with SLE showed high concentrations of complexes containing Cl inhibitor , C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Inhibition of complement proteins D , B , C 2 , C1s , C1r , 1 , and the catalytic fragments Bb and C2a by substituted isocoumarins was investigated . 3 , 4 Dichloroisocoumarin , a general serine protease inhibitor , inhibited factor D , C1r , and C1s moderately with second order inhibition constants ( kobs / [ 1 ] ) of 40 to 190 M 1 s 1 , but it did not inhibit C 2 , factor B , C2a , or Bb . ^^^ Most isocoumarins did not inhibit C 2 or C2a ; only 4 chloro 3 isothiureidoalkoxyisocoumarins were slightly inhibitory . 3 Alkoxy 4 chloro 7 guanidinoisocoumarins inhibited C1r and C1s moderately . ^^^ The best inhibitor for C1r and C1s was 4 chloro 3 ( 3 isothiureidopropoxy ) isocoumarin with kobs / [ 1 ] values of 6 , 600 and 130 , 000 M 1 s 1 , respectively . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Mouse MHC class 1 antigen specific determinants could also be detected in supernatant from mouse spleen cells incubated with C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r and C1s , the serine protease components of activated C 1 , form a tetramer in the presence of Ca2+ . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Analysis of a tld cDNA reveals three sequence motifs : an N terminal region of similarity to a metalloprotease , two EGF like repeats , and five copies of a repeat found in human complement proteins C1r and C1s . tld sequence is 41 % identical to human bone morphogenetic protein 1 ( BMP 1 ) ; the closest members to dpp within the TGF beta superfamily are BMP 2 and BMP 4 , two other bone morphogenetic proteins . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
At the time of acute edema the complement profile was typical : virtual absence of C 1 INH function was associated with diminished concentrations of the components of the classical pathway of complement ( C1q , C1r , C1s , C 2 , C 4 ) and reduced complement hemolytic activity ( CH 50 ) . ^^^ Although there was only a minor adjustment to the therapy , the C1q , C 2 , C 4 and CH 50 values gradually increased to levels close to the lower limit of the normal range , while C1r and C1s showed normal values . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Human IgG immobilized on the polyacrylate support was used for isolation of the first complement component from human serum and for its separation into subcomponents C1r , C1s and C1q by a one step method . ^^^ The stepwise elution of C1r , C1s and C1q from the column reflects the course of C 1 breakdown after its activation on immune complex formation . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Isolation of human complement subcomponents C1r and C1s in their unactivated , proenzyme forms . ^^^ We have modified a standard isolation procedure for C1r and C1s , which employs IgG Sepharose affinity chromatography followed by DEAE chromatography . ^^^ In addition , purification was improved by washing the IgG Sepharose column with a buffer free of added divalent cations immediately prior to elution of the C1r and C1s with EDTA . ^^^ The final yields of highly purified C1r and C1s were about 20 % ; little or no activated material was detected in these highly purified fractions . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Both type 1 and type 2 fibroblasts synthesized normal amounts of C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The first repeat bears homology to domain 3 of complement components C1r and C1s , and the second repeat is homologous to the C 1 and C 2 domains of coagulation factors 5 and 8 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Measurement of macromolecular interactions between complement subcomponents C1q , C1r , C1s , and immunoglobulin IgM by sedimentation analysis using the analytical ultracentrifuge . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
All of the disulfide bonds of the earlier described substructures of C1s , the EGF homologous part , the two SCR units , and the two domains typical for C1s and C1r are localized within these domains . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Virions activated the C 1 complex , reconstituted from C1q , proenzyme C1r , and 125I labeled proenzyme C1s , to an extent comparable with that obtained with immunoglobulin G ovalbumin immune complexes . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 inhibitor ( C1inh ) , a member of the serine protease inhibitor gene superfamily , is a glycosylated plasma protein inhibiting the proteolytic activities of C1r and C1s and involved in the regulation of coagulation , fibrinolysis and kinin releasing systems . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The specificity of this reaction was proved by the inhibitory effect of F ( ab ' ) 2 antibodies to C1q and by the inability of MPO to bind to C1r , C1s and IgG . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
To evaluate the involvement of the complement system in atherogenesis , we investigated the effect of camostat mesilate ( CM ) , C1r , and C 1 esterase inhibitor on cholesterol induced atherosclerosis in rabbits . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Complement components C1r / C1s , bone morphogenic protein 1 and Xenopus laevis developmentally regulated protein UVS . 2 share common repeats . ^^^ Property patterns were constructed , based on an alignment of related domains in human complement subcomponents C1r and C1s as well as in the sea urchin protein uEGF . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
We studied the activation and C 1 inactivator dependent dissociation of the first component of complement , the C1q ( C1r C1s ) 2 complex , in relation to recruitment of the classical activation pathway in the circulation of 24 patients with systemic lupus erythematosus ( SLE ) . ^^^ High serum concentrations of trimer complexes containing C 1 inactivator , activated C1r and zymogen C1s ( C 1 IA C1r C1s ) were found in the majority of the patients . ^^^ Some patients with high C 1 IA C1r C1s concentrations showed no evidence of classical pathway activation , indicating that C 1 activation was controlled by the action of C 1 IA at the C1r level . ^^^ By contrast , formation in serum of tetramer complexes in which C 1 IA was firmly bound to both C1r and C1s ( C 1 IA C1r C1s C 1 IA ) was associated with C 2 and C 3 cleavage in EDTA plasma , and with manifest hypocomplementemia . ^^^ Low C 1 IA C1r C1s C 1 IA values were observed in conjunction with substantial C 2 cleavage in a few patients . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The specificity of the IL 4 effect was also apparent when comparing the effect of IL 4 on the TNF induced synthesis of factor B to the effects on total protein synthesis ( increased 1 . 5 fold ) and the TNF induced increases in synthesis in C1r , C1s , C 1 inhibitor , C 2 , and factor H ( no changes ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
In contrast , both alpha 2 and the N terminal alpha 1 fragment , starting at serine 24 of the A chain , were able to compete significantly with intact C1s for the formation of the Ca 2 ( + ) dependent C 1 s C1r C 1 r C 1 s tetramer . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Neutron scattering study of the ( gamma B ) catalytic domains of complement proteases activated C1r and C1s . ^^^ The catalytic domains of activated C1r and C1s , comprising the C terminal region of the A chain ( gamma ) , disulphide linked to the B chain , were obtained by limited proteolysis of the native proteases with chymotrypsin and plasmin , respectively , and studied by small angle neutron scattering . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The specificity of this interaction was further substantiated by the finding that neither macromolecular C 1 , or subcomponents C1r and C1s , nor human or murine IgG nor IgM had any inhibitory activity when cultured with these cell lines . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The binding of C1s to the cell bound S MBP require the presence of C1r , suggesting that C1r2s2 binds to S MBP through C1r . ^^^ The activation of C1s from a proenzyme to a protease was mediated by cell bound S MBP in the presence of C1r and the activated protease remained associated with the cells and was not released into the medium . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Trimer and tetramer complexes containing C 1 esterase inhibitor , C1r and C1s , in serum and synovial fluid of patients with rheumatic disease . ^^^ During activation , the first component of complement C1q ( C1r C1s ) 2 is dissociated in conjunction with the formation of complexes containing C 1 esterase inhibitor ( C 1 INH ) . ^^^ Trimer complexes , with zymogen C1s associated with a firm C 1 INH C1r complex ( C 1 INH C1r C1s ) can be distinguished from tetramer complexes C 1 INH C1r C1s C 1 INH ) in which C 1 INH is firmly bound to both proteases . ^^^ In the present study a two stage electroimmunoassay was developed for the specific measurement of C 1 INH C1r C1s . ^^^ In the second step , C1s contained in C 1 INH C1r C1s was dissociated in the presence of EDTA and was measured by immunoprecipitation with anti C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NH 2 terminal calcium binding domain of human complement C1s mediates the interaction of C1r with C1q . ^^^ The assembly of C 1 , the first component of human complement , involves interactions between various domains of each of its three subcomponents , C1q , C1r , and C1s . ^^^ The isolation , assignment of function , and structural characterization of the individual domains of C1r and C1s are critical for a thorough understanding of this complex assembly . ^^^ This fragment , C1s alpha , was shown in the presence of Ca2+ to mimic the ability of whole C1s to self associate , bind to C1r , and facilitate the binding of C1r to C1q . ^^^ These results directly prove that the Ca 2 ( + ) binding sites of C1s as well as all of the determinants necessary for binding of C1s to C1r and C1q are located in the NH 2 terminal 27 kDa alpha region of the A chain . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
There was a discrepancy between the low C1q and the high C1r and C1s levels in blood . ^^^ Complexes of C1r C1s C 1 inactivator and factor B conversion products were found , especially in the peritoneal fluid , denoting an activation of the complement system . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Combined IgG 2 , IgG 4 and IgA deficiency : low C1q concentrations and the presence of excess C1r and C1s in an adult patient with recurrent pneumococcal infections . ^^^ However , the concentrations of circulating C1q were persistently decreased , and the sera contained an excess of C1r C1s complexes , resembling the C 1 aberrations previously found in children with recurrent acute otitis media . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
In vitro , C1q can be bound by immune complexes and induce activation of the proenzymes C1r and C1s , resulting in an activated C 1 molecule . ^^^ In the presence of C 1 In in the reaction mixture C1r and C1s are dissociated rapidly from the immune complex bound C1q . ^^^ This C1q has the possibility to interact with free precursor C1r and C1s to form a new C 1 molecule at the surface of the immune complex and induce a new cycle of activation . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Proteins of the C 1 complex , C1q , C1r , and C1s , of the classical pathway of complement activation are known to be synthesized in human skin fibroblasts . ^^^ As previously reported , fibroblasts also synthesized C1r and C1s . ^^^ IFN gamma , IFN beta 1 , and TNF had significant , but distinct , effects on synthesis of C 1 inhibitor , C1r , and C1s . ^^^ Incubation of the cells with IFN gamma , 1000 U / ml , for 24 h induced increases in the synthesis of C 1 inhibitor , C1r , and C1s by 4 . 2 , 1 . 9 and 1 . 6 fold , respectively . ^^^ TNF , 12 . 5 ng / ml , induced increases in the synthesis of C 1 inhibitor , C1r , and C1s by 1 . 5 , 1 . 4 and 2 . 6 fold . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Human genes for complement components C1r and C1s in a close tail to tail arrangement . ^^^ The amino acid sequence of C1s was 40 . 5 % identical to that of C1r , with excellent matches of tentative disulfide bond locations conserving the overall domain structure of C1r . ^^^ DNA blotting and sequencing analyses of genomic DNA and of an isolated genomic DNA clone clearly showed that the human genes for C1r and C1s are closely located in a `` tail to tail ' ' arrangement at a distance of about 9 . 5 kilobases . ^^^ Furthermore , RNA blot analyses showed that both C1r and C1s genes are primarily expressed in liver , whereas most other tissues expressed both C1r and C1s genes at much lower levels ( less than 10 % of that in liver ) . ^^^ Multiple molecular sizes of specific mRNAs were observed in the RNA blot analyses for both C1r and C1s , indicating that alternative RNA processing ( s ) , likely an alternative polyadenylylation , might take place for both genes . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
This report describes the different activation steps for C1q , C1r , C1s , C 4 and C 2 and summarizes monoclonal antibodies reported so far which recognize either conserved epitopes or activation dependent epitopes with particular emphasis on neoepitopes occurring during the activation cascade . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
It enhances C1r and C1s biosynthesis at a pretranslational level . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The association between inherited deficiencies of the classical pathway complement components ( C1q , C1r , C1s , C 4 , C 2 and C 3 ) and immune complex disease shows that complement is involved in protection against the development of immune complex disease ( ICD ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Although subcomponents C1r and C1s of the first complement component , C 1 , have been established to be in the same linkage group as the proline rich protein gene cluster on chromosome 12p13 . 2 , no direct analysis of linkage between the C1R and C1S structural gene loci has been available . ^^^ We have detected through a population screening study 5 families which are heterozygous at the structural loci for both C1R and C1S . ^^^ A maximum lod score of 1 . 505 at theta = 0 . 00 was found in a two point analysis between C1R and C1S . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The sequences of C1r and C1s show that each is constructed from six protein domains . ^^^ C1r and C1s are elongated macromolecules of lengths 18 20 nm . ^^^ This places each monomer of C1r and C1s on four adjacent arms of C1q , and offers the most reasonable explanation of the known properties of the C 1 complex . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Structure and function of C1r and C1s : current concepts . ^^^ C1r and C1s , the constituent proteins of C1s C1r C1r C1s , the Ca2+ dependent catalytic unit of C 1 , are homologous serine proteinases that share a common activation pattern and have similar structural organizations at the monomeric level . ^^^ Overall sequence comparison of C1r and C1s reveals 40 % amino acid identity and conservation of all cysteine residues . ^^^ In contrast , C1r and C1s widely differ from each other by their glycosylation patterns : both proteins contain Asn linked carbohydrates , but four glycosylation sites are present on C1r , and only two on C1s . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The structures of human C1r and C1s and their relationship to other serine proteases . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Biosynthesis of C1r and C1s subcomponents . ^^^ Biosynthesis of C1r and C1s subcomponents has been studied using monocytes and macrophages , hepatocytes and hepatoma cell lines or fibroblasts . ^^^ C1r and C1s were secreted by stimulated monocytes and by Hep G 2 cells , according to a 1 : 1 stoichiometry . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin . ^^^ While the protease regions of the serine zymogens are typically encoded by multiple exons , the protease domains of C1s and of its genetically linked and functionally interacting homolog C1r are encoded as intronless domains , not unlike a region of haptoglobin , which in fact is devoid of proteolytic activity . ^^^ Additional evidence of the common ancestry of C1r , C1s and haptoglobin is the presence , within the protease domain , of a set of sequence markers that distinguish these three proteins from all known serine proteases . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Despite structural similarities between MBP and the C1q subcomponent of the first complement component , MBP did not restore classical pathway activity to C1q deficient serum , nor did it activate C1s when added to a mixture of C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
An affinity sorbent comprising macroporous glass coated with the polymer with the polymer with immobilized immunoglobulin IgG was used for the isolation from human serum of the first component of the complement and for its separation into subcomponents C1r , C1s and C1q by the one step procedure . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Diamines at concentrations which dissociate C 1 into C1q and ( C1r , C1s ) 2 , strongly inhibited the interaction of C1q or C1qCLF with LPS . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The first component of complement : the subcomponents of C1q , C1r , C1s , C 1 inhibitor , C1q receptors . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Previously two distinct models for its structure have been described , in which C1r2C1s2 is either a linear rod like assembly of the globular domains found in each of C1s and C1r , or these domains are arranged to form an asymmetric 10 shaped structure . ^^^ The data on C1s , C1s2 and C1r are readily represented by straight hydrodynamic cylinders , but not C1r2 or C1r2C1s2 . ^^^ The total length of the C1s and C1r monomers was determined as 17 20 nm , which is compatible with electron microscopy . ^^^ On the basis of the known sequences of C1r and C1s , this length is accounted for by a linear arrangement of a serine proteinase domain ( length 4 nm ) , two short consensus repeat domains ( 2 10 4 nm ) , and a globular entity containing the 1 , 2 and 3 domains ( 4 7 nm ) . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 reconstituted from purified C1r expressed in insect cells together with human C1q and C1s proved biologically active in a hemolytic assay . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 deficiency results from an absence or lowering of the level of one or more of the proteins C1q , C1r and C1s , which are the subcomponents of the C 1 complex of the classical pathway of the serum complement system . ^^^ Both acquired and genetic deficiencies of the C 1 subcomponents have been reported ; the possible genetic deficiencies appear quite rare , with only 14 reports of C1q deficiency ( involving 24 people ) and six reports of C1r / C1s deficiency ( involving 11 people ) appearing in the literature to date . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Human complement C1r and C1s proteins and genes : studies with molecular probes . ^^^ We review here recent advances in studies of the C1r and C1s proteins and of the corresponding genes , using molecular probes . ^^^ Surprisingly , the C1r and the C1s genes feature an intronless serine protease domain , at variance with all vertebrate serine proteases . ^^^ Moreover , C1r and C1s are related in evolution to haptoglobin , a serine protease analog lacking enzymic activity . ^^^ The C1r and C1s genes are closely linked in an unusual tail to tail orientation . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
It is the only inhibitor of C1r and C1s in plasma , and is responsible for about half of the kallikrein and the majority of plasma factor 12 inactivating activity . ^^^ C 1 INH inactivation of C1r and C1s within activated macromolecular C 1 results in dissociation of C 1 with release of complexes consisting of two molecules of C 1 INH and one molecule each of C1r and C1s . ^^^ C1q is thus allowed to interact with zymogen C1r and C1s or with C1q receptors . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 INH is the only plasma protease inhibitor of activated C1r and C1s , the serine protease subcomponents of the first complement component . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Recently , using 35S methionine incorporation and immunoprecipitation techniques our laboratory has demonstrated the ability of tissue cells , i . e . , the human lung type 2 pneumocyte ( A 549 ) and human lung fibroblast ( WI 38 ) , to synthesize and secrete a variety of early and terminal complement components , as well as several regulatory proteins in vitro , i . e . , C1r , C1s , C 4 , C 3 , C 5 , C 6 , C 7 , C 8 , C 9 , factor B , factor H , factor 1 , and C1s inactivator . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r , C1s , C1q , C 3 , C 4 , and C reactive protein ( CRP ) , where tested , were found in most but not all IC . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
A highly purified N terminal fragment generated by tryptic digestion of C1r in the presence of Ca2+ retained its ability to interact with C1s , disrupting the formation of C1s dimers in the presence of Ca2+ . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
We have studied a number of these and report the presence of erythro beta hydroxyasparagine ( e beta Hyn ) in three non vitamin K dependent proteins : the plasma complement proteins C1r and C1s ( where overbar indicates activated form ) and the urinary protein uromodulin . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Spontaneous generation in human serum of a trimer complex containing C 1 inactivator , activated C1r , and zymogen C1s . ^^^ Activation of the C 1 complex in the presence of C 1 inactivator ( C 1 IA ) is known to result in the formation of tetramer C 1 IA C1r C1s C 1 IA complexes that are dissociated from C1q . ^^^ Both C1r and C1s of the tetramers are present in their activated forms . ^^^ The present investigation concerned the generation of trimer complexes containing C 1 IA , activated C1r , and zymogen C1s ( C 1 IA C1r C1s ) . ^^^ C 1 IA C1r C1s were released from C1q and were formed in high concentration during prolonged incubation ( 1 to 3 days ) of normal serum at 37 degrees C without addition of activators . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The effect of the antibody on haemolytic activity has shown that it is capable of inhibiting the formation of EAC 1 cells from EAC1q cells plus C1r and C1s but is incapable of inhibiting the C 1 activity of performed EAC 1 cells . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Two other complement components , C1r and C1s , have two of these repeating units in the carboxy terminal region of their noncatalytic A chains . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Addition of C1r and C1s to C1q and formation of C 1 did not affect its capacity to agglutinate EC3b . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
This structural unit is called SCR ( short consensus repeat ) and is found in the complement proteins C1r , C1s , C 2 , factor B , factor H , C4BP , DAF , MCP and CR 2 , each of which interacts with some cleavage products of C 3 and / or C 4 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Circulating C1INH C1r C1s complexes were evidenced by reduced ratios of functional to antigenic C1INH and antigenic C1r to C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
A rapid and efficient method for the purification of the complement subcomponents C1r and C1s in zymogen form using fast protein chromatography . ^^^ The purification of the subcomponents C1r and C1s of the first component of complement involves multiple steps and is time consuming . ^^^ The method provides C1r and C1s in a yield of 35 and 60 % respectively . ^^^ In addition , this study provides a simple and sensitive test to assess functional purity of C1r and C1s with respect to the other C 1 subcomponents . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Assignment of the complement serine protease genes C1r and C1s to chromosome 12 region 12p13 . ^^^ C1r and C1s are distinct , but structurally and functionally similar , serine protease zymogens responsible for the enzymatic activity of the first component of complement ( C 1 ) . ^^^ Recent comparisons indicate a significant degree of sequence similarity between C1r and C1s and support the hypothesis that they are related by gene duplication . ^^^ Complementary DNA probes for human C1r and C1s do not cross hybridize even at mild stringency conditions and are therefore gene specific . ^^^ Using a panel of 25 human rodent cell hybrids , we have independently assigned the C1r and the C1s genes to chromosome 12 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Domain structure and associated functions of subcomponents C1r and C1s of the first component of human complement . ^^^ The serine protease subcomponents of the activated form of the first component of human complement ( C 1 ) , C1r and C1s , were observed by electron microscopy after the native proteins and their limited proteolysis products , obtained from autolytic cleavage ( C1r ) or from incubation with plasmin ( C1s ) were rotary shadowed . ^^^ At the monomeric level , both C1r and C1s comprised two globular domains , a smaller interaction domain ( corresponding to the NH 2 terminal half of the A chain , alpha , and responsible for calcium binding and C1r C1s interaction ) and a larger catalytic domain ( corresponding to the COOH terminal part of the A chain , gamma , disulfide linked to the B chain and bearing the serine protease active site ) . ^^^ On the basis of the domain structure of C1r and C1s , a model of the calcium dependent C1s dimer is proposed , in which the two monomers interact through their NH 2 terminal interaction domains ; in the same way , a model of the C1s ( C1r ) 2 C1s catalytic subunit of C 1 is presented , in which ( C1r ) 2 forms a core , its distal interaction domains interacting with the corresponding domains of C1s . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Characteristics of complement subcomponents C1r and C1s synthesized by Hep G 2 cells . ^^^ The association and activation states of complement subcomponents C1r and C1s biosynthesized by Hep G 2 cells were studied . ^^^ C1r and C1s are secreted in stoichiometric amounts ; in the presence of Ca2+ they are associated in a complex that sediments similarly to plasma C1r2 C1s2 . ^^^ Secreted C1r is not autoactivatable but undergoes proteolysis by exogenous C1r ; secreted C1s is also proteolysed by exogenous C1r . ^^^ In the presence of immune complex bound C1q , secreted C1r and C1s are able to reconstitute C 1 , but normal activation requires extrinsic C1r2 C1s2 . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The finally purified preparation generates full Cl haemolytic activity when assayed with human complement subcomponents C1r and C1s , and have been identified as chicken C1q . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The human complement components C1r , C1s , C 4 , C 3 , factor B , and / or activated C1INH were functionally blocked in normal human serum ( NHS ) and EGTA or EDTA treated NHS by polyclonal monospecific Fab ' fragments to the individual components . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The proposed activation mechanism has four main features : steric exclusion of C 1 inhibitor from C 1 when it binds to an immune complex ; signal generation through multivalent binding of the C1q heads to an irregularly arranged cluster of antibody Fc regions , and signal transmission through the movement of the stiff C1q arms about their semi flexible joints , causing distortion of the symmetrical cone of C1q arms ; induction of rapid activation by a shift in equilibrium favoring the autocatalytic conformation of C1r2C1s2 ; and release of the activated C1s from the C1q arms , so that the ends of the tetramer are free for interaction with C 4 and C 2 and C 1 inhibitor , and the C1q subcomponent becomes more flexible , allowing access of C 1 inhibitor to C1r . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
A detailed model of C1s C1r2 C1s is proposed , according to which two C1s monomers bind to the outer globes of C1r2 by contacts between their heavy chains and those of C1r . ^^^ According to this model the catalytic domains of C1r are located in the center and those of C1s at the very tips of the C1s C1r2 C1s complex . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Differences in the mechanism of C 1 activation by nonimmune activators and by immune complexes : C1r independent activation of C1s by cardiolipin vesicles . ^^^ A similar dose response binding of C1s requiring C1q , but not C1r , was detected only on CL vesicles , but neither on PG vesicles nor on immune complexes . ^^^ The C1q bound C1s was specifically cleaved at 37 degrees C into its active 58 kDa and 28 kDa chains , in the absence of C1r . ^^^ When macromolecular C 1 was offered in the presence of C 1 INH , C1r cleavage was detected ; however , the presence of C1s was a critical factor for C1r activation , because it was required on CL vesicles , but not on immune complexes . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
CL vesicles which activate C 1 in the presence of C 1 inhibitor ( C 1 INH ) were found to bind C1s in the absence of C1r , and to induce a specific C1r independent cleavage of C1q bound C1s . ^^^ Therefore , several known natural nonimmune activators were analyzed by comparing their ability to activate C 1 in the presence of C 1 INH and to mediate a C1r independent cleavage of C1s . ^^^ DNA , known to activate C 1 only in the absence of C 1 INH , does not induce C1s cleavage in the absence of C1r . ^^^ By using C1qs2 as a probe , they exhibit a specific , C1r independent cleavage of C1s . ^^^ In the case of `` weak ' ' activators , such as E . coli smooth strains , DNA , or HHM , no C1s binding to activator bound C1q was detected , and C1r independent C1s cleavage and C 1 activation in the presence of C 1 INH were not observed . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The first component : C1q , C1r , C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Biosynthesis of the subcomponents C1q , C1r and C1s of the first component of complement ( C 1 ) by guinea pig hepatocyte primary cultures . ^^^ The hemolytic activity of C 1 and its subcomponents C1q and C1r / C1s was tested in the supernatants . ^^^ Guinea pig hepatocyte primary cultures synthesize and secrete up to 3 10 10 ( 3 ) effective C1q molecules / cell / 24 h and 34 10 10 ( 3 ) effective C1r / C1s molecules / cell / 24 h . ^^^ The synthesis of C1q and C1r / C1s could be reversibly inhibited by cycloheximide ( 50 micrograms / ml ) . ^^^ The data show that guinea pig hepatocytes are able to synthesize C 1 subcomponents , whereby the synthesis of C1q and C1r / C1s occurs independently . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Such a head to tail configuration , placed in the context of the model proposed for the C1s C1r C1r C1s catalytic subunit of C 1 [ Colomb , M . ^^^ London , B 306 , 283 292 ] , is compatible with autolytic activation of C1r through an intramolecular cross mechanism and with subsequent activation of C1s by activated C1r . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The composition of complexes containing C 1 inactivator ( C 1 IA ) , C1r and C1s was investigated in normal serum after activation of C 1 under various conditions . ^^^ Analyses were performed with PAGE of eluates from Sepharose beads coated with F ( ab ' ) 2 fragments of anti C1s followed by immunoblotting with anti C 1 IA , anti C1s or anti C1r . ^^^ Eluates obtained from serum treated with aggregated IgG ( AGG ) contained C 1 IA in complex with C1r and C1s with both subcomponents in activated form . ^^^ Eluates from serum incubated at 37 degrees C for 1 , 2 or 3 days without activators showed C 1 IA complexed with activated C1r and with C1s in proenzyme state associated to the complex . ^^^ On analysis of serum , treated as mentioned above , by a variant of the electroimmunoassay using an intermediate gel containing anti C 1 IA and with anti C1s in the anodal gel the two types of C1r C1s C 1 IA complexes could be distinguished . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Synovial fibroblast like cells synthesized C1r , C1s , C 1 inhibitor , C 2 , C 3 , factor B , and factor H , all with the same sizes and subunit structures as the proteins synthesized in skin fibroblasts . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
We have previously shown that serum levels of C1q , unbound to C1r 10 C1s , are elevated in rheumatoid arthritis . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Sera from patients with systemic lupus erythematosus contained normal levels of RHP and were characterized by deficits of C1q required to form C 1 from existing levels of C1r and C1s . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
We have studied the effects of polyclonal monospecific Fab ' preparations against C1r , C1s , C1INH , C 4 , C4bp , and fragment Bb of factor B on complement activation in NHS and HAES . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 inhibitor is a heavily glycosylated plasma protein that regulates the activity of the first component of complement ( C 1 ) by inactivation of the serine protease subcomponents , C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The findings suggested intra articular C 1 activation with dissociation of C 1 into free C1q and complexes containing C1r , C1s , and C 1 inactivator . ^^^ However , the immunochemical properties of synovial fluid C1r C1s C 1 inactivator complexes appeared to differ from those of the complexes formed in serum , which hampered quantification with the assay used . ^^^ Slightly increased concentrations of free C1q and C1r C1s C 1 inactivator complexes in serum and C3dg / d fragments in EDTA plasma were observed , particularly in the patients with rheumatoid arthritis . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The N terminal chain ( 422 residues ) of C1s , like that of C1r with which it is broadly homologous , contains five domains : domains 1 and 3 are homologous to one another and to similar regions in C1r , domain 2 is homologous to the epidermal growth factor sequence found in C1r and several other proteins , and domains 4 and 5 are homologous to one another and to the 60 residue repeating sequence found in C1r , C 2 , factor B , C 4 binding protein and some apparently unrelated proteins . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The lytic effect of NHS and C2d HS on SGL was abolished by immunochemically depleting C 1 from these sera , and reconstituted by adding purified C1q plus C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
This action of the C 1 inhibitor was over and above its ability to regulate fully activated C 1 by covalent bond formation with either the serine esterase of C1s or C1r . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The effective human urinary kallikrein inhibitors were further examined for their effect on other serine proteases , including human plasma kallikrein , plasmin , complement components ( C1s , C1r ) , bovine coagulation factors ( IIa , IXa , and Xa ) , elastase , and trypsin . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Upon activation of C 1 , C1r and C1s are rapidly inactivated by C 1 In which also forms a complex with these two subcomponents , resulting in their release from C 1 immune aggregate complexes . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
When human fibronectin ( FN ) was added after C1q , but before addition of C1r and C1s ( subunits of the first complement component ) , inhibition of haemolytic activity was observed which was strictly dependent upon the dose of FN . ^^^ When FN was added after addition of C 1 ( reconstituted from C1q , C1r and C1s ) , the haemolytic activity of complement was not affected by the presence of FN . ^^^ These data suggest that FN binds on C1q by interfering with C1r and C1s fixation . ^^^ In addition , FN was unable to displace the activated subcomponents ( C1r and C1s ) from their binding site on C1q . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Proenzyme and activated forms of C 1 subcomponents C1r and C1s and their Ca2+ dependent association ( C1r C1s ) 2 do not bind to E . coli D 31 m4 . ^^^ No turnover of the ( C1r C1s ) 2 subunit is observed . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The first component of complement , C 1 , is a calcium dependent complex of the three distinct subcomponents , C1q , C1r , and C1s . ^^^ In contrast , after dissociation of C 1 or C 1 by citrate , 100 % of the original C1q activity is recoverable on addition of C1q deficient serum as source of C1r and C1s . ^^^ EDTA treated C1q , fluid phase or bound to EA , was no longer able to form an hemolytically active C 1 complex by interaction with C1r and C1s . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Serum levels of C1q , C1r and C1s in normal and pathologic sera . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Interaction between C1q , C1r and C1s from human serum . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
A tetrameric complex of C1r2 C1s2 binds to the collagenous tails and leads to formation of the serine type proteases C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Using this simple yet sensitive assay to investigate the efficiency of reconstitution of C 1 activity from the purified components C1q , C1r , and C1s , we also find evidence for temperature and concentration dependent reaction steps in the formation of functional C1 . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Kinetics of appearance of activated C1r was the same as that of activated C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
LMW Hep ( 2 . 5 nM ) inhibited the ability of C1q ( 0 . 5 nM ) to recombine with C1r ( 1 . 4 nM ) and C1s ( 1 . 6 nM ) to form hemolytically active C 1 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Kinetics of reaction of human C 1 inhibitor with the human complement system proteases C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Activation of a complex of C1r and C1s subcomponents of human complement C 1 by the third subcomponent C1q . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Calcium binding properties of the C 1 subcomponents C1q , C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The product , C1r 2 , retained the original antigenic properties of C1r and a functional active site , but lost the capacity to bind C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The reconstitution of human C 1 , the first complement component : binding of C1r and C1s to C1q influences the C1q conformation . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Conformational changes of the subunits C1q , C1r and C1s of human complement component C 1 demonstrated by 125I labeling . ^^^ C1s and C1r proenzymes and enzymes ( C1s , C1r ) and C1q were labeled with 125I . ^^^ The presence of either C1s , C1q or C1qs during labeling reduced the C1r H chain level , although C1r remained in the proenzyme form . ^^^ This was unexpected because one would have anticipated a diminution of the C1q label due to the apposition of C1r and C1s , similarly as it occurs during C1rs complex and C1s dimer formation for the H chain label of C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The flexible rod like structure of C1r2 C1s2 is folded around two arms of C1q , with the catalytic domains of C1r and C1s inserted inside the cone defined by the C1q stalks . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Structure and activity of C1r and C1s . ^^^ During activation of the first component of the classical complement pathway the two zymogen subcomponents , C1r and C1s are converted to active proteolytic enzymes . ^^^ Activated C1r cleaves C1s which then becomes the activator of C 4 and C 2 . ^^^ Amino acid sequence studies of the proteolytic chains of C1r and C1s , carried out in Oxford and Aberdeen respectively , have shown that they belong to the serine proteinase family . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The formation of neoantigens within the C1q molecule after the binding of C1r and C1s to C1q and the binding of C1q to immune complexes is described . ^^^ This immunochemical study supports the hypothesis drawn from functional studies that the activation of the classical C pathway results from conformational changes within the C1q molecule leading to the activation of C1r and subsequently C1s . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The classical pathway has a calcium dependent step ( C1q , C1r , C1s ) and a magnesium dependent reaction ( the enzymatic action of C1s on C 4 and C 2 ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Fluid phase interaction of C 1 inhibitor ( C 1 Inh ) and the subcomponents C1r and C1s of the first component of complement , C 1 . ^^^ The interaction of C 1 Inh with the Ca2+ dependent C1r2 C1s2 complex ( 8 . 8 S ) led to an 8 . 5 S inhibited C1r C1s C 1 Inh complex ( 1 : 1 : 2 ) , indicating a disruption of C1r2 and of C1s2 on C 1 Inh binding . ^^^ The 8 . 5 S inhibited complex was stable in the presence of EDTA ; it was also formed from a mixture of C1r , C1s and C 1 Inh in the presence of EDTA or from bimolecular complexes of C1r C 1 Inh and C1s C 1 Inh . ^^^ C1r 2 , a modified C1r molecule , deprived of a Ca2+ binding site after autoproteolysis , did not lead to an inhibited tetrameric complex on incubation with C1s and C 1 Inh . ^^^ An ester link between a serine residue at the active site of C1r or C1s and C 1 Inh is postulated . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
New synthetic inhibitors of C1r , C 1 esterase , thrombin , plasmin , kallikrein and trypsin . p Guanidinobenzoate derivates were prepared and their inhibitory effects on trypsin , plasmin , pancreatic kallikrein , plasma kallikrein , thrombin , C1r and C 1 esterase were examined . ^^^ Among the various inhibitors tested , 6 ' amidino 2 naphthyl 4 guanidinobenzoate dihydrochloride , 4 ( beta amidinoethenyl ) phenyl 4 guanidinobenzoate dimethanesulfonate and 4 amidino 2 benzoylphenyl 4 guanidinobenzoate dimethanesulfonate were the most effective inhibitors of trypsin , plasmin , pancreatic kallikrein . plasma kallikrein and thrombin and they strongly inhibited the esterolytic activities of C1r and C 1 esterase , and then strongly inhibited complement mediated hemolysis . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Mapping the substrate binding site of human C1r and C1s with peptide thioesters . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
So far , human complement sub components C1r and C1s are the only known mammalian serine proteinases lacking this disulphide bridge . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Under specified conditions purified C1q , activated C1r and C1s and C1r C1s complexes were bound independently of Ca2+ , to heparin Sepharose , and could be eluted by an increasing salt gradient . ^^^ Zymogen C1r and C1s , C1r C1s complexes , C 1 inactivator , and C1r C1s C 1 activator complexes were not bound . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
For biochemical characterization , the first component of human complement ( C 1 ) was reconstituted from physiologic concentrations of purified C1q , 125I C1r , and 131I C1s . ^^^ Upon incubation at 37 degrees C , C 1 spontaneously activated , as evidenced by the characteristic proteolysis of the C1r and C1s polypeptide chains as detected by SDS PAGE analysis . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The human complement system serine proteases C1r and C1s and their proenzymes . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Proenzymic subcomponents C1r and C1s associated to form a trimeric C1r2 C1s complex ( 7 . 6 S ) in the presence of EDTA , and a tetrameric Clr 2 C1s2 complex ( 9 . 1 S ) in the presence of Ca2+ . ^^^ Iodination of the 9 . 1 S complex led to a predominant labelling of C1r ( 70 % ) over C1s ( 30 % ) , essentially located in the b chain moiety of C1r and in the a chain moiety of C1s . 2 . ^^^ Reconstruction of proenzymic soluble C 1 ( 15 . 2 S ) from C1q , C1r and C1s was partially inhibited when C1s labelled in its monomeric form was used and almost abolished when iodinated C1r was used . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The human hepatoma derived cell line , HepG 2 , synthesized and secreted functional complement proteins C1r , C1s , C 2 , C 3 , C 4 , C 5 , factor B , C 1 inhibitor , C3b inactivator , a small amount of C 6 , and trace amounts of C 8 ; but failed to produce detectable C1q , C 7 , or C 9 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Kinetics of the reaction between human C 1 esterase inhibitor and C1r or C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The first component of human complement ( C 1 ) was reconstituted from equimolar concentrations of its purified subunits C1q , C1r , and C1s , in the presence of each of nine different metal ions for the purpose of studying the qualitative and quantitative nature of the metal ion requirement for C 1 assembly and function . ^^^ For C 1 reconstituted with each metal ion , three assays characteristic of C 1 were performed as follows : ( 1 ) spontaneous C 1 activation in the absence of the regulatory protein C 1 inhibitor was assessed by sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis by simultaneously quantifying the specific proteolysis of the C1r and C1s subunits ; ( 2 ) C 1 activation induced by aggregated IgG in the presence of C 1 inhibitor was similarly analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis ; and ( 3 ) formation of 16 S macromolecular C 1 was determined in the analytical ultracentrifuge . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Incubation of HFf with highly purified C1r also resulted in activation of C1r as assessed directly using a synthetic substrate or indirectly by activation of C1s and consumption of C 2 . ^^^ However , incubation of HFf with highly purified C1s resulted in formation of activated C1s ( C1s ) but this was less efficient than HFf activation of C1r . ^^^ We therefore conclude that activation of C 1 in macromolecular C 1 is the result of HFf conversion of C1r to C1r ; activation of C1s then occurs primarily by C 1r and to a lesser degree by the direct action of HFf . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
When C1r and C1s were added , the binding of Fn to C1q was abolished ; removal of C1r and C1s restored Fn binding to C1q . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
No such fluorescence increase is observed during C1s activation by trace amounts of C1r . ^^^ The slight changes observed on activation are not restricted to C1r , as comparable results are obtained for proenzyme and activated C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Somewhat surprisingly , when the C1s sequence is compared with that of complement subcomponent C1r , the percentage difference ( 59 % ) is approximately the same as that found between the other mammalian serine proteinases ( 56 71 % ) . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Activation of the classical pathway was demonstrated in all patients by formation of complexes between C1r , C1s , and C 1 inactivator . ^^^ Large amounts of free C1q , not in complex with C1r and C1s , were demonstrated in the majority of patient sera . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
FUT 175 was found to inhibit , in an intense , specific and reversible way , the enzyme activities of trypsin , C1r , C1s , thrombin , kallikrein and plasmin with IC 50 values of the order of 10 ( 6 ) 10 ( 8 ) M . ^^^ FUT 175 also inhibited complement mediated hemolysis , including both classical and alternative pathways , sites of inhibition being on C1r and C1s as evidenced by the intermediate cell technique . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The antibody independent interaction with C 1 occurs via C1q , which binds to LPS and possibly also via another C 1 subcomponent , C1r and / or C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Evidently this protein , which binds to antigen antibody complexes and to C1r and C1s , thereby forming a physical link between the immune and complement systems , has been highly conserved in evolution . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
These findings can be explained by using recent findings concerning the association dissociation equilibrium between C1q and the tetrameric complex of C1r and C1s . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Human C1r has no affinity for the virus nor does guinea pig C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
In their sera , C1q like material was found , whereas C1r and C1s were normal or increased in concentration , as were the other complement components tested . ^^^ It did not bind to C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The turnover numbers of C 2 and C 4 cleavage by C1s were affected to different extents , depending on whether C1s was alone or associated with C1r or with monoclonal antibodies to C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Using these assays , we show that C1q serum levels are significantly increased in rheumatoid arthritis ( RA ) and that the excess C1q levels in this disease are not accompanied by increased levels of C1r and C1s . ^^^ Active RA is therefore characterized by increased levels of hemolytically active C1q that has a physiologically active stem region unbound to C1r and C1s . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
By electroimmunoassay , complement components were quantitated in serum ( C1q , C1r , C1s , C 1 IA , C 2 , P , D . 1 , H , C 6 and C 7 ) or in EDTA plasma ( C 4 , C 3 , B , C 5 . and C ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Also appraised for each method was the ability of the labeled molecules to bind to antibody sensitized cells and to interact with C1r and C1s to form C 1 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Radial double immunodiffusion experiments using antiserum to C1q , C1r , and C1s on HFf treated serum demonstrated the dissociation of the C 1 trimolecular complex , with concomitant reduction of C1r antigenicity that is indicative of C 1 activation . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Immunochemical and functional analysis of a complete C1q deficiency in man : evidence that C1r and C1s are in the native form , and that they reassociate with purified C1q to form macromolecular C 1 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
From SDS PAGE analysis of the self activated C 1 , all the C1r and C1s subcomponents are converted to the activated split products , indicating that all C 1 molecules are biologically active . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The binding of fibronectin to C1q could be inhibited by the restoration of C1r + C1s to the C 1 macromolecular complex before the addition of fibronectin . ^^^ The inhibition was dependent on the concentration of C1r + C1s and achieved a maximum of 70 % at 100 micrograms / ml . ^^^ This inhibition could be reversed by the removal of C1r and C1s subunits with EDTA or C 1 inhibitor . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Several serum proteins were identified in the purified IC : IgG , IgA , IgM , C1q , C1r , C1s , C3bi and Bb . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Assembly of subcomponents C1r and C1s of first component of complement : electron microscopic and ultracentrifugal studies . ^^^ Monomeric C1s ( Mr , 85 , 000 ; s 20 , w , 4 . 3S ) , a subcomponent of first component of complement ( C 1 ) , the dimer ( Mr , 170 , 000 ; s 20 , w , 6 . 7 S ) of C1r , another subcomponent , and the tetrameric complex ( C1r , C1s ) 2 ( Mr , 340 , 000 ; s 20 , w , 8 . 7 S ) are elongated molecules . ^^^ Hydrodynamic equivalents of cylindrical shape have a diameter of 3 . 3 nm and lengths of 20 nm for C1s , 36 nm for ( C1r ) 2 , and 64 nm for ( C1r , C1s ) 2 . ^^^ In electron micrographs the C1r , C1s complex appears as a chain composed of six to eight globular domains with a contour length of 51 nm . ^^^ A structure is proposed in which ( C1r ) 2 forms a core to which C1s protomers are associated at both ends . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Immunochemical quantitation of C components in both sera showed depressed levels of C1q , whereas the levels of C1r , C1s , and C 1 inhibitor were elevated . ^^^ Furthermore , the C1q of both siblings was unable to interact with immunoglobulins or to associate with C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The first component of complement ( C 1 ) is a macromolecule consisting of three distinct subcomponents , C1q , C1r , and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1q binding appears to be mediated via the collagenous portion of the molecule in that 1 ) type 1 collagen inhibits this binding ; 2 ) C 1 reconstituted from purified C1q , C1r , and C1s does not bind to mononuclear cells , whereas the same amount of free C1q binds avidly ; and 3 ) C1q enhances the binding of aggregated IgG to mononuclear cells . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The rate of activation of C 1 has been studied by following the extent of hydrolysis of the C1r and C1s subcomponents , using a purified preparation of C 1 labelled with 125I . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
A study on the structure and interactions of the C 1 sub components C1r and C1s in the fluid phase . 1 . ^^^ It appears likely that the two monomers of C1r interact through their A chain and that the A and B chains are relatively independent from each other . 2 . 125I labelling of C1s in the presence of lactoperoxidase confirmed the calcium dependent dimerization of this subcomponent . ^^^ C1r dimer and C1s monomer were found to interact in the absence of calcium to form a C1r2 C1s complex ( 7 . 7 S ) , whereas in the presence of calcium the two sub components were associated into a C1r2 C1s2 complex ( 8 . 7S ) . ^^^ It appears likely that the formation of this tetrameric complex involves both calcium dependent , and calcium independent binding forces , and that C1r and C1s interact through their respective A chain which , in the case of C1s , is hidden upon association . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
We report that amnion tissue explants and amnion derived epithelial cells synthesize and secrete six proteins of the complement system , C1r , C1s , C 1 inhibitor , factor B , C 3 , and factor H . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Using hemolytic assays , we were able to demonstrate that C1qR prevents the association of C1q with C1r and C1s to form macromolecular C 1 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
To analyze the synovial site and the cell types expressing C1q , C1r / C1s , and C 1 esterase inhibitor ( C1INH ) and to characterize newly synthesized C1q in patients with rheumatoid arthritis ( RA ) . ^^^ Complement components C1q , C1r / C1s , and C1INH in rheumatoid arthritis . ^^^ Tissue and primary cell cultures of synovium from RA patients were analyzed for C1q , C1r / C1s , and C1INH by Northern blotting , in situ hybridization , and pulse chase experiments for C1q . ^^^ The de novo synthesis of C1q , C1r / C1s , and C1INH in synovium and primary cell cultures was proven by Northern blot and by antigenic and functional analysis . ^^^ The synovium is important for the synthesis and secretion of C1q and C1r / C1s , as well as the control protein C1INH , which supports the idea of a locally occurring inflammatory process in RA patients . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
These include a region of similarity to astacin , a crayfish metalloprotease , five copies of a repeat first found in complement proteins C1r and C1s , and two copies of an epidermal growth factor like sequence . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
This similarity extends to the serine protease component , which shares a similar modular construction and about 40 % sequence identity with the C1r and C1s subcomponents of C 1 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The other half complexed with C1s but showed little complex formation with C1r . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Identical binding of C1s , C1r , kallikrein , and beta factor XIIa was observed with the three molecules . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Northern blot and dot blot analysis showed that the mRNAs for all classical pathway complement components ( C1qA chain , C1qB chain , C1qC chain , C1r , C1s , C 4 and C 2 ) and the fluid phase regulatory components ( C 1 inhibitor , C 4 bp and factor 1 ) were present in all three types of synovial membrane . ^^^ Monocytes secreted C1q , C1r , C1s , C 4 , C 2 , C 1 inhibitor and C 4 bp but not factor 1 . ^^^ Fibroblasts secreted C1r , C1s , C 2 , C 3 , C 1 inhibitor and factor 1 but not C1q , C 4 or C 4 bp . ^^^ HUVEC secreted C1s , C 2 , C 1 inhibitor and factor 1 but not C1q , C1r , C 4 or C 4 bp . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Non coordinated biosynthesis of early complement components in a deficiency of complement proteins C1r and C1s . ^^^ We report on a 60 year old woman with systemic lupus erythematosus and a total ( 95 % ) C1r and a partial ( 36 % ) C1s deficiency . ^^^ Indeed C1r component was below the limits of detection whereas C1s component was lowered ( 36 % ) . ^^^ Biosynthesis of C1r and C1s by patient ' s monocytes was spontaneously normal but not up regulated by interferon gamma for C1r alone , whereas the biosynthesis of C1s , but also of interleukin 6 , was increased , indicating a specific disregulation of C1r . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
In comparison to the baseline , the mean values for C1q , C1r , C 2 , C 5 , C 6 , C 7 , C 8 , C 9 , FB , C1INH , C4BP , FH and FI exhibited a 3 5 fold increase , C 3 , total C 4 , albumin and the alpha 1 globulin fraction a 6 9 fold increase , and C1s , C4A , C4B , FB and alpha 2 , beta and gamma globulins a 10 20 fold increase . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The concept of this research is to construct deletion , point and hybrid mutants of the highly homologous C1r and C1s subcomponents , to reveal the functional role of individual modules , map the interaction sites between subcomponents of the C 1 complex and refine the structural model of C 1 . ^^^ Autographa californica nuclear polyhedrosis virus was used as vector to express human C1r and C1s in Spodoptera frugiperda cell culture and in lepidopteran larvae . ^^^ It is clear now , that this post translational modification does not play a role in the Ca2+ dependent C1r C1s interaction . ^^^ This observation indicates that the function of the C1s alpha part in the hybrid is modulated by the C1r part ( gamma B ) of the molecule . ^^^ The C1Rs hybrid behaves like C1r , providing haemolytically active C 1 with C1q and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Electroimmunoassays showed that lipoteichoic acid separately , yielded detectable amounts of free C1r2s2 subunits ; it also generated significantly more trimer complexes between C1r , C1s and C 1 inhibitor ( C1INH ) than did the other two activators . ^^^ Lipoteichoic acid was , however , a comparatively weak inducer of tetramer C1INH C1r C1s C1INH complexes . ^^^ Analysis through Western blotting showed that all activators accelerated consumption of C1r , induced complex formations between C1INH and C1s and produced cleavage products of C 2 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The activation of human C 1 , a Ca ( 2+ ) dependent complex proteinase comprising a non enzymic protein , C1q , and two serine proteinases , C1r and C1s , is based primarily on the intrinsic property of C1r to autoactivate . ^^^ Complete stabilization of C1r in its proenzyme form was obtained upon incorporation within the Ca ( 2+ ) dependent C1s C1r C1r C1s tetramer , and a comparable effect was observed when C1s was replaced by its Ca ( 2+ ) binding alpha fragment . ^^^ Both tetramers , C1s C1r C1r C1s and C1s alpha C1r C1r C1s alpha , readily associated with C1q to form 16 . 0 S and 14 . 7 S complexes respectively in which C1r fully recovered its activation potential . ^^^ Both complexes showed indistinguishable activation kinetics , indicating that the gamma B catalytic region of C1s plays no role in the mechanism that triggers C1r activation in C 1 . ^^^ The collagen like fragments of C1q retained the ability to bind to C1s C1r C1r C1s , but , in contrast with intact C1q , failed to induce C1r activation in the resulting complex at temperatures above 25 degrees C . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The amino terminal heavy chain contains domains that are homologous to segments of the low density lipoprotein receptor , complement components C1r and C1s , the macrophage scavenger receptor , and a recently described motif shared by the metalloprotease meprin and the Xenopus A 5 neuronal recognition protein . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Ca ( 2+ ) linked association of human complement C1s and C1r . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The zygotic dorsal ventral patterning gene tolloid ( tld ) exhibits a complex structure consisting of an N terminal domain with sequence similarity to the astacin family of metalloproteases and a C terminal domain composed of two EGF like repeats and five copies of the CUB repeat which was first found in human complement proteins C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
A 100 kDa protein in the C 4 activating component of Ra reactive factor is a new serine protease having module organization similar to C1r and C1s . ^^^ Although homology in the amino acid sequence of P 100 with that of human C1r and C1s subcomponents of C was less than 40 % , a striking similarity in domain organization was found among these proteins , indicating that P 100 is a new C 4 activating serine protease structurally similar to C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
All molecules in C 1 inhibitor purified from affected members ' plasma bind to activated C1s ( C 1 s ) , but approximately 50 % of molecules in these preparations do not bind to activated C1r ( C1r ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Like huBMP 1 it also contains an N terminal metalloendoprotease domain that shares sequence similarity with the astacin protease from crayfish , a C terminal domain that is similar to the repeat domain found in C1r or C1s serine proteases , and an EGF like segment . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 , the first component of complement : structure function relationship of C1q and collectins ( MBP , SP A , SP D , conglutinin ) , C 1 esterases ( C1r and C1s ) , and C 1 inhibitor in health and disease . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Protein engineering studies on C1r and C1s . 1 . ^^^ C1r and C1s cDNAs were placed downstream the strong polyhedrin promoter in the Autographa californica nuclear polyhedrosis virus and the recombinant proteins were expressed in insect cells , in biologically active form . ^^^ It is clear now , that this post translational modification does not play a role in the Ca2+ dependent C1r C1s interaction . 3 . ^^^ This observation indicates that the function of the C1s alpha part in the hybrid is modulated by the C1r part ( gamma B ) of the molecule . 5 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 esterase inhibitor is a M ( r ) approximately 105 , 000 glycoprotein and the sole regulation of the activities of C1r and C1s . ^^^ C 1 esterase inhibitor is a M ( r ) approximately 105 , 000 glycoprotein and the sole regulation of the activities of C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The catalytic subunit , C1s C1r C1r C1s , is a Ca ( 2+ ) dependent tetrameric association of two serine protease zymogens , C1r and C1s , that are sequentially activated by cleavage of a single peptide bond , upon binding of C 1 to activators . ^^^ The catalytic ( gamma B ) regions of C1r and C1s are respectively located in the centre and at each end of the isolated tetramer , and the Ca ( 2+ ) dependent C1r C1s associations are mediated by the interaction ( alpha ) regions , which contain one Ca2+ binding site each . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
We have investigated the synthesis of C1q , C1r , C1s and C 1 inhibitor in HepG 2 cells , human umbilical vein endothelial cells ( HUVEC ) , fibroblasts ( skin and synovial membrane ) , chondrocytes and monocytes . ^^^ C1r , C1s and C 1 inhibitor were synthesised by all cell types . ^^^ The secretion rates of C1r and C1s were approximately equimolar in fibroblasts and chondrocytes whereas the secretion rate for C1s exceeded that for C1r in the other cell types . ^^^ Molar ratios of C1s to C1r were approximately 2 : 1 for HepG 2 cells , 5 : 1 for monocytes and 10 : 1 for HUVEC . ^^^ The C1s : C1r ratio did not alter in chondrocytes or fibroblasts , but approached unity in HepG 2 , monocytes and HUVEC , due to relatively greater stimulation of C1r gene expression . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Progress in determining module structures in C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The sequences of nine serine proteinases of known crystal structure were compared with the serine proteinase sequences in the six complement proteins C1r , C1s , C 2 , factor B , factor 1 and factor D to assess the degree of structural homology of the latter with the crystal structures . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
In this paper we demonstrate the synthesis of the components of the classical complement pathway , namely C1q , C1r , C1s , C 1 Inh , C 2 , C 4 , and C 5 , by human glioma cell lines ( U118MG , T 193 , and T98G ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
This protein exhibits 87 . 4 % amino acid homology with mouse P 100 , and 36 . 4 % and 37 . 1 % homologies with that of the C1r and C1s subcomponents of human complement , respectively . ^^^ The characteristic nodules and domain of C1r and C1s were highly conserved in this protein . ^^^ This indicates that the P 100 , together with the C1r and C1s , forms a unique protein family having the same module / domain constitution . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Human complement serine proteases C1r and C1s and their proenzymes . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Genetic deficiency of one of the early components of the classical pathway of complement ( C1q , C1r , C1s , C 4 and C 2 ) is often associated with clinical symptoms and immunochemical abnormalities common in idiopathic autoimmune diseases , such as lupus erythematosus , but also with an increased incidence of various , local and generalized infections . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
It was observed that incubation of isolated NIA with fresh normal human serum resulted in the formation of sodium dodecyl sulfate ( SDS ) irreversible complexes of activated C1r C 1 inhibitor and activated C1s C 1 inhibitor and in activated C1s mediated C 4 conversion . ^^^ Preincubation of NIA with C1q , blocked NIA mediated C1r and C1s activation and C 4 conversion . ^^^ The concn of NIA required to activate C1r and C1s was similar to that of heat aggregated human IgG . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The full sequence was found to have characteristics of a serine protease and exhibited 29 % and 30 % homologies with those of light chains of the C1r and C1s subcomponents of complement , respectively . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
By developing 6 amidino 2 naphthyl 4 guanidinobenzoate ( 1 , FUT 175 ) as a basic structure , its various derivatives were synthesized and their inhibitory activities on trypsin , plasmin , kallikrein , thrombin , C1r and C1s as well as on complement mediated hemolysis were examined . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 inh antigenic levels were normal in all patients ; however , the function of the C 1 inh tested against C1s and C1r was variable and outside the normal functional range in seven of the eight patients . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Of the 22 complement proteins examined , 13 bound heparin ( C1q , C 2 , C 4 , C4bp , C1INH , B , D , H , P , C 6 , C 8 , C 9 , and vitronectin ) while 9 did not bind heparin ( C1r , C1s , C 3 , Factor 1 , C 5 , C 7 , C3b , Ba and Bb ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 inhibitor is a serine proteinase inhibitor that is active against C1s , C1r , kallikrein , and factor 12 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Using metabolic labeling with [ 35S ] methionine , immunoprecipitation , and SDS PAGE , we demonstrated that HEp 2 cells synthesized C1r , C1s , C 1 inhibitor , C 3 , C 4 , factor B , and factor H . ^^^ The constitutive synthesis of C1r and C1s were the highest among these proteins , whereas the synthesis of C 4 was observed only when the cells were stimulated with IFN gamma . ^^^ C1r and C1s were secreted readily , whereas the rate of the secretion of C 4 and C 1 inhibitor was much slower . ^^^ Activated forms of C1r , C1s , and complexes of C 1 inhibitor C1s were found . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1qBP , when bound to C1q , prevents the assembly with C1r and C1s to form a functional C 1 complex . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Immunohistochemically , C 1 esterase inhibitor ( C 1 Inh ) and the C 1 subcomponents C1s and C1r can not , or only occasionally , be detected in plaques or in astrocytes . ^^^ The present finding that C1q , C1s and C 1 Inh mRNA are present in both AD and control brains suggests that the variable immunohistochemical staining results for C1r , C1s and C 1 Inh are due to a rapid consumption , and that the inability to detect C1s , C1r or C 1 Inh is probably due to the dissociation of C1s C 1 Inh and C1r C 1 Inh complexes from the activator bound C1q into the fluid phase . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Analysis of the reactivity of this recombinant protein with target proteases demonstrated no complex formation with C1s , C1r , or kallikrein . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Articular chondrocytes cultured in vitro synthesized C1r , C1s , C 4 , C 2 , C 3 and C 1 inhibitor but not C1q , C 4 binding protein or factor 1 , as assessed by enzyme linked immunosorbent assay ( ELISA ) and Northern blot analysis . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Exon structure of the gene encoding the human mannose binding protein associated serine protease light chain : comparison with complement C1r and C1s genes . ^^^ In this study , we analyzed MASP genomic clones and found that the light chain ( catalytic domain ) is encoded by six exons , whereas those of the complement C 1 subunits , C1r and C1s , and the haptoglobin segment have been reported to be encoded by a single exon . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Serum samples were obtained at that time and tested for total complement activity ( CH 100 ) and antigenic levels of C1q , C1r , C1s , C 3 and C 4 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
By interaction of CSPG with solid phase bound C1q , formation of the C 1 complex upon the addition of C1r and C1s was impaired . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
MBL is structurally related to the complement C 1 subcomponent , C1q , and seems to activate the complement system through an associated serine protease known as MASP ( ref . 4 ) or p 100 ( ref . 5 ) , which is similar to C1r and C1s of the classical pathway . ^^^ We have now identified a new MBL associated serine protease ( MASP 2 ) which shows a striking homology with the previously reported MASP ( MASP 1 ) and the two C1q associated serine proteases C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r is one of the two serine proteases of C 1 , the first component of complement , in which it is associated in a calcium dependent manner to the homologous serine protease C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Surprisingly , neither clone is related to Bf / C2 but rather share the same domain structure of mammalian C1r / C1s / MASP ( mannan binding protein associated serine protease ) , and are more related evolutionarily to mammalian MASP than to mammalian C1r or C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
A dysfunctional C 1 inhibitor ( C 1 INH ) from a family in whom the propositus presented with systemic lupus erythematosus but without angioedema previously was shown to have diminished inhibitory activity toward isolated C1r and C1s , and intact C 1 . ^^^ However , the mutant with Asp at this position is unable to bind C1r and beta factor XIIa , and also has a decreased rate of reaction with C1s and kallikrein . ^^^ Although defective in inhibition of C1r and C1s , the P 2 A > 5 mutant had acquired the ability to complex with trypsin . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Using biosynthetic labelling , immunoprecipitation and sodium dodecyl sulfate polyacrylamide gel electrophoresis , we demonstrated that GECs synthesized C1r , C1s , C 1 inhibitor , C 3 , C 2 and factor B . ^^^ Both factor B and C 3 proteins were increased following addition of either IL 1beta , IL 6 or TNF alpha to GEC cultures ; however , these cytokines did not increase either C 2 , C1r , C1s or C 1 inhibitor biosynthesis . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
We used an enzyme linked immunosorbent assay to measure plasma levels of three multimolecular complement activation protein ( CAP ) complexes : C1r : C1s : C 1 inhibitor , C3bP and C5b 9 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Occurrence of the classical pathway complement proteins C1q , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 6 , C 7 , C 8 and C 9 was studied in human hippocampus and temporal cortex by immunohistochemistry and Western blotting . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
When added to solutions of the C1r2C1s2 tetramer , HI 532 converted the 8 . 7 S tetramer into an 18 S complex , which was seen by electron microscopy to be a dimer of parallel C1s 10 C1r 10 C1r 10 C1s molecules cross linked by two bivalent monoclonal antibodies . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
A neoepitope based enzyme immunoassay for quantification of C 1 inhibitor in complex with C1r and C1s . ^^^ A previously produced and characterized mouse MoAb , recognizing a neoepitope on the human plasma protein C 1 inhibitor complexed with its substrates , was used to design an enzyme immunoassay for detection of C 1 inhibitor complexed with C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
All recombinant fragments were expressed in a proenzyme form and cleaved by C1r to generate active enzymes expressing esterolytic activity and reactivity toward C 1 inhibitor comparable to those of intact C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Human myoblasts in vitro produced C1q , C1r , C1s , C 2 and C 4 constitutively and all syntheses were upregulated after stimulation with IFN gamma . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The calcium dependent interaction between C1r and C1s , the two homologous serine proteases of the first component of human complement C 1 , is mediated by their N terminal regions . ^^^ Due to its Ca2+ binding ability , the C1r EGF like module ( C1r EGF ) is supposed to participate in the C1r C1s interaction . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
MBL can activate C 4 , C 2 , and later acting complement components in the presence of serine proteases similar to but distinct from C1r and C1s via the lectin pathway of complement activation . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
MASP , C1r and C1s belong to the same family of serine proteases . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
For this purpose , the serum levels of the serum complement proteins C1q , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 6 , C 7 , C 8 , C 9 , Factor B and properdin were repeatedly evaluated by means of radial immunodiffusion assay in 26 CLL patients over a period of 2 years . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
When C1s alpha ( 159 ) 2 was mixed with the 6 . 8 S C1r2 in Ca2+ , a 7 . 5 S complex was formed , presumably the C1s alpha ( 159 ) 10 C1r 10 C1r 10 C1s alpha ( 159 ) tetramer . ^^^ This suggested that the presence of the 159 amino acid C1s alpha domain , which held the C1r to the C1q , was sufficient to permit activation by an immune complex , even though the catalytic domains of C1s were not present . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
These proteins include the complement proteases C1r , C1s and MASPs , the Limulus clotting factor C , and the proteins of the haptoglobin family . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The accuracies of the police report ( PR ) , the emergency department record ( EDR ) , and the ambulance report ( AR ) for each patient were compared with the CIR by computing percent agreement , with 95 % confidence intervals ( 95 % CIs ) for each variable and for each data source . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
In human heart , we detected mRNAs and proteins for C1q , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 6 , C 7 , C 8 , and C 9 with the use of reverse transcriptase polymerase chain reaction , Western blotting , and immunohistochemical techniques . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Structural and functional studies on C1r and C1s : new insights into the mechanisms involved in C 1 activity and assembly . ^^^ C1r and C1s , the enzymes responsible for the activation and proteolytic activity of the C 1 complex of complement , are modular serine proteases featuring similar overall structural organizations , yet expressing very distinct functional properties within C 1 . ^^^ This review will initially summarize available information on the structure and function of the protein modules and serine protease domains of C1r and C1s . ^^^ It will then focus on the regions of both proteases involved in : ( 1 ) assembly of C1s C1r C1r C1s , the Ca ( 2+ ) dependent tetrameric catalytic subunit of C 1 ; ( 2 ) expression of C 1 catalytic activities . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Our protein engineering studies on human C1r and C1s revealed important characteristics of the individual domains of these multidomain serine proteases , and supplied evidence about the cooperation of the domains to create binding sites , and to control the activation process . ^^^ Deletions and point mutants of C1r were constructed and C1r C1s chimeras were also produced . ^^^ Our deletion mutants demonstrated that the N terminal CUB domain and the EGF like domain of C1r together are responsible for the calcium dependent C1r C1s interaction . ^^^ The substrate specificity of the serine protease is also determined by the five N terminal noncatalytic domain of C1r / C1s chimera , which contains the catalytic domain of C1s preceded by the N terminal region of C1r , could replace the C1r in the hemolytically active C 1 complex . ^^^ The C1s / C1r chimera , in which the alpha fragment of the C1r was replaced for that of the C1s exibits both C1r and C1s like characteristics . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
These two proteases , MASP 1 and MASP 2 , are structurally similar to one another as well as to C1r and C1s . ^^^ Together , MASP , C1r and C1s constitute a novel serine protease family . ^^^ Based on the analysis of MASP cDNA of vertebrates and ascidians , the MASP / C1r / C1s family can be classified into two groups . ^^^ The second group includes human MASP 2 , Xenopus MASP 2 , carp MASP , shark MASP , C1r and C1s . ^^^ The TCN type of MASP may have emerged prior to the AGY type as an ancestral protease of the MASP / C1r / C1s family and played a crucial role in cleaving C3 . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The two MASPs share the domain organisation of C1r and C1s and it may be speculated that interaction between the two MASPs is required for complement activation in the same manner as with the C 1 proteases . ^^^ Phylogenetic analysis indicates that MASP 2 is closer to C1r and C1s than is MASP 1 , but no particular association between MASP 2 and the C 4 cleaving enzyme , C1s , can be deduced from sequence comparison . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Besides binding of HNP 1 to C1q , also a limited binding to C 1 and to a mixture of C1r and C1s was observed , whereas no binding to C 1 inhibitor was found . ^^^ Because binding of HNP 1 to C 1 inhibitor has been suggested in earlier studies , we also assessed the binding of HNP 1 to mixtures of C 1 inhibitor with either C1r / C1s or C 1 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 , the first component of the classical pathway of complement activation is a complex of three proteins called C1q , C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Deficiencies of the first complement components , C1r / C1s , often cause systemic lupus erythematosus like syndromes and severe pyogenic infections . ^^^ Up to now no genetic analysis of the C1r / C1s deficiencies has been carried out . ^^^ In the present work , we report the first genetic analysis of selective C1s deficiency , the patient having a normal amount of C1r . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The classical C activation pathway was reconstituted from the proteins C1q , C1r , C1s , C 4 , C 2 , C 3 , factor H , and factor 1 ; each were purified to homogeneity . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Analysis of the cDNA reveals three sequence motifs : a carboxyl terminal region with similarity to the trypsin like serine proteases , four tandem cysteine rich repeats homologous to the low density lipoprotein receptor , and two copies of tandem repeats originally found in the complement subcomponents C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The ratio of AD to control mRNAs in these four areas was 1 . 17 for C 1 inh and 1 . 12 for CD 59 , compared to 3 . 06 for C1r , 2 . 67 for C1s , 2 . 35 for C 5 , 2 . 56 for C 6 , 2 . 42 for C 7 , 5 . 08 for C 8 and 16 . 3 for C 9 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Structure and functions of the interaction domains of C1r and C1s : keystones of the architecture of the C 1 complex . ^^^ C1r and C1s , the proteases responsible for activation and proteolytic activity of the C 1 complex of complement , share similar overall structural organizations featuring five nonenzymic protein modules ( two CUB modules surrounding a single EGF module , and a pair of CCP modules ) followed by a serine protease domain . ^^^ These properties include the ability to bind Ca2+ ions with high affinity , to associate with each other within a Ca2+ dependent C1s C1r C1r C1s tetramer , and to interact with C1q upon C 1 assembly . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Mannan binding lectin ( MBL ) is an acute phase protein which activates the classical complement pathway at the level of C 4 and C 2 via two novel serine proteases homologous to C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
P 100 activates the C 4 component of the complement system and its domain organization is similar to C1r and C1s . ^^^ Its non protease region consisted of 10 exons , as in the case of C1r and C1s , and the introns were found present in the boundary separating two CUB domains , an EGF like domain and two CCP domains and each CUB and CCP domain contained extra internal introns . ^^^ The serine protease region was comprised of 6 exons in contrast to C1r and C1s , either of which consists of a single exon . ^^^ The exon intron structure was found to reflect the evolution of these molecules and P 100 to have derived earlier in the stage of evolution than C1r or C1s . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
We used reverse transcriptase polymerase chain reaction and Western blotting techniques to measure the levels of complement mRNAs and their protein products in Alzheimer ' s disease ( AD ) brain compared with non AD brain . mRNAs for C1q , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 6 , C 7 , C 8 , and C 9 were detected in the 11 regions of brain that were investigated . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
MASP 1 and MASP 2 are composed of modular structural motifs similar to those of the C1q associated serine proteases C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 inhibitor is the main inhibitor of the classical pathway of the complement system ( C1s and C1r ) , of the contact activation system ( factor XIIa and kallikrein ) and of the intrinsic pathway of coagulation ( factor XIa ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r and C1s were secreted at low levels by astrocytes and neuroblastoma cell lines . ^^^ Exposure of cells to IL 1 alpha , IL 1 beta , TNF alpha and to a far lesser extent IL 6 , markedly upregulated C1r , C1s , and C 3 production . ^^^ Thus , C 1 Inh production is refractory to stimulation by plaque associated cytokines , whereas these cytokines do stimulate C1r , C1s , and also C 4 and C 3 secretion by astrocytes and neuronal cells in culture . ^^^ In contrast to the amyloid plaque associated cytokines IL 1 beta , IL 1 alpha , and TNF alpha , the amyloid peptide A beta 1 42 itself did not stimulate C1r and C1s synthesis by astrocytes , microglial cells , or neuroblastoma cell lines . ^^^ The ability of C1q to reassociate with newly formed C1r and C1s upon activation of C 1 and subsequent inactivation by C 1 Inh , may enable ongoing complement activation at sites of amyloid deposition , especially when C 1 Inh is consumed and not replaced . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
It was shown that the C3a receptor C1r and C1s genes form an unexpected complement gene cluster towards the telomeric end of chromosome 6 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
RESULTS : FUT 175 inhibited C1r and C1s with IC50s of 1 . 7x10 ( 6 ) and 3 . 2x10 ( 7 ) M , respectively . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Interaction of C1q and mannan binding lectin ( MBL ) with C1r , C1s , MBL associated serine proteases 1 and 2 , and the MBL associated protein MAp 19 . ^^^ The proteases C1r and C1s were initially discovered in a complex with C1q , whereas the MBL associated serine proteases 1 and 2 ( MASP 1 and 2 ) were discovered in a complex with MBL . ^^^ There is controversy as to whether MBL can utilize C1r and C1s or , inversely , whether C1q can utilize MASP 1 and 2 . ^^^ In serum , C1r and C1s were found to be associated only with C1q , whereas MASP 1 , MASP 2 , and a third protein , MAp 19 ( 19 kDa MBL associated protein ) , were found to be associated only with MBL . ^^^ The interactions of MASP 1 , MASP 2 , and MAp 19 with MBL differ from those of C1r and C1s with C1q in that both high salt concentrations and calcium chelation ( EDTA ) are required to fully dissociate the MASPs or MAp 19 from MBL . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Cerebral endothelial cells and HUVEC expressed detectable levels of complement gene mRNAs for the C1q B chain , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 7 , C 8 gamma subunit and C 9 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
By binding directly to carbohydrates on the surfaces of potential microbial pathogens , MBP and MBP associated serine proteases ( MASPs ) can replace antibodies and complement components C1q , C1r , and C1s of the classical complement pathway . ^^^ The biophysical properties of the truncated MASPs indicate that the interactions with MBP leading to complement activation differ significantly from those between components C1q , C1r , and C1s of the classical pathway . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Structural similarities shared by MBL and C 1 complexes and by the MBL and C1q associated serine proteases , MBL associated serine protease ( MASP ) 1 and MASP 2 , and C1r and C1s , respectively , have led to the expectation that the pathways of complement activation by MBL and C 1 complexes are likely to be very similar . ^^^ We have expressed rMASP 2 and show that , whereas C 1 complex autoactivation proceeds via a two step mechanism requiring proteolytic activation of both C1r and C1s , reconstitution with MASP 2 alone is sufficient for complement activation by MBL . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 inhibitor ( C 1 INH ) , an inhibitor for C1r and C1s , formed equimolar complexes with MASP 1 and MASP 2 and inhibited their proteolytic activities . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Sequencing of the high pressure liquid chromatography purified peptides yielded the complement components C1r and C1s . ^^^ To confirm that C1r / C1s accounted for the proteolytic activity in the medium , immunoaffinity chromatography was performed . ^^^ Amino acid sequencing confirmed that the 88 kDa band contained only C1r and C1s . ^^^ C1r in the fibroblast medium underwent autoactivation , and the activated form cleaved C1s . ^^^ In summary , human fibroblasts secrete C1r and C1s that actively cleave IGFBP 5 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The complement serine proteases include the closely related C1r , C1s , MASPs 1 3 ( 80 90 kDa ) , C 2 and Factor B ( 100 kDa ) , Factor D ( 25 kDa ) and Factor 1 ( 85 kDa ) . ^^^ The C1r , C1s and MASP group occur as proenzymes . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The cleavage of two C1s subunits by a single active C1r reveals substantial flexibility of the C1s C1r C1r C1s tetramer in the C 1 complex . ^^^ The activation of the C1s C1r C1r C1s tetramer in the C 1 complex , which involves the cleavage of an Arg Ile bond in the catalytic domains of the subcomponents , is a two step process . ^^^ First , the autolytic activation of C1r takes place , then activated C1r cleaves zymogen C1s . ^^^ This mutant was used to form a C1q ( C1s C1rQI C1r C1s ) heteropentamer to study the relative position of the C1r and C1s subunits in the C 1 complex . ^^^ After triggering the C 1 by IgG Sepharose , both C1s subunits are cleaved by the single proteolytically active C1r subunit in the C1s C1rQI C1r C1s tetramer . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Taken together with previous findings , these and other data strongly support the hypothesis that MASP 2 is the protease that , in association with MBL , triggers complement activation via the MBL pathway , through combined self activation and proteolytic properties devoted to C1r and C1s in the C 1 complex . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Activated C1r then cleaves and activates zymogen C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Using C 1 reconstituted from purified C1q , C1r , and C1s , it was shown that Abeta 1 42 fibrils trigger direct C 1 activation both in the absence of C 1 inhibitor and at C 1 inhibitor : C 1 ratios up to 8 : 0 , i . e . , under conditions consistent with the physiological context in serum . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Molecular cloning of the complement ( C1r / C1s / MASP2 like serine proteases from the common carp ( Cyprinus carpio ) . ^^^ C 1 is a Ca2+ dependent complex of C1q , C1r , and C1s , and analogous to an initiation complex of the lectin pathway of complement , which consists of the mannose binding lectin ( MBL ) homologous to C1q and the MBL associated serine proteases ( MASPs ) homologous to C1r and C1s . ^^^ Thus divergence of Clq and MBL and that of C1r , C1s and the MASPs are considered to be crucial events in the establishment and evolution of the classical complement pathway . ^^^ Here we describe two distinct C1r / C1s / MASP2 like cDNA clones ( C1r / s A , C1r / s B ) isolated from the common carp ( Cyprinus carpio ) . ^^^ They share 83 % identity at the amino acid level and have a domain structure similar to that of C1r / C1s / MASPs from other species . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
This patient ' s complement profile was characterized by the absence of CH 50 activity , C 1 functional activity < 10 % , and undetectable levels of C1s Ag associated with normal levels of C1r and C1q Ags . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The classical pathway of complement is initiated by the C 1 complex , a multimolecular protease comprising a recognition subunit ( C1q ) and two modular serine proteases ( C1r and C1s ) associated as a Ca2+ dependent tetramer ( C1s C1r C1r C1s ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The genes for the classical complement activation pathway proteases , C1r and C1s , are linked on chromosome 12p13 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r and its activated fragments all cleaved C1s , with relative efficiencies in the order C1r < CCP1 / 2 SP < CCP 2 SP , indicating that CCP 1 is not involved in C1s recognition . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
However , in plaques , the mRNAs for C1r and C1s , the substrates for the C 1 inhibitor , were increased 2 . 35 and 4 . 96 fold , respectively , compared with normal artery ; mRNA for C 4 , the target for C4BP , was elevated l . 34 fold ; and mRNAs for C 7 and C 8 , the targets for CD 59 , were elevated 2 . 61 and 3 . 25 fold , respectively . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Reactivity of the inhibitors toward target ( C1s , C1r , kallikrein , beta factor XIIa , and plasmin ) and nontarget proteases ( alpha thrombin and trypsin ) were studied . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 , the first protein of the classical pathway of complement activation , is a calcium dependent complex of one molecule of C1q and two molecules each of C1r and C1s , the serine proteases that cleave complement proteins . ^^^ Upon binding of C1q to Ag bound IgG or IgM , C1r and C1s are sequentially activated and initiate the classical pathway of complement . ^^^ Further investigation revealed that the binding of SP A to C1q prevents the association of C1q with C1r and C1s , and therefore the formation of the active C 1 complex required for classical pathway activation . ^^^ This finding suggests that SP A may share a common binding site for C1r and C1s or Clq . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
B 7 alphaCEA was also found to strongly enhance survival and tumor specific activation of T cells expressing an anti CEA TCRzeta based chimeric immune receptor ( CIR ) both when expressed in cis by the T cells themselves as well as in trans , when added to the culture medium . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Each complex has a recognition subunit ( C1q in the classical and mannose binding lectin ( MBL ) in the lectin pathway ) , which associates with serine protease zymogens ( C1q with C1r and C1s , and MBL with MBL associated serine proteases : MASP 1 , MASP 2 ) to form the C 1 and MBL MASPs complexes , respectively . ^^^ Special emphasis will be laid on the serine proteases : the role of the individual domains in the assembly of the C1s C1r C1r C1s tetramer and in the control of the protease activity will be discussed . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r , the enzyme responsible for intrinsic activation of the C 1 complex of complement , is a modular serine protease featuring an overall structural organization homologous to those of C1s and the mannan binding lectin associated serine proteases ( MASPs ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The MASPs show identical domain structure , shared also with C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Initially it was thought likely that the MBL + MASPs system would resemble very closely the C 1 complex of the complement classical pathway , and that MASP 1 and MASP 2 would have similar activities to their classical pathway homologues C1r and C1s . ^^^ MASP 2 does certainly have similar activities to C1s , but MASP 1 does not have the activities of either C1r or C1s . ^^^ MASP 1 and MASP 2 appear not to have such a narrow specificity as C1r and C1s , and may have significant substrates other than complement proteins . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
This 790 , 000 Da complex is formed from the association of a recognition protein , C1q , and a catalytic subunit , the Ca2+ dependent tetramer C1s C1r C1r C1s comprising two copies of each of the modular proteases C1r and C1s . ^^^ Early studies mainly based on biochemical analysis and electron microscopy of C 1 and its isolated components have allowed for characterization of their domain structure and led to a low resolution model of the C 1 complex in which the elongated C1s C1r C1r C1s tetramer folds into a more compact , `` 8 shaped ' ' conformation upon interaction with C1q . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Complement C1r and C1s genes are duplicated in the mouse : differential expression generates alternative isomorphs in the liver and in the male reproductive system . ^^^ C1r and C1s are the serine proteases that form the catalytic unit of the C 1 complex , the first component of complement . ^^^ In the present study , we found that the genes encoding murine C1r and C1s are duplicated . ^^^ One set of these genes , referred to as c1rA and c1sA , are primarily expressed in the liver and are therefore the homologues of the human C1r and C1s genes . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1r and C1s are highly specific serine proteases that initiate the classical pathway of complement activation . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Moreover , within the range of concentrations studied , the studied inhibitors did not affect the subsequent C1q binding to the C1r and C1s enzymes . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
RT PCR analysis showed that the oligodendroglial cells expressed detectable levels of complement mRNAs for the C1q B chain , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 6 , C 7 , C 8 gamma subunit , and C 9 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Because the IGFBP 5 protease activity that is secreted by fibroblasts has been shown to be due to the complement components C1r and C1s , these studies were undertaken to determine whether smooth muscle cells also secreted these proteases and to identify some of the factors that regulate their secretion by both cell types . ^^^ Both smooth muscle cells and human fibroblasts were shown to release C1r and C1s into conditioned medium . ^^^ Both C1r and C1s were detected as activated forms , as determined by SDS PAGE using reducing conditions . ^^^ The addition of increasing concentrations of either IL 1beta or TNFalpha resulted in increased synthesis of C1s by fibroblasts and smooth muscle cells , and they each increased C1r release . ^^^ In contrast dexamethasone ( 10 ( 7 ) M ) had no effect on C1s release and stimulated C1r release only by smooth muscle cells . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
This pathway is triggered by C 1 , a multimolecular protease formed from the association of a recognition protein , C1q , and a catalytic subunit , the calcium dependent tetramer C1s C1r C1r C1s , which comprises two copies of each of the modular proteases C1r and C1s . ^^^ All activators of the pathway are recognized by the C1q moiety of C 1 , a process that generates a conformational signal that triggers self activation of C1r , which in turn activates C1s , the enzyme that mediates specific cleavage of C 4 and C 2 , the C 1 substrates . ^^^ Early work based on biochemical and electron microscopy studies has allowed characterization of the domain structure of the C 1 subcomponents and led to a low resolution model of the complex in which the elongated C1s C1r C1r C1s tetramer folds into a compact , figure of 8 shaped conformation upon interaction with C1q . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
In addition , mRNAs for C1r , C1s , C 2 , C 3 , C 4 , C 5 and C 6 were also detected in T98G cells , but very low amount of mRNAs for C1q and MBL . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The trout translation shows highest homology with carp C1r / s , and lower , equal homologies to mammalian C1r and C1s , and MASPs from other vertebrate species . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Expression of C1q ( but not IL1beta , TNFalpha or Egr 1 ) remains high after BBB function is restored , and is accompanied by late up regulation of the C1q associated serine proteases , C1r and C1s , suggesting that microglial biosynthesis of the activation complex of the classical pathway may support the removal of cell debris by activation of complement . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The classical complement pathway , which plays a vital role in preventing infection , is initiated by the action of the serine proteases C1r and C1s . ^^^ When C1s was in complex with C1q and C1r , as would occur under physiological conditions , the same behavior was observed , indicating that this mechanism is relevant in the complement pathway in vivo . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Binding causes activation of a series of serine protease proenzymes , such as C1r , C1s and MASP 2 ( MBL associated serine protease 2 ) , which in turn activate the atypical serine proteases factor B and C 2 , which then activate the major opsonin of the system , C 3 . ^^^ C1r , C1s and the MASPs , in contrast , are regulated more conventionally by the natural serpin , C 1 inhibitor . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C 1 , the complex that triggers the classical pathway of complement , is assembled from two modular proteases C1r and C1s and a recognition protein C1q . ^^^ The N terminal CUB 1 EGF segments of C1r and C1s are key elements of the C 1 architecture , because they mediate both Ca2+ dependent C1r C1s association and interaction with C1q . ^^^ The C1s structure was used to build a model of the C1r C1s CUB 1 EGF heterodimer , which in C 1 connects C1r to C1s and mediates interaction with C1q . ^^^ A structural model of the C1q / C1r / C1s interface is proposed , where the rod like collagen triple helix of C1q is accommodated into a groove along the transversal axis of the C1r C1s heterodimer . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
In addition , adipsin , which belongs to the alternative pathway , and the classical pathway components C1QB , C1R , and C1S were expressed in both depots . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
The MASPs are homologous to the C1q associated proteases , C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
In this study we investigated the exon intron organization of the human C1R gene , which spans 11 kb from the initiation codon to the stop codon , and is very similar in exon intron structure to the C1S gene . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Fucoidan binds C1q , likely to its collagen like region through interactions involving lysine residues , and then prevents the association of the C1r ( 2 ) C1s ( 2 ) subunit , required to form the fully active C 1 . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Regulation of complement system activation takes place through inactivation of the classical pathway proteases , C1r and C1s , the lectin pathway protease , MASP 2 , and perhaps via inhibition of alternative pathway activation by reversible binding to C3b . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
A novel human complement related protein , C1r like protease ( C1r LP ) , specifically cleaves pro C1s . ^^^ Recombinant C1r LP exhibits esterolytic activity against peptide thioesters with arginine at the P 1 position , but its catalytic efficiency ( kcat / K ( m ) ) is lower than that of C1r and C1s . ^^^ Most importantly , C1r LP also expresses proteolytic activity , cleaving pro C1s into two fragments of sizes identical with those of the two chains of active C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
RESULTS : Complement has been shown to possess approximately 31 proteins , some of which are enzymes ( C1r , C1s , C 2 , factor B , factor D ) , some cofactors , some inhibitors or inactivators , and others composed of membrane integrated proteins . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
It was showed by ELISA that several compounds studied interact with C1q , C1r / C1s components of complement . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Specificities of 13 serine proteases ( activated protein C , plasma kallikrein , factor VIIa , factor IXabeta , factor XIa and factor alpha XIIa , activated complement C1s , C1r , and D , tryptase , trypsin , subtilisin Carlsberg , and cathepsin G ) and 11 papain like cysteine proteases ( cathepsin B , H , K , L , S , and 5 , rhodesain , papain , chymopapain , ficin , and stem bromelain ) were obtained from 103 , 968 separate microarray fluorogenic reactions ( 722 substrates 10 24 different proteases 10 6 replicates ) . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
None of the mutations significantly altered C1s ability to assemble with C1r and C1q within C 1 . ^^^ Whereas the other mutations had no effect on C1s activation , the Q340E mutant was totally resistant to C1r mediated activation , both in the fluid phase and within the C 1 complex . ^^^ Thus , flexibility of the C1s CCP 1 CCP2 linker plays no significant role in C 1 assembly or C1s activation by C1r inside C 1 but plays a critical role in C 4 cleavage by adjusting positioning of this substrate for optimal cleavage by the C1s active site . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
PURPOSE OF REVIEW : Hereditary angioedema is an autosomal dominant deficiency of C 1 inhibitor a serpin inhibitor of kallikrein , C1r , C1s , factor 12 , and plasmin . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Whereas C1s ( MASP 2 SP ) was recovered as an active enzyme , C1s ( MASP 2 CCP1 / 2 ) was produced in a proenzyme form and was susceptible to activation by C1r , indicating that the activation properties of the chimeras were dictated by the nature of their SP domain . ^^^ Remarkably , C1s ( MASP 2 CCP1 / 2 ) retained C1s ability to associate with C1r and C1q to form a pseudo C 1 complex and to undergo activation within this complex , indicating that the C1s CCP modules have no direct implication in either function . . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Besides its catalytic protease domain , the procollagen C proteinase contains several C terminal CUB modules ( named after complement factors C1r and C1s , the sea urchin UEGF protein , and BMP 1 ) and EGF like domains . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
Genes induced by IFNs ( GBP 1 , GBP 2 , C1S , C1R , MHC2TA , PSMB 8 , TAP 1 , TAP 2 ) showed increased expression during porcine lung infection . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
C1q is the first subcomponent of the classical complement pathway that binds antigen bound IgG or IgM and initiates complement activation via association of serine proteases C1r and C1s . ^^^
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P00736 and P09871	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.51600385
Single chain C1s proenzyme was activated to two chain C1s with self activated C1r . 0.51600385^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.58474979
In order to define the boundaries of the C1r domain ( s ) responsible for Ca2+ binding and Ca2+ dependent interaction with C1s and to assess the contribution of individual modules to these functions , the CUB , EGF , and CUB EGF fragments were expressed in eucaryotic systems or synthesized chemically . 0.58474979^^^ These data demonstrate that the C1r CUB EGF module pair ( residues 1 175 ) is the minimal segment required for high affinity Ca2+ binding and Ca2+ dependent interaction with C1s and indicate that Ca2+ binding induces a more compact folding of the CUB EGF pair . . 0.57446553^^^ Ca2+ dependent interaction of intact C1r with C1s was studied using surface plasmon resonance spectroscopy , yielding KD values of 10 . 9 29 . 7 nM . 0.50213176^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Synthetic inhibitors of trypsin , plasmin , kallikrein , thrombin , C1r , and C 1 esterase . p Carbethoxyphenyl episol guanidinocaproate and p ( p ' guanidinobenzoyloxy ) phenyl derivatives were prepared , and their inhibitory effects on trypsin , plasmin , plasma kallikrein , thrombin , C1r and C 1 esterase were examined . ^^^ Among the various inhibitors tested , p nitrophenyl p ' guanidinobenzoate , N , N dimethylamino p ( p ' guanidinobenzoyloxy ) benzoyl glycolate and N , N dimethylamino p ( p ' guanidinobenzoyloxy ) benzilcarbonyloxy glycolate were the most effective inhibitors of trypsin , plasmin , plasma kallikrien and thrombin , and they strongly inhibited the esterolytic activities of C1r and C 1 esterase . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
However , the peptide esterase inhibitors Trasylol , hirudin , leupeptin , and C 1 esterase inhibitor had no effect on the esterase activity of C1r . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The role of C 1 esterase inhibitor in the activation of C1r , a subcomponent of the first component of complement from human plasma . ^^^ On thecolumn , the C 1 esterase inhibitor activity was found to coincide with Clr but not C1s ( another subcomponent of the first component ) C1r was isolated from the euglobulin fraction of human serum by DEAE cellulose column chromatograph . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
To evaluate the involvement of the complement system in atherogenesis , we investigated the effect of camostat mesilate ( CM ) , C1r , and C 1 esterase inhibitor on cholesterol induced atherosclerosis in rabbits . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Trimer and tetramer complexes containing C 1 esterase inhibitor , C1r and C1s , in serum and synovial fluid of patients with rheumatic disease . ^^^ During activation , the first component of complement C1q ( C1r C1s ) 2 is dissociated in conjunction with the formation of complexes containing C 1 esterase inhibitor ( C 1 INH ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
New synthetic inhibitors of C1r , C 1 esterase , thrombin , plasmin , kallikrein and trypsin . p Guanidinobenzoate derivates were prepared and their inhibitory effects on trypsin , plasmin , pancreatic kallikrein , plasma kallikrein , thrombin , C1r and C 1 esterase were examined . ^^^ Among the various inhibitors tested , 6 ' amidino 2 naphthyl 4 guanidinobenzoate dihydrochloride , 4 ( beta amidinoethenyl ) phenyl 4 guanidinobenzoate dimethanesulfonate and 4 amidino 2 benzoylphenyl 4 guanidinobenzoate dimethanesulfonate were the most effective inhibitors of trypsin , plasmin , pancreatic kallikrein . plasma kallikrein and thrombin and they strongly inhibited the esterolytic activities of C1r and C 1 esterase , and then strongly inhibited complement mediated hemolysis . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Kinetics of the reaction between human C 1 esterase inhibitor and C1r or C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
To analyze the synovial site and the cell types expressing C1q , C1r / C1s , and C 1 esterase inhibitor ( C1INH ) and to characterize newly synthesized C1q in patients with rheumatoid arthritis ( RA ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 esterase inhibitor is a M ( r ) approximately 105 , 000 glycoprotein and the sole regulation of the activities of C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Immunohistochemically , C 1 esterase inhibitor ( C 1 Inh ) and the C 1 subcomponents C1s and C1r can not , or only occasionally , be detected in plaques or in astrocytes . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r and C1s were disproportionally high compared with the C1q levels . ^^^ Furthermore , crossed immunoelectrophoresis revealed abnormal complexes composed of C1r and C1s , and complexes composed of C1r , C1s and C 1 IA . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Binding of C 1 via C1q in this manner leads to activation of C1r , C1s , and thus of the classical C pathway . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
All of the C1q , C1r , and C1s detected in normal serum was found to be in the C 1 complex . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Analysis of C components immunochemically demonstrated a marked reduction of C1q and C1s inhibitor , undetectable C1r , C1s and an elevated B . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Formation of complexes composed of C1r , C1s , and C 1 inactivator in human serum on activation of C 1 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Studies have been performed with platelets using C 1 haemolytic assays and platelet aggregation induced by anti C1q , anti C1s and aggregated IgG in the presence of C 1 subcomponents C1q , C1r and C1s . ^^^ The addition of C1q restored the reactivity of the platelets to aggregated IgG while the addition of C1r or C1s was without effect . ^^^ Furthermore , the addition of C1r or C1s to C1q inhibited the action of C1q in platelet aggregation induced by IgG . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Proenzymic C1s associated with catalytic amounts of C1r . ^^^ Proenzymic C1s isolated from human plasma by euglobulin precipitation and DEAE cellulose chromatography is associated with trace amounts of C1r ( 0 . 5 1 % on a molar basis ) . ^^^ From the kinetic experiments and from the inhibition characteristics , the activation of C1s can be attributed to the presence of C1r , which appears to undergo activation and then to activate secondarily C1s . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Hemolytic titrations of C 1 , C 4 , C 2 , C 3 , and C 5 showed a complete inhibition of C 4 , C 2 and C 3 , and a partial inhibition of C 1 ( C1q , C1r , C1s , Ca++ ) and C 5 , by this drug . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The peptic fragment blocked the reconstitution of C 1 haemolytic activity by competing with intact subcomponent C1q in the utilization of a mixture of the other two subcomponents , C1r and C1s . 4 . ^^^ The peptic fragment was unable to block efficiently the reconstitution of C 1 haemolytic activity unless it was added to the mixture of subcomponents C1r and C1s before the attempt to reconstitute C 1 haemolytic activity , in solution , or on the surface of antibody coated erythrocytes . 7 . ^^^ Evidence was obtained that suggested that subcomponent C1q bound the subcomponent C1r C1s complex more efficiently when the subcomponent C1q was bound to antibody than when it was free in solution . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The inability of C 1 to induce particle agglutination might be caused by the C 1 subunits C1r and C1s sterically inhibiting the subunit C1q to bridge between the particles . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The C1r was found to reconstitute C 1 complex when it reacted with rabbit C1q and C1s in the presence of Ca2+ , since C1s was able to bind to C1q bound on sensitized sheep erythrocytes only in the presence of C1r . ^^^ This result indicates that a part of the H chain of C1s not contributing to the structural integrity of an active site may be involved in the binding of C1s to C1r . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The inhibitor binds rapidly to subcomponent C1s , and more slowly to subcomponent C1r . ^^^ Formation of the C1r C 1 inhibitor complex causes rapid dissociation of subcomponents C1r and C1s from the antibody antigen component C 1 aggregate . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The isolated complexes were shown to contain antigen , antibody , C1q , C1r , C1s and C 3 . ^^^ The isolated material was found to contain IgM , IgG , C1q , C1r , C1s , C3c and C3d . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Activation can be achieved by incubation with human C1r , resulting in cleavage of the C1s chain into two chains of 65000 and 27000 mol . wt . and the generation of an isoleucine N terminal residue on the smaller chain . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The role of C1s , C1r and properdin in the initiation of the C3b dependent feedback mechanism of the complement system . ^^^ The influence of activated C1s , C1r and properdin in the fluid phase initiation of the C3b dependent feedback mechanism of the human complement was studied . ^^^ When a normal serum was incubated with C1r before incubation with C1s , only C 3 was converted , whereas factor B remained in the unaltered native state . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Epithelial and mesenchymal cells synthesized and secreted all three subcomponents of the first component of complement ( C 1 ) : C1q , C1r , and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Modulation of the antigenicity of C1r and C1s by C 1 inactivator . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r and C1s associated with a lupus erythematosus like disease . ^^^ Complete absence of C1r and almost complete absence of C1s were found in 4 of 8 living siblings . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The activation of subcomponents C1r and C1s in the first component of complement , C 1 , when bound to antibody antigen complexes was investigated . ^^^ Activation was followed both by the splitting of the peptide chains of subcomponents C1r and C1s and by the development of proteolytic activity . ^^^ For the maximum rate of activation to occur , all components must be present in approximate molar proportions of antibody : C1q : C1r : C1s of 13 : 1 : 5 : 5 . ^^^ For activation of subcomponent C1s , subcomponents C1r or C1r , but not C1r inactivated with iPr2P F ( di isopropyl phosphorofluorideate ) , are effective . ^^^ For activation of subcomponent C1r , subcomponents C1s , C1s or C1s inactivated with iPr2P F are effective . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Interaction of C 1 inhibitor with the C1r and C1s subcomponents in human C 1 . 1 . ^^^ C 1 inhibitor bound to both subcomponents ( C1r and C1s in C 1 and formed stable complexes of respective apparent molecular weights 197 , 000 and 185 , 000 , as determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis . ^^^ The binding reaction proceeded more readily with C1s than with C1r and was correlated with the inhibition of C1s esterase activity . 3 . ^^^ At physiological ionic strength , binding of C 1 inhibitor to subcomponents C1r and C1s caused release of these subcomponents from the C 1 immune aggregates complex , indicating that C 1 inhibitor binding decreased the inter subcomponent binding forces in C 1 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Fractionation of C 1 by DEAE Cellulose chromatography under the conditions that led to the original identification of C1q , C1r , and C1s resulted in recovery of 2 P 2 in the fractions containing C1r . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Affinity chromatography of serum on Sepharose tryptophan modified IgG resulted in the binding of only C1r and C1s . ^^^ By the use of purified C 1 proteins and Sepharose IgG in binding studies it was confirmed that both C1q and C1r bind independently to sites on IgG and hold C1s and C1t by Ca++ dependent bonds . ^^^ Both C1t and C1r independently enhanced the C 1 activity of C1q C1s mixtures ; maximal activity required all four subcomponents . ^^^ The evidence suggests that the spatial sequence of the components of the Sepharose IgG Serum C 1 complex is : Sepharose IgG : C1q : C1t : C1s : C1r : IgG Sepharose . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r had a high affinity for active C1s or proenzyme C1s in the presence of calcium and was able to activate C1s and to form C 1 in conjunction with C1q and C1s . ^^^ Activation of C1s by C1r was inhibited by calcium , C 1 inactivator , polyanethol sulfonate , and DFP . ^^^ Activation of C1s by C1r occurred only after a preliminary incubation of C1r for a brief time at 37 degrees C before addition of C1s . ^^^ The ability of C1r to form C 1 in conjunction with C1q and C1s was , however , progressively lost on incubation at 37 degrees C . ^^^ The binding of 125I C1r to sensitized sheep erythrocytes required the presence of C1q and calcium but not C1s , whereas the binding of 125I C1s required C1q , C1r and calcium . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Studies have been performed with platelets using C 1 haemolytic assays and platelet aggregation induced by anti C1q , anti C1s and aggregated IgG in the presence of C 1 subcomponents C1q , C1r and C1s . ^^^ Furthermore , the addition of C1r or C1s to C1q inhibited the action of C1q in platelet aggregation induced by IgG . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Highly purified subcomponents C1q , C1r and C1s were recovered at DEAE Sephadex chromatography from such purified C 1 material after EDTA treatment . ^^^ Tests on isolated C1q , C1r and C1s disclosed in addition to the well known interaction between heparin and C1q an equally strong or even stronger interaction between heparin and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The substrate profile of D was dinstinct when compared to that of CIs , CIr , plasmin , urokinase , and trypsin . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1q , C1r , C1s , C 3 , C 4 and C 1 IA were determined by electroimmunoassay in sera from 150 patients with chronic urticaria or angioedema . ^^^ Sera from 11 % of the patients contained C1r C1s complexes . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Interaction with complement subcomponents C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
In the case of proenzymic C1s , di isopropyl phosphorofluoridate ( 0 . 5 5 mM ) is added at all stages of the purification procedure , which includes euglobulin precipation followed by DEAE cellulose chromatography and affinity chromatography on anti C1r IgG Sepharose 6B . ^^^ The final step completely removes contaminant traces of C1r and / or C1r , ensuring that the final preparation of C1s is stable in the proenzyme form and suitable for activation studies . 2 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 was reconstituted in macromolecular proenzyme , nonactivated form by incubation of highly purified C1q , C1r , and 125I C1s together in the presence of calcium . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
We describe a 46 year old women with a seven year history of urticarial like symptoms and cutaneous vasculitis with marked deficiency of C1q in the presence of normal levels of C1r and C1s and high titers of low molecular weight ( 7S ) C1q precipitins . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r and C1s were recovered in the proenzyme form and their identity was established by SDS polyacrylamide gel electrophoresis before and after reduction and alkylation , and on the basis of their esterolytic activities toward different substrates . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The structure and enzymic activities of the C1r and C1s subcomponents of C 1 , the first component of human serum complement . ^^^ The subcomponents C1r and C1s and their activated forms C 1r and C 1s were each found to have mol . wts . in dissociating solvents of about 83000 . ^^^ The amino acid compositions of each were similar , but there were significant differences in the monosaccharide analyses of subcomponents C1r and C1s , whether activated or not . ^^^ Subcomponents C1r and C1s have only one polypeptide chain , but subcomponents C 1r and C 1s each contain two peptide chains of approx . mol . wts . 56000 ( `` a ' ' chain ) and 27000 ( `` b ' ' chain ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Isolation and comparison of the proenzyme and activated forms of the human serum complement subcomponents C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
These results suggest that , in the case of rabbit C1s , the primary product of activation with C1r , C1s ( 1 ) , may be susceptible to further cleavage of its H chain without any loss of C1s activity , resulting in the formation of C1s ( 2 ) , though the active principle responsible for this conversion remains to be elucidated . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r was unable to cleave and activate proenzyme C1s unless first incubated at 37 degrees C in the absence of calcium before the addition of C1s . ^^^ Thus , C1r is converted from an inactive form into an enzyme , C1r , able to cleave and activate C1s by proteolytic cleavage in marked analogy to the activation of several other complement enzymes . ^^^ In other studies , cleavage of C1r was not accelerated by the addition of C1r ot C1s . ^^^ Proteolytic cleavage of the C1r molecule was found to occur on addition of aggregated IgG to a mixture of C1q , C1r , and C1s in the presence of calcium . ^^^ Neither C1q , C1s nor aggregated IgG alone , not C1r nor C1s induced C1r cleavage . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The protein contains several domains : a signal peptide , a putative propeptide , a catalytic domain with an active center typical of a Zn ( 2+ ) metalloprotease , an EGF like domain and two internal repeats similar to repeated domains found in the C1s and C1r serine proteases of the complement cascade . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The unactivated subcomponents were also isolated , and evidence is given that the three subcomponents C1q , C1r and C1s account wholly for the activity of component C 1 in serum . ^^^ The approximate molar proportions of the subcomponents in serum are C1q / C1r / C1s = 1 : 2 : 2 . ^^^ Optimum activity by haemolytic assay was found at approximate molar proportions C1q / C1r / C1s of 1 : 4 : 4 . ^^^ No activity was found when subcomponents were assayed singly or in pairs , except for subcomponents C1q and C1s , which in molar ratio 1 : 4 gave 15 20 % of the activity of the mixture C1q + C1r + C1s . ^^^ Subcomponents C1q + C1r + C1s and C1q + C1s in the presence of antibody antigen aggregates were activated and inactivated simultaneously , showing a peak of activity and subsequent loss of activity . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r values were well correlated to the levels of C1q ( r = 0 . 708 ) and of C1s ( r = 0 . 768 ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The alpha 2 peak was a complex composed of C 1 IA , C1s and C1r proteins . ^^^ The molecular species in the beta 1 region was shown to be a calcium dependent complex of C1r and C1s , probably in proenzyme form . the C1r C1s complex formed macromolecular C 1 on addition of purified C1q to serum . ^^^ During electrophoresis activation of C 1 subcomponents was initiated by a mechanism involving CIr with generation of CIs activity in eluted fractions corresponding to the position of macromolecular C 1 as well as in the beta region . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Based on analyses of molecular size , antigenicity , and 11 NH 2 terminal amino acid sequences of the L chain , we conclude that MASP is a novel protein different from C1r or C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 inhibitor ( C1I ) , a member of the serine protease inhibitor superfamily , is the principal regulator of the activation classical pathway of complement by reducing the proteolytic activity of activated C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The use of the method is illustrated on distantly related domains shared by complement components C1S and C1R , calcium dependent serine proteinase and bone morphogenetic protein 1 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Apart from cleaving C1s , we demonstrate for the first time that : 1 ) at concentrations found in serum , the activated forms of the complement components C1r in addition to C1s can cleave the heavy chain of MHC class 1 antigens , 2 ) the cleavage by C1r and C1s is seemingly dependent upon a native configuration of the MHC class 1 antigen , since heat denaturation of the HLA antigens reduce the cleavage . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r is a Ca ( 2+ ) binding serine protease that interacts with two other plasma proteins , C1q and C1s , to form C 1 , the first component of the complement cascade . ^^^ The antibody reacts with native and heat denatured C1r , and with zymogen C1r , but does not cross react with C1s or C1q . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Factor H was shown to complex with intact C 1 , to isolated C1q and to the C1r : C1s tetramer . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Recombinant human complement subcomponent C1s lacking beta hydroxyasparagine , sialic acid , and one of its two carbohydrate chains still reassembles with C1q and C1r to form a functional C 1 complex . ^^^ Furthermore , the mutated protein displays good hemolytic activity when reassembled with C1q and either human serum or recombinant C1r , demonstrating that these posttranslational modifications are not critical for any of the multiple interactions between C1s and C1q , C1r , C 2 , and C 4 required for reassembly of the C 1 complex , activation , and initiation of the classical complement pathway . ^^^ The 4 . 0S recombinant C1s dimerizes to yield 5 . 6S C1s2 in the presence of Ca2+ and forms the 9 . 1S C1s C1r C1r C1s tetramer upon the addition of human serum C1r and the 15 . 6S C 1 complex upon the addition of C1q to the tetramer . ^^^ The recombinant C1s is secreted and isolated as the unactivated zymogen , and it may be activated by human serum C1r which cleaves at Arg 422 Ile423 to yield the characteristic heavy and light chains . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Interestingly , patients with evidence of HUVS fairly consistently had zymogen ( C1r C1s ) 2 complexes in their serum , while patients with SLE showed high concentrations of complexes containing Cl inhibitor , C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Inhibition of complement proteins D , B , C 2 , C1s , C1r , 1 , and the catalytic fragments Bb and C2a by substituted isocoumarins was investigated . 3 , 4 Dichloroisocoumarin , a general serine protease inhibitor , inhibited factor D , C1r , and C1s moderately with second order inhibition constants ( kobs / [ 1 ] ) of 40 to 190 M 1 s 1 , but it did not inhibit C 2 , factor B , C2a , or Bb . ^^^ Most isocoumarins did not inhibit C 2 or C2a ; only 4 chloro 3 isothiureidoalkoxyisocoumarins were slightly inhibitory . 3 Alkoxy 4 chloro 7 guanidinoisocoumarins inhibited C1r and C1s moderately . ^^^ The best inhibitor for C1r and C1s was 4 chloro 3 ( 3 isothiureidopropoxy ) isocoumarin with kobs / [ 1 ] values of 6 , 600 and 130 , 000 M 1 s 1 , respectively . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Mouse MHC class 1 antigen specific determinants could also be detected in supernatant from mouse spleen cells incubated with C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r and C1s , the serine protease components of activated C 1 , form a tetramer in the presence of Ca2+ . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Virions activated the C 1 complex , reconstituted from C1q , proenzyme C1r , and 125I labeled proenzyme C1s , to an extent comparable with that obtained with immunoglobulin G ovalbumin immune complexes . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Analysis of a tld cDNA reveals three sequence motifs : an N terminal region of similarity to a metalloprotease , two EGF like repeats , and five copies of a repeat found in human complement proteins C1r and C1s . tld sequence is 41 % identical to human bone morphogenetic protein 1 ( BMP 1 ) ; the closest members to dpp within the TGF beta superfamily are BMP 2 and BMP 4 , two other bone morphogenetic proteins . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
At the time of acute edema the complement profile was typical : virtual absence of C 1 INH function was associated with diminished concentrations of the components of the classical pathway of complement ( C1q , C1r , C1s , C 2 , C 4 ) and reduced complement hemolytic activity ( CH 50 ) . ^^^ Although there was only a minor adjustment to the therapy , the C1q , C 2 , C 4 and CH 50 values gradually increased to levels close to the lower limit of the normal range , while C1r and C1s showed normal values . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Human IgG immobilized on the polyacrylate support was used for isolation of the first complement component from human serum and for its separation into subcomponents C1r , C1s and C1q by a one step method . ^^^ The stepwise elution of C1r , C1s and C1q from the column reflects the course of C 1 breakdown after its activation on immune complex formation . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Measurement of macromolecular interactions between complement subcomponents C1q , C1r , C1s , and immunoglobulin IgM by sedimentation analysis using the analytical ultracentrifuge . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
All of the disulfide bonds of the earlier described substructures of C1s , the EGF homologous part , the two SCR units , and the two domains typical for C1s and C1r are localized within these domains . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Complement components C1r / C1s , bone morphogenic protein 1 and Xenopus laevis developmentally regulated protein UVS . 2 share common repeats . ^^^ Property patterns were constructed , based on an alignment of related domains in human complement subcomponents C1r and C1s as well as in the sea urchin protein uEGF . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
We studied the activation and C 1 inactivator dependent dissociation of the first component of complement , the C1q ( C1r C1s ) 2 complex , in relation to recruitment of the classical activation pathway in the circulation of 24 patients with systemic lupus erythematosus ( SLE ) . ^^^ High serum concentrations of trimer complexes containing C 1 inactivator , activated C1r and zymogen C1s ( C 1 IA C1r C1s ) were found in the majority of the patients . ^^^ Some patients with high C 1 IA C1r C1s concentrations showed no evidence of classical pathway activation , indicating that C 1 activation was controlled by the action of C 1 IA at the C1r level . ^^^ By contrast , formation in serum of tetramer complexes in which C 1 IA was firmly bound to both C1r and C1s ( C 1 IA C1r C1s C 1 IA ) was associated with C 2 and C 3 cleavage in EDTA plasma , and with manifest hypocomplementemia . ^^^ Low C 1 IA C1r C1s C 1 IA values were observed in conjunction with substantial C 2 cleavage in a few patients . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The specificity of the IL 4 effect was also apparent when comparing the effect of IL 4 on the TNF induced synthesis of factor B to the effects on total protein synthesis ( increased 1 . 5 fold ) and the TNF induced increases in synthesis in C1r , C1s , C 1 inhibitor , C 2 , and factor H ( no changes ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Isolation of human complement subcomponents C1r and C1s in their unactivated , proenzyme forms . ^^^ We have modified a standard isolation procedure for C1r and C1s , which employs IgG Sepharose affinity chromatography followed by DEAE chromatography . ^^^ In addition , purification was improved by washing the IgG Sepharose column with a buffer free of added divalent cations immediately prior to elution of the C1r and C1s with EDTA . ^^^ The final yields of highly purified C1r and C1s were about 20 % ; little or no activated material was detected in these highly purified fractions . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Both type 1 and type 2 fibroblasts synthesized normal amounts of C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The first repeat bears homology to domain 3 of complement components C1r and C1s , and the second repeat is homologous to the C 1 and C 2 domains of coagulation factors 5 and 8 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 inhibitor ( C1inh ) , a member of the serine protease inhibitor gene superfamily , is a glycosylated plasma protein inhibiting the proteolytic activities of C1r and C1s and involved in the regulation of coagulation , fibrinolysis and kinin releasing systems . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The specificity of this reaction was proved by the inhibitory effect of F ( ab ' ) 2 antibodies to C1q and by the inability of MPO to bind to C1r , C1s and IgG . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The specificity of this interaction was further substantiated by the finding that neither macromolecular C 1 , or subcomponents C1r and C1s , nor human or murine IgG nor IgM had any inhibitory activity when cultured with these cell lines . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The binding of C1s to the cell bound S MBP require the presence of C1r , suggesting that C1r2s2 binds to S MBP through C1r . ^^^ The activation of C1s from a proenzyme to a protease was mediated by cell bound S MBP in the presence of C1r and the activated protease remained associated with the cells and was not released into the medium . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NH 2 terminal calcium binding domain of human complement C1s mediates the interaction of C1r with C1q . ^^^ The assembly of C 1 , the first component of human complement , involves interactions between various domains of each of its three subcomponents , C1q , C1r , and C1s . ^^^ The isolation , assignment of function , and structural characterization of the individual domains of C1r and C1s are critical for a thorough understanding of this complex assembly . ^^^ This fragment , C1s alpha , was shown in the presence of Ca2+ to mimic the ability of whole C1s to self associate , bind to C1r , and facilitate the binding of C1r to C1q . ^^^ These results directly prove that the Ca 2 ( + ) binding sites of C1s as well as all of the determinants necessary for binding of C1s to C1r and C1q are located in the NH 2 terminal 27 kDa alpha region of the A chain . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
In contrast , both alpha 2 and the N terminal alpha 1 fragment , starting at serine 24 of the A chain , were able to compete significantly with intact C1s for the formation of the Ca 2 ( + ) dependent C 1 s C1r C 1 r C 1 s tetramer . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Neutron scattering study of the ( gamma B ) catalytic domains of complement proteases activated C1r and C1s . ^^^ The catalytic domains of activated C1r and C1s , comprising the C terminal region of the A chain ( gamma ) , disulphide linked to the B chain , were obtained by limited proteolysis of the native proteases with chymotrypsin and plasmin , respectively , and studied by small angle neutron scattering . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
There was a discrepancy between the low C1q and the high C1r and C1s levels in blood . ^^^ Complexes of C1r C1s C 1 inactivator and factor B conversion products were found , especially in the peritoneal fluid , denoting an activation of the complement system . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
It enhances C1r and C1s biosynthesis at a pretranslational level . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The association between inherited deficiencies of the classical pathway complement components ( C1q , C1r , C1s , C 4 , C 2 and C 3 ) and immune complex disease shows that complement is involved in protection against the development of immune complex disease ( ICD ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
In vitro , C1q can be bound by immune complexes and induce activation of the proenzymes C1r and C1s , resulting in an activated C 1 molecule . ^^^ In the presence of C 1 In in the reaction mixture C1r and C1s are dissociated rapidly from the immune complex bound C1q . ^^^ This C1q has the possibility to interact with free precursor C1r and C1s to form a new C 1 molecule at the surface of the immune complex and induce a new cycle of activation . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Combined IgG 2 , IgG 4 and IgA deficiency : low C1q concentrations and the presence of excess C1r and C1s in an adult patient with recurrent pneumococcal infections . ^^^ However , the concentrations of circulating C1q were persistently decreased , and the sera contained an excess of C1r C1s complexes , resembling the C 1 aberrations previously found in children with recurrent acute otitis media . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Human genes for complement components C1r and C1s in a close tail to tail arrangement . ^^^ The amino acid sequence of C1s was 40 . 5 % identical to that of C1r , with excellent matches of tentative disulfide bond locations conserving the overall domain structure of C1r . ^^^ DNA blotting and sequencing analyses of genomic DNA and of an isolated genomic DNA clone clearly showed that the human genes for C1r and C1s are closely located in a `` tail to tail ' ' arrangement at a distance of about 9 . 5 kilobases . ^^^ Furthermore , RNA blot analyses showed that both C1r and C1s genes are primarily expressed in liver , whereas most other tissues expressed both C1r and C1s genes at much lower levels ( less than 10 % of that in liver ) . ^^^ Multiple molecular sizes of specific mRNAs were observed in the RNA blot analyses for both C1r and C1s , indicating that alternative RNA processing ( s ) , likely an alternative polyadenylylation , might take place for both genes . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
This report describes the different activation steps for C1q , C1r , C1s , C 4 and C 2 and summarizes monoclonal antibodies reported so far which recognize either conserved epitopes or activation dependent epitopes with particular emphasis on neoepitopes occurring during the activation cascade . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Proteins of the C 1 complex , C1q , C1r , and C1s , of the classical pathway of complement activation are known to be synthesized in human skin fibroblasts . ^^^ As previously reported , fibroblasts also synthesized C1r and C1s . ^^^ IFN gamma , IFN beta 1 , and TNF had significant , but distinct , effects on synthesis of C 1 inhibitor , C1r , and C1s . ^^^ Incubation of the cells with IFN gamma , 1000 U / ml , for 24 h induced increases in the synthesis of C 1 inhibitor , C1r , and C1s by 4 . 2 , 1 . 9 and 1 . 6 fold , respectively . ^^^ TNF , 12 . 5 ng / ml , induced increases in the synthesis of C 1 inhibitor , C1r , and C1s by 1 . 5 , 1 . 4 and 2 . 6 fold . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Although subcomponents C1r and C1s of the first complement component , C 1 , have been established to be in the same linkage group as the proline rich protein gene cluster on chromosome 12p13 . 2 , no direct analysis of linkage between the C1R and C1S structural gene loci has been available . ^^^ We have detected through a population screening study 5 families which are heterozygous at the structural loci for both C1R and C1S . ^^^ A maximum lod score of 1 . 505 at theta = 0 . 00 was found in a two point analysis between C1R and C1S . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The sequences of C1r and C1s show that each is constructed from six protein domains . ^^^ C1r and C1s are elongated macromolecules of lengths 18 20 nm . ^^^ This places each monomer of C1r and C1s on four adjacent arms of C1q , and offers the most reasonable explanation of the known properties of the C 1 complex . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Structure and function of C1r and C1s : current concepts . ^^^ C1r and C1s , the constituent proteins of C1s C1r C1r C1s , the Ca2+ dependent catalytic unit of C 1 , are homologous serine proteinases that share a common activation pattern and have similar structural organizations at the monomeric level . ^^^ Overall sequence comparison of C1r and C1s reveals 40 % amino acid identity and conservation of all cysteine residues . ^^^ In contrast , C1r and C1s widely differ from each other by their glycosylation patterns : both proteins contain Asn linked carbohydrates , but four glycosylation sites are present on C1r , and only two on C1s . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The structures of human C1r and C1s and their relationship to other serine proteases . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Biosynthesis of C1r and C1s subcomponents . ^^^ Biosynthesis of C1r and C1s subcomponents has been studied using monocytes and macrophages , hepatocytes and hepatoma cell lines or fibroblasts . ^^^ C1r and C1s were secreted by stimulated monocytes and by Hep G 2 cells , according to a 1 : 1 stoichiometry . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin . ^^^ While the protease regions of the serine zymogens are typically encoded by multiple exons , the protease domains of C1s and of its genetically linked and functionally interacting homolog C1r are encoded as intronless domains , not unlike a region of haptoglobin , which in fact is devoid of proteolytic activity . ^^^ Additional evidence of the common ancestry of C1r , C1s and haptoglobin is the presence , within the protease domain , of a set of sequence markers that distinguish these three proteins from all known serine proteases . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Previously two distinct models for its structure have been described , in which C1r2C1s2 is either a linear rod like assembly of the globular domains found in each of C1s and C1r , or these domains are arranged to form an asymmetric 10 shaped structure . ^^^ The data on C1s , C1s2 and C1r are readily represented by straight hydrodynamic cylinders , but not C1r2 or C1r2C1s2 . ^^^ The total length of the C1s and C1r monomers was determined as 17 20 nm , which is compatible with electron microscopy . ^^^ On the basis of the known sequences of C1r and C1s , this length is accounted for by a linear arrangement of a serine proteinase domain ( length 4 nm ) , two short consensus repeat domains ( 2 10 4 nm ) , and a globular entity containing the 1 , 2 and 3 domains ( 4 7 nm ) . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 reconstituted from purified C1r expressed in insect cells together with human C1q and C1s proved biologically active in a hemolytic assay . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 deficiency results from an absence or lowering of the level of one or more of the proteins C1q , C1r and C1s , which are the subcomponents of the C 1 complex of the classical pathway of the serum complement system . ^^^ Both acquired and genetic deficiencies of the C 1 subcomponents have been reported ; the possible genetic deficiencies appear quite rare , with only 14 reports of C1q deficiency ( involving 24 people ) and six reports of C1r / C1s deficiency ( involving 11 people ) appearing in the literature to date . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Human complement C1r and C1s proteins and genes : studies with molecular probes . ^^^ We review here recent advances in studies of the C1r and C1s proteins and of the corresponding genes , using molecular probes . ^^^ Surprisingly , the C1r and the C1s genes feature an intronless serine protease domain , at variance with all vertebrate serine proteases . ^^^ Moreover , C1r and C1s are related in evolution to haptoglobin , a serine protease analog lacking enzymic activity . ^^^ The C1r and C1s genes are closely linked in an unusual tail to tail orientation . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Despite structural similarities between MBP and the C1q subcomponent of the first complement component , MBP did not restore classical pathway activity to C1q deficient serum , nor did it activate C1s when added to a mixture of C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
It is the only inhibitor of C1r and C1s in plasma , and is responsible for about half of the kallikrein and the majority of plasma factor 12 inactivating activity . ^^^ C 1 INH inactivation of C1r and C1s within activated macromolecular C 1 results in dissociation of C 1 with release of complexes consisting of two molecules of C 1 INH and one molecule each of C1r and C1s . ^^^ C1q is thus allowed to interact with zymogen C1r and C1s or with C1q receptors . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 INH is the only plasma protease inhibitor of activated C1r and C1s , the serine protease subcomponents of the first complement component . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Recently , using 35S methionine incorporation and immunoprecipitation techniques our laboratory has demonstrated the ability of tissue cells , i . e . , the human lung type 2 pneumocyte ( A 549 ) and human lung fibroblast ( WI 38 ) , to synthesize and secrete a variety of early and terminal complement components , as well as several regulatory proteins in vitro , i . e . , C1r , C1s , C 4 , C 3 , C 5 , C 6 , C 7 , C 8 , C 9 , factor B , factor H , factor 1 , and C1s inactivator . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r , C1s , C1q , C 3 , C 4 , and C reactive protein ( CRP ) , where tested , were found in most but not all IC . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
A highly purified N terminal fragment generated by tryptic digestion of C1r in the presence of Ca2+ retained its ability to interact with C1s , disrupting the formation of C1s dimers in the presence of Ca2+ . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
We have studied a number of these and report the presence of erythro beta hydroxyasparagine ( e beta Hyn ) in three non vitamin K dependent proteins : the plasma complement proteins C1r and C1s ( where overbar indicates activated form ) and the urinary protein uromodulin . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
An affinity sorbent comprising macroporous glass coated with the polymer with the polymer with immobilized immunoglobulin IgG was used for the isolation from human serum of the first component of the complement and for its separation into subcomponents C1r , C1s and C1q by the one step procedure . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Diamines at concentrations which dissociate C 1 into C1q and ( C1r , C1s ) 2 , strongly inhibited the interaction of C1q or C1qCLF with LPS . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The first component of complement : the subcomponents of C1q , C1r , C1s , C 1 inhibitor , C1q receptors . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Spontaneous generation in human serum of a trimer complex containing C 1 inactivator , activated C1r , and zymogen C1s . ^^^ Activation of the C 1 complex in the presence of C 1 inactivator ( C 1 IA ) is known to result in the formation of tetramer C 1 IA C1r C1s C 1 IA complexes that are dissociated from C1q . ^^^ Both C1r and C1s of the tetramers are present in their activated forms . ^^^ The present investigation concerned the generation of trimer complexes containing C 1 IA , activated C1r , and zymogen C1s ( C 1 IA C1r C1s ) . ^^^ C 1 IA C1r C1s were released from C1q and were formed in high concentration during prolonged incubation ( 1 to 3 days ) of normal serum at 37 degrees C without addition of activators . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The effect of the antibody on haemolytic activity has shown that it is capable of inhibiting the formation of EAC 1 cells from EAC1q cells plus C1r and C1s but is incapable of inhibiting the C 1 activity of performed EAC 1 cells . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
A rapid and efficient method for the purification of the complement subcomponents C1r and C1s in zymogen form using fast protein chromatography . ^^^ The purification of the subcomponents C1r and C1s of the first component of complement involves multiple steps and is time consuming . ^^^ The method provides C1r and C1s in a yield of 35 and 60 % respectively . ^^^ In addition , this study provides a simple and sensitive test to assess functional purity of C1r and C1s with respect to the other C 1 subcomponents . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Assignment of the complement serine protease genes C1r and C1s to chromosome 12 region 12p13 . ^^^ C1r and C1s are distinct , but structurally and functionally similar , serine protease zymogens responsible for the enzymatic activity of the first component of complement ( C 1 ) . ^^^ Recent comparisons indicate a significant degree of sequence similarity between C1r and C1s and support the hypothesis that they are related by gene duplication . ^^^ Complementary DNA probes for human C1r and C1s do not cross hybridize even at mild stringency conditions and are therefore gene specific . ^^^ Using a panel of 25 human rodent cell hybrids , we have independently assigned the C1r and the C1s genes to chromosome 12 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Two other complement components , C1r and C1s , have two of these repeating units in the carboxy terminal region of their noncatalytic A chains . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Addition of C1r and C1s to C1q and formation of C 1 did not affect its capacity to agglutinate EC3b . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
This structural unit is called SCR ( short consensus repeat ) and is found in the complement proteins C1r , C1s , C 2 , factor B , factor H , C4BP , DAF , MCP and CR 2 , each of which interacts with some cleavage products of C 3 and / or C 4 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Circulating C1INH C1r C1s complexes were evidenced by reduced ratios of functional to antigenic C1INH and antigenic C1r to C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The finally purified preparation generates full Cl haemolytic activity when assayed with human complement subcomponents C1r and C1s , and have been identified as chicken C1q . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The human complement components C1r , C1s , C 4 , C 3 , factor B , and / or activated C1INH were functionally blocked in normal human serum ( NHS ) and EGTA or EDTA treated NHS by polyclonal monospecific Fab ' fragments to the individual components . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The proposed activation mechanism has four main features : steric exclusion of C 1 inhibitor from C 1 when it binds to an immune complex ; signal generation through multivalent binding of the C1q heads to an irregularly arranged cluster of antibody Fc regions , and signal transmission through the movement of the stiff C1q arms about their semi flexible joints , causing distortion of the symmetrical cone of C1q arms ; induction of rapid activation by a shift in equilibrium favoring the autocatalytic conformation of C1r2C1s2 ; and release of the activated C1s from the C1q arms , so that the ends of the tetramer are free for interaction with C 4 and C 2 and C 1 inhibitor , and the C1q subcomponent becomes more flexible , allowing access of C 1 inhibitor to C1r . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Domain structure and associated functions of subcomponents C1r and C1s of the first component of human complement . ^^^ The serine protease subcomponents of the activated form of the first component of human complement ( C 1 ) , C1r and C1s , were observed by electron microscopy after the native proteins and their limited proteolysis products , obtained from autolytic cleavage ( C1r ) or from incubation with plasmin ( C1s ) were rotary shadowed . ^^^ At the monomeric level , both C1r and C1s comprised two globular domains , a smaller interaction domain ( corresponding to the NH 2 terminal half of the A chain , alpha , and responsible for calcium binding and C1r C1s interaction ) and a larger catalytic domain ( corresponding to the COOH terminal part of the A chain , gamma , disulfide linked to the B chain and bearing the serine protease active site ) . ^^^ On the basis of the domain structure of C1r and C1s , a model of the calcium dependent C1s dimer is proposed , in which the two monomers interact through their NH 2 terminal interaction domains ; in the same way , a model of the C1s ( C1r ) 2 C1s catalytic subunit of C 1 is presented , in which ( C1r ) 2 forms a core , its distal interaction domains interacting with the corresponding domains of C1s . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Characteristics of complement subcomponents C1r and C1s synthesized by Hep G 2 cells . ^^^ The association and activation states of complement subcomponents C1r and C1s biosynthesized by Hep G 2 cells were studied . ^^^ C1r and C1s are secreted in stoichiometric amounts ; in the presence of Ca2+ they are associated in a complex that sediments similarly to plasma C1r2 C1s2 . ^^^ Secreted C1r is not autoactivatable but undergoes proteolysis by exogenous C1r ; secreted C1s is also proteolysed by exogenous C1r . ^^^ In the presence of immune complex bound C1q , secreted C1r and C1s are able to reconstitute C 1 , but normal activation requires extrinsic C1r2 C1s2 . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Differences in the mechanism of C 1 activation by nonimmune activators and by immune complexes : C1r independent activation of C1s by cardiolipin vesicles . ^^^ A similar dose response binding of C1s requiring C1q , but not C1r , was detected only on CL vesicles , but neither on PG vesicles nor on immune complexes . ^^^ The C1q bound C1s was specifically cleaved at 37 degrees C into its active 58 kDa and 28 kDa chains , in the absence of C1r . ^^^ When macromolecular C 1 was offered in the presence of C 1 INH , C1r cleavage was detected ; however , the presence of C1s was a critical factor for C1r activation , because it was required on CL vesicles , but not on immune complexes . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
CL vesicles which activate C 1 in the presence of C 1 inhibitor ( C 1 INH ) were found to bind C1s in the absence of C1r , and to induce a specific C1r independent cleavage of C1q bound C1s . ^^^ Therefore , several known natural nonimmune activators were analyzed by comparing their ability to activate C 1 in the presence of C 1 INH and to mediate a C1r independent cleavage of C1s . ^^^ DNA , known to activate C 1 only in the absence of C 1 INH , does not induce C1s cleavage in the absence of C1r . ^^^ By using C1qs2 as a probe , they exhibit a specific , C1r independent cleavage of C1s . ^^^ In the case of `` weak ' ' activators , such as E . coli smooth strains , DNA , or HHM , no C1s binding to activator bound C1q was detected , and C1r independent C1s cleavage and C 1 activation in the presence of C 1 INH were not observed . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The first component : C1q , C1r , C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Biosynthesis of the subcomponents C1q , C1r and C1s of the first component of complement ( C 1 ) by guinea pig hepatocyte primary cultures . ^^^ The hemolytic activity of C 1 and its subcomponents C1q and C1r / C1s was tested in the supernatants . ^^^ Guinea pig hepatocyte primary cultures synthesize and secrete up to 3 10 10 ( 3 ) effective C1q molecules / cell / 24 h and 34 10 10 ( 3 ) effective C1r / C1s molecules / cell / 24 h . ^^^ The synthesis of C1q and C1r / C1s could be reversibly inhibited by cycloheximide ( 50 micrograms / ml ) . ^^^ The data show that guinea pig hepatocytes are able to synthesize C 1 subcomponents , whereby the synthesis of C1q and C1r / C1s occurs independently . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Such a head to tail configuration , placed in the context of the model proposed for the C1s C1r C1r C1s catalytic subunit of C 1 [ Colomb , M . ^^^ London , B 306 , 283 292 ] , is compatible with autolytic activation of C1r through an intramolecular cross mechanism and with subsequent activation of C1s by activated C1r . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
A detailed model of C1s C1r2 C1s is proposed , according to which two C1s monomers bind to the outer globes of C1r2 by contacts between their heavy chains and those of C1r . ^^^ According to this model the catalytic domains of C1r are located in the center and those of C1s at the very tips of the C1s C1r2 C1s complex . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Sera from patients with systemic lupus erythematosus contained normal levels of RHP and were characterized by deficits of C1q required to form C 1 from existing levels of C1r and C1s . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
We have studied the effects of polyclonal monospecific Fab ' preparations against C1r , C1s , C1INH , C 4 , C4bp , and fragment Bb of factor B on complement activation in NHS and HAES . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 inhibitor is a heavily glycosylated plasma protein that regulates the activity of the first component of complement ( C 1 ) by inactivation of the serine protease subcomponents , C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The composition of complexes containing C 1 inactivator ( C 1 IA ) , C1r and C1s was investigated in normal serum after activation of C 1 under various conditions . ^^^ Analyses were performed with PAGE of eluates from Sepharose beads coated with F ( ab ' ) 2 fragments of anti C1s followed by immunoblotting with anti C 1 IA , anti C1s or anti C1r . ^^^ Eluates obtained from serum treated with aggregated IgG ( AGG ) contained C 1 IA in complex with C1r and C1s with both subcomponents in activated form . ^^^ Eluates from serum incubated at 37 degrees C for 1 , 2 or 3 days without activators showed C 1 IA complexed with activated C1r and with C1s in proenzyme state associated to the complex . ^^^ On analysis of serum , treated as mentioned above , by a variant of the electroimmunoassay using an intermediate gel containing anti C 1 IA and with anti C1s in the anodal gel the two types of C1r C1s C 1 IA complexes could be distinguished . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Synovial fibroblast like cells synthesized C1r , C1s , C 1 inhibitor , C 2 , C 3 , factor B , and factor H , all with the same sizes and subunit structures as the proteins synthesized in skin fibroblasts . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
We have previously shown that serum levels of C1q , unbound to C1r 10 C1s , are elevated in rheumatoid arthritis . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The findings suggested intra articular C 1 activation with dissociation of C 1 into free C1q and complexes containing C1r , C1s , and C 1 inactivator . ^^^ However , the immunochemical properties of synovial fluid C1r C1s C 1 inactivator complexes appeared to differ from those of the complexes formed in serum , which hampered quantification with the assay used . ^^^ Slightly increased concentrations of free C1q and C1r C1s C 1 inactivator complexes in serum and C3dg / d fragments in EDTA plasma were observed , particularly in the patients with rheumatoid arthritis . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The N terminal chain ( 422 residues ) of C1s , like that of C1r with which it is broadly homologous , contains five domains : domains 1 and 3 are homologous to one another and to similar regions in C1r , domain 2 is homologous to the epidermal growth factor sequence found in C1r and several other proteins , and domains 4 and 5 are homologous to one another and to the 60 residue repeating sequence found in C1r , C 2 , factor B , C 4 binding protein and some apparently unrelated proteins . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Using this simple yet sensitive assay to investigate the efficiency of reconstitution of C 1 activity from the purified components C1q , C1r , and C1s , we also find evidence for temperature and concentration dependent reaction steps in the formation of functional C1 . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Kinetics of appearance of activated C1r was the same as that of activated C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The lytic effect of NHS and C2d HS on SGL was abolished by immunochemically depleting C 1 from these sera , and reconstituted by adding purified C1q plus C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
This action of the C 1 inhibitor was over and above its ability to regulate fully activated C 1 by covalent bond formation with either the serine esterase of C1s or C1r . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The effective human urinary kallikrein inhibitors were further examined for their effect on other serine proteases , including human plasma kallikrein , plasmin , complement components ( C1s , C1r ) , bovine coagulation factors ( IIa , IXa , and Xa ) , elastase , and trypsin . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Upon activation of C 1 , C1r and C1s are rapidly inactivated by C 1 In which also forms a complex with these two subcomponents , resulting in their release from C 1 immune aggregate complexes . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
When human fibronectin ( FN ) was added after C1q , but before addition of C1r and C1s ( subunits of the first complement component ) , inhibition of haemolytic activity was observed which was strictly dependent upon the dose of FN . ^^^ When FN was added after addition of C 1 ( reconstituted from C1q , C1r and C1s ) , the haemolytic activity of complement was not affected by the presence of FN . ^^^ These data suggest that FN binds on C1q by interfering with C1r and C1s fixation . ^^^ In addition , FN was unable to displace the activated subcomponents ( C1r and C1s ) from their binding site on C1q . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Proenzyme and activated forms of C 1 subcomponents C1r and C1s and their Ca2+ dependent association ( C1r C1s ) 2 do not bind to E . coli D 31 m4 . ^^^ No turnover of the ( C1r C1s ) 2 subunit is observed . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The first component of complement , C 1 , is a calcium dependent complex of the three distinct subcomponents , C1q , C1r , and C1s . ^^^ In contrast , after dissociation of C 1 or C 1 by citrate , 100 % of the original C1q activity is recoverable on addition of C1q deficient serum as source of C1r and C1s . ^^^ EDTA treated C1q , fluid phase or bound to EA , was no longer able to form an hemolytically active C 1 complex by interaction with C1r and C1s . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Serum levels of C1q , C1r and C1s in normal and pathologic sera . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Interaction between C1q , C1r and C1s from human serum . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
A tetrameric complex of C1r2 C1s2 binds to the collagenous tails and leads to formation of the serine type proteases C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The flexible rod like structure of C1r2 C1s2 is folded around two arms of C1q , with the catalytic domains of C1r and C1s inserted inside the cone defined by the C1q stalks . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Structure and activity of C1r and C1s . ^^^ During activation of the first component of the classical complement pathway the two zymogen subcomponents , C1r and C1s are converted to active proteolytic enzymes . ^^^ Activated C1r cleaves C1s which then becomes the activator of C 4 and C 2 . ^^^ Amino acid sequence studies of the proteolytic chains of C1r and C1s , carried out in Oxford and Aberdeen respectively , have shown that they belong to the serine proteinase family . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The formation of neoantigens within the C1q molecule after the binding of C1r and C1s to C1q and the binding of C1q to immune complexes is described . ^^^ This immunochemical study supports the hypothesis drawn from functional studies that the activation of the classical C pathway results from conformational changes within the C1q molecule leading to the activation of C1r and subsequently C1s . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The classical pathway has a calcium dependent step ( C1q , C1r , C1s ) and a magnesium dependent reaction ( the enzymatic action of C1s on C 4 and C 2 ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
LMW Hep ( 2 . 5 nM ) inhibited the ability of C1q ( 0 . 5 nM ) to recombine with C1r ( 1 . 4 nM ) and C1s ( 1 . 6 nM ) to form hemolytically active C 1 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Kinetics of reaction of human C 1 inhibitor with the human complement system proteases C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Activation of a complex of C1r and C1s subcomponents of human complement C 1 by the third subcomponent C1q . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Calcium binding properties of the C 1 subcomponents C1q , C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The product , C1r 2 , retained the original antigenic properties of C1r and a functional active site , but lost the capacity to bind C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The reconstitution of human C 1 , the first complement component : binding of C1r and C1s to C1q influences the C1q conformation . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Conformational changes of the subunits C1q , C1r and C1s of human complement component C 1 demonstrated by 125I labeling . ^^^ C1s and C1r proenzymes and enzymes ( C1s , C1r ) and C1q were labeled with 125I . ^^^ The presence of either C1s , C1q or C1qs during labeling reduced the C1r H chain level , although C1r remained in the proenzyme form . ^^^ This was unexpected because one would have anticipated a diminution of the C1q label due to the apposition of C1r and C1s , similarly as it occurs during C1rs complex and C1s dimer formation for the H chain label of C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Mapping the substrate binding site of human C1r and C1s with peptide thioesters . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
So far , human complement sub components C1r and C1s are the only known mammalian serine proteinases lacking this disulphide bridge . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Under specified conditions purified C1q , activated C1r and C1s and C1r C1s complexes were bound independently of Ca2+ , to heparin Sepharose , and could be eluted by an increasing salt gradient . ^^^ Zymogen C1r and C1s , C1r C1s complexes , C 1 inactivator , and C1r C1s C 1 activator complexes were not bound . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
For biochemical characterization , the first component of human complement ( C 1 ) was reconstituted from physiologic concentrations of purified C1q , 125I C1r , and 131I C1s . ^^^ Upon incubation at 37 degrees C , C 1 spontaneously activated , as evidenced by the characteristic proteolysis of the C1r and C1s polypeptide chains as detected by SDS PAGE analysis . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The human complement system serine proteases C1r and C1s and their proenzymes . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Fluid phase interaction of C 1 inhibitor ( C 1 Inh ) and the subcomponents C1r and C1s of the first component of complement , C 1 . ^^^ The interaction of C 1 Inh with the Ca2+ dependent C1r2 C1s2 complex ( 8 . 8 S ) led to an 8 . 5 S inhibited C1r C1s C 1 Inh complex ( 1 : 1 : 2 ) , indicating a disruption of C1r2 and of C1s2 on C 1 Inh binding . ^^^ The 8 . 5 S inhibited complex was stable in the presence of EDTA ; it was also formed from a mixture of C1r , C1s and C 1 Inh in the presence of EDTA or from bimolecular complexes of C1r C 1 Inh and C1s C 1 Inh . ^^^ C1r 2 , a modified C1r molecule , deprived of a Ca2+ binding site after autoproteolysis , did not lead to an inhibited tetrameric complex on incubation with C1s and C 1 Inh . ^^^ An ester link between a serine residue at the active site of C1r or C1s and C 1 Inh is postulated . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Proenzymic subcomponents C1r and C1s associated to form a trimeric C1r2 C1s complex ( 7 . 6 S ) in the presence of EDTA , and a tetrameric Clr 2 C1s2 complex ( 9 . 1 S ) in the presence of Ca2+ . ^^^ Iodination of the 9 . 1 S complex led to a predominant labelling of C1r ( 70 % ) over C1s ( 30 % ) , essentially located in the b chain moiety of C1r and in the a chain moiety of C1s . 2 . ^^^ Reconstruction of proenzymic soluble C 1 ( 15 . 2 S ) from C1q , C1r and C1s was partially inhibited when C1s labelled in its monomeric form was used and almost abolished when iodinated C1r was used . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The human hepatoma derived cell line , HepG 2 , synthesized and secreted functional complement proteins C1r , C1s , C 2 , C 3 , C 4 , C 5 , factor B , C 1 inhibitor , C3b inactivator , a small amount of C 6 , and trace amounts of C 8 ; but failed to produce detectable C1q , C 7 , or C 9 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The first component of human complement ( C 1 ) was reconstituted from equimolar concentrations of its purified subunits C1q , C1r , and C1s , in the presence of each of nine different metal ions for the purpose of studying the qualitative and quantitative nature of the metal ion requirement for C 1 assembly and function . ^^^ For C 1 reconstituted with each metal ion , three assays characteristic of C 1 were performed as follows : ( 1 ) spontaneous C 1 activation in the absence of the regulatory protein C 1 inhibitor was assessed by sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis by simultaneously quantifying the specific proteolysis of the C1r and C1s subunits ; ( 2 ) C 1 activation induced by aggregated IgG in the presence of C 1 inhibitor was similarly analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis ; and ( 3 ) formation of 16 S macromolecular C 1 was determined in the analytical ultracentrifuge . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Incubation of HFf with highly purified C1r also resulted in activation of C1r as assessed directly using a synthetic substrate or indirectly by activation of C1s and consumption of C 2 . ^^^ However , incubation of HFf with highly purified C1s resulted in formation of activated C1s ( C1s ) but this was less efficient than HFf activation of C1r . ^^^ We therefore conclude that activation of C 1 in macromolecular C 1 is the result of HFf conversion of C1r to C1r ; activation of C1s then occurs primarily by C 1r and to a lesser degree by the direct action of HFf . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
When C1r and C1s were added , the binding of Fn to C1q was abolished ; removal of C1r and C1s restored Fn binding to C1q . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
No such fluorescence increase is observed during C1s activation by trace amounts of C1r . ^^^ The slight changes observed on activation are not restricted to C1r , as comparable results are obtained for proenzyme and activated C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
In their sera , C1q like material was found , whereas C1r and C1s were normal or increased in concentration , as were the other complement components tested . ^^^ It did not bind to C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The turnover numbers of C 2 and C 4 cleavage by C1s were affected to different extents , depending on whether C1s was alone or associated with C1r or with monoclonal antibodies to C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Using these assays , we show that C1q serum levels are significantly increased in rheumatoid arthritis ( RA ) and that the excess C1q levels in this disease are not accompanied by increased levels of C1r and C1s . ^^^ Active RA is therefore characterized by increased levels of hemolytically active C1q that has a physiologically active stem region unbound to C1r and C1s . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
By electroimmunoassay , complement components were quantitated in serum ( C1q , C1r , C1s , C 1 IA , C 2 , P , D . 1 , H , C 6 and C 7 ) or in EDTA plasma ( C 4 , C 3 , B , C 5 . and C ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Somewhat surprisingly , when the C1s sequence is compared with that of complement subcomponent C1r , the percentage difference ( 59 % ) is approximately the same as that found between the other mammalian serine proteinases ( 56 71 % ) . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Activation of the classical pathway was demonstrated in all patients by formation of complexes between C1r , C1s , and C 1 inactivator . ^^^ Large amounts of free C1q , not in complex with C1r and C1s , were demonstrated in the majority of patient sera . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
FUT 175 was found to inhibit , in an intense , specific and reversible way , the enzyme activities of trypsin , C1r , C1s , thrombin , kallikrein and plasmin with IC 50 values of the order of 10 ( 6 ) 10 ( 8 ) M . ^^^ FUT 175 also inhibited complement mediated hemolysis , including both classical and alternative pathways , sites of inhibition being on C1r and C1s as evidenced by the intermediate cell technique . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The antibody independent interaction with C 1 occurs via C1q , which binds to LPS and possibly also via another C 1 subcomponent , C1r and / or C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Evidently this protein , which binds to antigen antibody complexes and to C1r and C1s , thereby forming a physical link between the immune and complement systems , has been highly conserved in evolution . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
These findings can be explained by using recent findings concerning the association dissociation equilibrium between C1q and the tetrameric complex of C1r and C1s . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Human C1r has no affinity for the virus nor does guinea pig C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The binding of fibronectin to C1q could be inhibited by the restoration of C1r + C1s to the C 1 macromolecular complex before the addition of fibronectin . ^^^ The inhibition was dependent on the concentration of C1r + C1s and achieved a maximum of 70 % at 100 micrograms / ml . ^^^ This inhibition could be reversed by the removal of C1r and C1s subunits with EDTA or C 1 inhibitor . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Several serum proteins were identified in the purified IC : IgG , IgA , IgM , C1q , C1r , C1s , C3bi and Bb . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Assembly of subcomponents C1r and C1s of first component of complement : electron microscopic and ultracentrifugal studies . ^^^ Monomeric C1s ( Mr , 85 , 000 ; s 20 , w , 4 . 3S ) , a subcomponent of first component of complement ( C 1 ) , the dimer ( Mr , 170 , 000 ; s 20 , w , 6 . 7 S ) of C1r , another subcomponent , and the tetrameric complex ( C1r , C1s ) 2 ( Mr , 340 , 000 ; s 20 , w , 8 . 7 S ) are elongated molecules . ^^^ Hydrodynamic equivalents of cylindrical shape have a diameter of 3 . 3 nm and lengths of 20 nm for C1s , 36 nm for ( C1r ) 2 , and 64 nm for ( C1r , C1s ) 2 . ^^^ In electron micrographs the C1r , C1s complex appears as a chain composed of six to eight globular domains with a contour length of 51 nm . ^^^ A structure is proposed in which ( C1r ) 2 forms a core to which C1s protomers are associated at both ends . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Immunochemical quantitation of C components in both sera showed depressed levels of C1q , whereas the levels of C1r , C1s , and C 1 inhibitor were elevated . ^^^ Furthermore , the C1q of both siblings was unable to interact with immunoglobulins or to associate with C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The first component of complement ( C 1 ) is a macromolecule consisting of three distinct subcomponents , C1q , C1r , and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Also appraised for each method was the ability of the labeled molecules to bind to antibody sensitized cells and to interact with C1r and C1s to form C 1 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Radial double immunodiffusion experiments using antiserum to C1q , C1r , and C1s on HFf treated serum demonstrated the dissociation of the C 1 trimolecular complex , with concomitant reduction of C1r antigenicity that is indicative of C 1 activation . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Immunochemical and functional analysis of a complete C1q deficiency in man : evidence that C1r and C1s are in the native form , and that they reassociate with purified C1q to form macromolecular C 1 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
From SDS PAGE analysis of the self activated C 1 , all the C1r and C1s subcomponents are converted to the activated split products , indicating that all C 1 molecules are biologically active . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1q binding appears to be mediated via the collagenous portion of the molecule in that 1 ) type 1 collagen inhibits this binding ; 2 ) C 1 reconstituted from purified C1q , C1r , and C1s does not bind to mononuclear cells , whereas the same amount of free C1q binds avidly ; and 3 ) C1q enhances the binding of aggregated IgG to mononuclear cells . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The rate of activation of C 1 has been studied by following the extent of hydrolysis of the C1r and C1s subcomponents , using a purified preparation of C 1 labelled with 125I . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
We report that amnion tissue explants and amnion derived epithelial cells synthesize and secrete six proteins of the complement system , C1r , C1s , C 1 inhibitor , factor B , C 3 , and factor H . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Using hemolytic assays , we were able to demonstrate that C1qR prevents the association of C1q with C1r and C1s to form macromolecular C 1 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
These include a region of similarity to astacin , a crayfish metalloprotease , five copies of a repeat first found in complement proteins C1r and C1s , and two copies of an epidermal growth factor like sequence . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
In comparison to the baseline , the mean values for C1q , C1r , C 2 , C 5 , C 6 , C 7 , C 8 , C 9 , FB , C1INH , C4BP , FH and FI exhibited a 3 5 fold increase , C 3 , total C 4 , albumin and the alpha 1 globulin fraction a 6 9 fold increase , and C1s , C4A , C4B , FB and alpha 2 , beta and gamma globulins a 10 20 fold increase . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The concept of this research is to construct deletion , point and hybrid mutants of the highly homologous C1r and C1s subcomponents , to reveal the functional role of individual modules , map the interaction sites between subcomponents of the C 1 complex and refine the structural model of C 1 . ^^^ Autographa californica nuclear polyhedrosis virus was used as vector to express human C1r and C1s in Spodoptera frugiperda cell culture and in lepidopteran larvae . ^^^ It is clear now , that this post translational modification does not play a role in the Ca2+ dependent C1r C1s interaction . ^^^ This observation indicates that the function of the C1s alpha part in the hybrid is modulated by the C1r part ( gamma B ) of the molecule . ^^^ The C1Rs hybrid behaves like C1r , providing haemolytically active C 1 with C1q and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
This similarity extends to the serine protease component , which shares a similar modular construction and about 40 % sequence identity with the C1r and C1s subcomponents of C 1 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The other half complexed with C1s but showed little complex formation with C1r . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
A study on the structure and interactions of the C 1 sub components C1r and C1s in the fluid phase . 1 . ^^^ It appears likely that the two monomers of C1r interact through their A chain and that the A and B chains are relatively independent from each other . 2 . 125I labelling of C1s in the presence of lactoperoxidase confirmed the calcium dependent dimerization of this subcomponent . ^^^ C1r dimer and C1s monomer were found to interact in the absence of calcium to form a C1r2 C1s complex ( 7 . 7 S ) , whereas in the presence of calcium the two sub components were associated into a C1r2 C1s2 complex ( 8 . 7S ) . ^^^ It appears likely that the formation of this tetrameric complex involves both calcium dependent , and calcium independent binding forces , and that C1r and C1s interact through their respective A chain which , in the case of C1s , is hidden upon association . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Identical binding of C1s , C1r , kallikrein , and beta factor XIIa was observed with the three molecules . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Northern blot and dot blot analysis showed that the mRNAs for all classical pathway complement components ( C1qA chain , C1qB chain , C1qC chain , C1r , C1s , C 4 and C 2 ) and the fluid phase regulatory components ( C 1 inhibitor , C 4 bp and factor 1 ) were present in all three types of synovial membrane . ^^^ Monocytes secreted C1q , C1r , C1s , C 4 , C 2 , C 1 inhibitor and C 4 bp but not factor 1 . ^^^ Fibroblasts secreted C1r , C1s , C 2 , C 3 , C 1 inhibitor and factor 1 but not C1q , C 4 or C 4 bp . ^^^ HUVEC secreted C1s , C 2 , C 1 inhibitor and factor 1 but not C1q , C1r , C 4 or C 4 bp . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Non coordinated biosynthesis of early complement components in a deficiency of complement proteins C1r and C1s . ^^^ We report on a 60 year old woman with systemic lupus erythematosus and a total ( 95 % ) C1r and a partial ( 36 % ) C1s deficiency . ^^^ Indeed C1r component was below the limits of detection whereas C1s component was lowered ( 36 % ) . ^^^ Biosynthesis of C1r and C1s by patient ' s monocytes was spontaneously normal but not up regulated by interferon gamma for C1r alone , whereas the biosynthesis of C1s , but also of interleukin 6 , was increased , indicating a specific disregulation of C1r . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Electroimmunoassays showed that lipoteichoic acid separately , yielded detectable amounts of free C1r2s2 subunits ; it also generated significantly more trimer complexes between C1r , C1s and C 1 inhibitor ( C1INH ) than did the other two activators . ^^^ Lipoteichoic acid was , however , a comparatively weak inducer of tetramer C1INH C1r C1s C1INH complexes . ^^^ Analysis through Western blotting showed that all activators accelerated consumption of C1r , induced complex formations between C1INH and C1s and produced cleavage products of C 2 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The activation of human C 1 , a Ca ( 2+ ) dependent complex proteinase comprising a non enzymic protein , C1q , and two serine proteinases , C1r and C1s , is based primarily on the intrinsic property of C1r to autoactivate . ^^^ Complete stabilization of C1r in its proenzyme form was obtained upon incorporation within the Ca ( 2+ ) dependent C1s C1r C1r C1s tetramer , and a comparable effect was observed when C1s was replaced by its Ca ( 2+ ) binding alpha fragment . ^^^ Both tetramers , C1s C1r C1r C1s and C1s alpha C1r C1r C1s alpha , readily associated with C1q to form 16 . 0 S and 14 . 7 S complexes respectively in which C1r fully recovered its activation potential . ^^^ Both complexes showed indistinguishable activation kinetics , indicating that the gamma B catalytic region of C1s plays no role in the mechanism that triggers C1r activation in C 1 . ^^^ The collagen like fragments of C1q retained the ability to bind to C1s C1r C1r C1s , but , in contrast with intact C1q , failed to induce C1r activation in the resulting complex at temperatures above 25 degrees C . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The zygotic dorsal ventral patterning gene tolloid ( tld ) exhibits a complex structure consisting of an N terminal domain with sequence similarity to the astacin family of metalloproteases and a C terminal domain composed of two EGF like repeats and five copies of the CUB repeat which was first found in human complement proteins C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
A 100 kDa protein in the C 4 activating component of Ra reactive factor is a new serine protease having module organization similar to C1r and C1s . ^^^ Although homology in the amino acid sequence of P 100 with that of human C1r and C1s subcomponents of C was less than 40 % , a striking similarity in domain organization was found among these proteins , indicating that P 100 is a new C 4 activating serine protease structurally similar to C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
All molecules in C 1 inhibitor purified from affected members ' plasma bind to activated C1s ( C 1 s ) , but approximately 50 % of molecules in these preparations do not bind to activated C1r ( C1r ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Like huBMP 1 it also contains an N terminal metalloendoprotease domain that shares sequence similarity with the astacin protease from crayfish , a C terminal domain that is similar to the repeat domain found in C1r or C1s serine proteases , and an EGF like segment . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 , the first component of complement : structure function relationship of C1q and collectins ( MBP , SP A , SP D , conglutinin ) , C 1 esterases ( C1r and C1s ) , and C 1 inhibitor in health and disease . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The amino terminal heavy chain contains domains that are homologous to segments of the low density lipoprotein receptor , complement components C1r and C1s , the macrophage scavenger receptor , and a recently described motif shared by the metalloprotease meprin and the Xenopus A 5 neuronal recognition protein . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Ca ( 2+ ) linked association of human complement C1s and C1r . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Protein engineering studies on C1r and C1s . 1 . ^^^ C1r and C1s cDNAs were placed downstream the strong polyhedrin promoter in the Autographa californica nuclear polyhedrosis virus and the recombinant proteins were expressed in insect cells , in biologically active form . ^^^ It is clear now , that this post translational modification does not play a role in the Ca2+ dependent C1r C1s interaction . 3 . ^^^ This observation indicates that the function of the C1s alpha part in the hybrid is modulated by the C1r part ( gamma B ) of the molecule . 5 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The catalytic subunit , C1s C1r C1r C1s , is a Ca ( 2+ ) dependent tetrameric association of two serine protease zymogens , C1r and C1s , that are sequentially activated by cleavage of a single peptide bond , upon binding of C 1 to activators . ^^^ The catalytic ( gamma B ) regions of C1r and C1s are respectively located in the centre and at each end of the isolated tetramer , and the Ca ( 2+ ) dependent C1r C1s associations are mediated by the interaction ( alpha ) regions , which contain one Ca2+ binding site each . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
We have investigated the synthesis of C1q , C1r , C1s and C 1 inhibitor in HepG 2 cells , human umbilical vein endothelial cells ( HUVEC ) , fibroblasts ( skin and synovial membrane ) , chondrocytes and monocytes . ^^^ C1r , C1s and C 1 inhibitor were synthesised by all cell types . ^^^ The secretion rates of C1r and C1s were approximately equimolar in fibroblasts and chondrocytes whereas the secretion rate for C1s exceeded that for C1r in the other cell types . ^^^ Molar ratios of C1s to C1r were approximately 2 : 1 for HepG 2 cells , 5 : 1 for monocytes and 10 : 1 for HUVEC . ^^^ The C1s : C1r ratio did not alter in chondrocytes or fibroblasts , but approached unity in HepG 2 , monocytes and HUVEC , due to relatively greater stimulation of C1r gene expression . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Progress in determining module structures in C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The sequences of nine serine proteinases of known crystal structure were compared with the serine proteinase sequences in the six complement proteins C1r , C1s , C 2 , factor B , factor 1 and factor D to assess the degree of structural homology of the latter with the crystal structures . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
In this paper we demonstrate the synthesis of the components of the classical complement pathway , namely C1q , C1r , C1s , C 1 Inh , C 2 , C 4 , and C 5 , by human glioma cell lines ( U118MG , T 193 , and T98G ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
This protein exhibits 87 . 4 % amino acid homology with mouse P 100 , and 36 . 4 % and 37 . 1 % homologies with that of the C1r and C1s subcomponents of human complement , respectively . ^^^ The characteristic nodules and domain of C1r and C1s were highly conserved in this protein . ^^^ This indicates that the P 100 , together with the C1r and C1s , forms a unique protein family having the same module / domain constitution . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Human complement serine proteases C1r and C1s and their proenzymes . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Genetic deficiency of one of the early components of the classical pathway of complement ( C1q , C1r , C1s , C 4 and C 2 ) is often associated with clinical symptoms and immunochemical abnormalities common in idiopathic autoimmune diseases , such as lupus erythematosus , but also with an increased incidence of various , local and generalized infections . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
It was observed that incubation of isolated NIA with fresh normal human serum resulted in the formation of sodium dodecyl sulfate ( SDS ) irreversible complexes of activated C1r C 1 inhibitor and activated C1s C 1 inhibitor and in activated C1s mediated C 4 conversion . ^^^ Preincubation of NIA with C1q , blocked NIA mediated C1r and C1s activation and C 4 conversion . ^^^ The concn of NIA required to activate C1r and C1s was similar to that of heat aggregated human IgG . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The full sequence was found to have characteristics of a serine protease and exhibited 29 % and 30 % homologies with those of light chains of the C1r and C1s subcomponents of complement , respectively . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 inh antigenic levels were normal in all patients ; however , the function of the C 1 inh tested against C1s and C1r was variable and outside the normal functional range in seven of the eight patients . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Of the 22 complement proteins examined , 13 bound heparin ( C1q , C 2 , C 4 , C4bp , C1INH , B , D , H , P , C 6 , C 8 , C 9 , and vitronectin ) while 9 did not bind heparin ( C1r , C1s , C 3 , Factor 1 , C 5 , C 7 , C3b , Ba and Bb ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 inhibitor is a serine proteinase inhibitor that is active against C1s , C1r , kallikrein , and factor 12 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Using metabolic labeling with [ 35S ] methionine , immunoprecipitation , and SDS PAGE , we demonstrated that HEp 2 cells synthesized C1r , C1s , C 1 inhibitor , C 3 , C 4 , factor B , and factor H . ^^^ The constitutive synthesis of C1r and C1s were the highest among these proteins , whereas the synthesis of C 4 was observed only when the cells were stimulated with IFN gamma . ^^^ C1r and C1s were secreted readily , whereas the rate of the secretion of C 4 and C 1 inhibitor was much slower . ^^^ Activated forms of C1r , C1s , and complexes of C 1 inhibitor C1s were found . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1qBP , when bound to C1q , prevents the assembly with C1r and C1s to form a functional C 1 complex . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Analysis of the reactivity of this recombinant protein with target proteases demonstrated no complex formation with C1s , C1r , or kallikrein . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Articular chondrocytes cultured in vitro synthesized C1r , C1s , C 4 , C 2 , C 3 and C 1 inhibitor but not C1q , C 4 binding protein or factor 1 , as assessed by enzyme linked immunosorbent assay ( ELISA ) and Northern blot analysis . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Exon structure of the gene encoding the human mannose binding protein associated serine protease light chain : comparison with complement C1r and C1s genes . ^^^ In this study , we analyzed MASP genomic clones and found that the light chain ( catalytic domain ) is encoded by six exons , whereas those of the complement C 1 subunits , C1r and C1s , and the haptoglobin segment have been reported to be encoded by a single exon . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Serum samples were obtained at that time and tested for total complement activity ( CH 100 ) and antigenic levels of C1q , C1r , C1s , C 3 and C 4 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
By developing 6 amidino 2 naphthyl 4 guanidinobenzoate ( 1 , FUT 175 ) as a basic structure , its various derivatives were synthesized and their inhibitory activities on trypsin , plasmin , kallikrein , thrombin , C1r and C1s as well as on complement mediated hemolysis were examined . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
By interaction of CSPG with solid phase bound C1q , formation of the C 1 complex upon the addition of C1r and C1s was impaired . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
MBL is structurally related to the complement C 1 subcomponent , C1q , and seems to activate the complement system through an associated serine protease known as MASP ( ref . 4 ) or p 100 ( ref . 5 ) , which is similar to C1r and C1s of the classical pathway . ^^^ We have now identified a new MBL associated serine protease ( MASP 2 ) which shows a striking homology with the previously reported MASP ( MASP 1 ) and the two C1q associated serine proteases C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r is one of the two serine proteases of C 1 , the first component of complement , in which it is associated in a calcium dependent manner to the homologous serine protease C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Surprisingly , neither clone is related to Bf / C2 but rather share the same domain structure of mammalian C1r / C1s / MASP ( mannan binding protein associated serine protease ) , and are more related evolutionarily to mammalian MASP than to mammalian C1r or C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
A dysfunctional C 1 inhibitor ( C 1 INH ) from a family in whom the propositus presented with systemic lupus erythematosus but without angioedema previously was shown to have diminished inhibitory activity toward isolated C1r and C1s , and intact C 1 . ^^^ However , the mutant with Asp at this position is unable to bind C1r and beta factor XIIa , and also has a decreased rate of reaction with C1s and kallikrein . ^^^ Although defective in inhibition of C1r and C1s , the P 2 A > 5 mutant had acquired the ability to complex with trypsin . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Using biosynthetic labelling , immunoprecipitation and sodium dodecyl sulfate polyacrylamide gel electrophoresis , we demonstrated that GECs synthesized C1r , C1s , C 1 inhibitor , C 3 , C 2 and factor B . ^^^ Both factor B and C 3 proteins were increased following addition of either IL 1beta , IL 6 or TNF alpha to GEC cultures ; however , these cytokines did not increase either C 2 , C1r , C1s or C 1 inhibitor biosynthesis . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
We used an enzyme linked immunosorbent assay to measure plasma levels of three multimolecular complement activation protein ( CAP ) complexes : C1r : C1s : C 1 inhibitor , C3bP and C5b 9 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Occurrence of the classical pathway complement proteins C1q , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 6 , C 7 , C 8 and C 9 was studied in human hippocampus and temporal cortex by immunohistochemistry and Western blotting . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
When added to solutions of the C1r2C1s2 tetramer , HI 532 converted the 8 . 7 S tetramer into an 18 S complex , which was seen by electron microscopy to be a dimer of parallel C1s 10 C1r 10 C1r 10 C1s molecules cross linked by two bivalent monoclonal antibodies . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
A neoepitope based enzyme immunoassay for quantification of C 1 inhibitor in complex with C1r and C1s . ^^^ A previously produced and characterized mouse MoAb , recognizing a neoepitope on the human plasma protein C 1 inhibitor complexed with its substrates , was used to design an enzyme immunoassay for detection of C 1 inhibitor complexed with C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
All recombinant fragments were expressed in a proenzyme form and cleaved by C1r to generate active enzymes expressing esterolytic activity and reactivity toward C 1 inhibitor comparable to those of intact C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Human myoblasts in vitro produced C1q , C1r , C1s , C 2 and C 4 constitutively and all syntheses were upregulated after stimulation with IFN gamma . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The calcium dependent interaction between C1r and C1s , the two homologous serine proteases of the first component of human complement C 1 , is mediated by their N terminal regions . ^^^ Due to its Ca2+ binding ability , the C1r EGF like module ( C1r EGF ) is supposed to participate in the C1r C1s interaction . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
MBL can activate C 4 , C 2 , and later acting complement components in the presence of serine proteases similar to but distinct from C1r and C1s via the lectin pathway of complement activation . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
MASP , C1r and C1s belong to the same family of serine proteases . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
For this purpose , the serum levels of the serum complement proteins C1q , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 6 , C 7 , C 8 , C 9 , Factor B and properdin were repeatedly evaluated by means of radial immunodiffusion assay in 26 CLL patients over a period of 2 years . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
When C1s alpha ( 159 ) 2 was mixed with the 6 . 8 S C1r2 in Ca2+ , a 7 . 5 S complex was formed , presumably the C1s alpha ( 159 ) 10 C1r 10 C1r 10 C1s alpha ( 159 ) tetramer . ^^^ This suggested that the presence of the 159 amino acid C1s alpha domain , which held the C1r to the C1q , was sufficient to permit activation by an immune complex , even though the catalytic domains of C1s were not present . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
These proteins include the complement proteases C1r , C1s and MASPs , the Limulus clotting factor C , and the proteins of the haptoglobin family . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The accuracies of the police report ( PR ) , the emergency department record ( EDR ) , and the ambulance report ( AR ) for each patient were compared with the CIR by computing percent agreement , with 95 % confidence intervals ( 95 % CIs ) for each variable and for each data source . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
In human heart , we detected mRNAs and proteins for C1q , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 6 , C 7 , C 8 , and C 9 with the use of reverse transcriptase polymerase chain reaction , Western blotting , and immunohistochemical techniques . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
These two proteases , MASP 1 and MASP 2 , are structurally similar to one another as well as to C1r and C1s . ^^^ Together , MASP , C1r and C1s constitute a novel serine protease family . ^^^ Based on the analysis of MASP cDNA of vertebrates and ascidians , the MASP / C1r / C1s family can be classified into two groups . ^^^ The second group includes human MASP 2 , Xenopus MASP 2 , carp MASP , shark MASP , C1r and C1s . ^^^ The TCN type of MASP may have emerged prior to the AGY type as an ancestral protease of the MASP / C1r / C1s family and played a crucial role in cleaving C3 . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The two MASPs share the domain organisation of C1r and C1s and it may be speculated that interaction between the two MASPs is required for complement activation in the same manner as with the C 1 proteases . ^^^ Phylogenetic analysis indicates that MASP 2 is closer to C1r and C1s than is MASP 1 , but no particular association between MASP 2 and the C 4 cleaving enzyme , C1s , can be deduced from sequence comparison . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Structural and functional studies on C1r and C1s : new insights into the mechanisms involved in C 1 activity and assembly . ^^^ C1r and C1s , the enzymes responsible for the activation and proteolytic activity of the C 1 complex of complement , are modular serine proteases featuring similar overall structural organizations , yet expressing very distinct functional properties within C 1 . ^^^ This review will initially summarize available information on the structure and function of the protein modules and serine protease domains of C1r and C1s . ^^^ It will then focus on the regions of both proteases involved in : ( 1 ) assembly of C1s C1r C1r C1s , the Ca ( 2+ ) dependent tetrameric catalytic subunit of C 1 ; ( 2 ) expression of C 1 catalytic activities . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Our protein engineering studies on human C1r and C1s revealed important characteristics of the individual domains of these multidomain serine proteases , and supplied evidence about the cooperation of the domains to create binding sites , and to control the activation process . ^^^ Deletions and point mutants of C1r were constructed and C1r C1s chimeras were also produced . ^^^ Our deletion mutants demonstrated that the N terminal CUB domain and the EGF like domain of C1r together are responsible for the calcium dependent C1r C1s interaction . ^^^ The substrate specificity of the serine protease is also determined by the five N terminal noncatalytic domain of C1r / C1s chimera , which contains the catalytic domain of C1s preceded by the N terminal region of C1r , could replace the C1r in the hemolytically active C 1 complex . ^^^ The C1s / C1r chimera , in which the alpha fragment of the C1r was replaced for that of the C1s exibits both C1r and C1s like characteristics . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Besides binding of HNP 1 to C1q , also a limited binding to C 1 and to a mixture of C1r and C1s was observed , whereas no binding to C 1 inhibitor was found . ^^^ Because binding of HNP 1 to C 1 inhibitor has been suggested in earlier studies , we also assessed the binding of HNP 1 to mixtures of C 1 inhibitor with either C1r / C1s or C 1 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 , the first component of the classical pathway of complement activation is a complex of three proteins called C1q , C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Deficiencies of the first complement components , C1r / C1s , often cause systemic lupus erythematosus like syndromes and severe pyogenic infections . ^^^ Up to now no genetic analysis of the C1r / C1s deficiencies has been carried out . ^^^ In the present work , we report the first genetic analysis of selective C1s deficiency , the patient having a normal amount of C1r . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
We used reverse transcriptase polymerase chain reaction and Western blotting techniques to measure the levels of complement mRNAs and their protein products in Alzheimer ' s disease ( AD ) brain compared with non AD brain . mRNAs for C1q , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 6 , C 7 , C 8 , and C 9 were detected in the 11 regions of brain that were investigated . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
MASP 1 and MASP 2 are composed of modular structural motifs similar to those of the C1q associated serine proteases C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The classical C activation pathway was reconstituted from the proteins C1q , C1r , C1s , C 4 , C 2 , C 3 , factor H , and factor 1 ; each were purified to homogeneity . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Analysis of the cDNA reveals three sequence motifs : a carboxyl terminal region with similarity to the trypsin like serine proteases , four tandem cysteine rich repeats homologous to the low density lipoprotein receptor , and two copies of tandem repeats originally found in the complement subcomponents C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The ratio of AD to control mRNAs in these four areas was 1 . 17 for C 1 inh and 1 . 12 for CD 59 , compared to 3 . 06 for C1r , 2 . 67 for C1s , 2 . 35 for C 5 , 2 . 56 for C 6 , 2 . 42 for C 7 , 5 . 08 for C 8 and 16 . 3 for C 9 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Structure and functions of the interaction domains of C1r and C1s : keystones of the architecture of the C 1 complex . ^^^ C1r and C1s , the proteases responsible for activation and proteolytic activity of the C 1 complex of complement , share similar overall structural organizations featuring five nonenzymic protein modules ( two CUB modules surrounding a single EGF module , and a pair of CCP modules ) followed by a serine protease domain . ^^^ These properties include the ability to bind Ca2+ ions with high affinity , to associate with each other within a Ca2+ dependent C1s C1r C1r C1s tetramer , and to interact with C1q upon C 1 assembly . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Mannan binding lectin ( MBL ) is an acute phase protein which activates the classical complement pathway at the level of C 4 and C 2 via two novel serine proteases homologous to C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
P 100 activates the C 4 component of the complement system and its domain organization is similar to C1r and C1s . ^^^ Its non protease region consisted of 10 exons , as in the case of C1r and C1s , and the introns were found present in the boundary separating two CUB domains , an EGF like domain and two CCP domains and each CUB and CCP domain contained extra internal introns . ^^^ The serine protease region was comprised of 6 exons in contrast to C1r and C1s , either of which consists of a single exon . ^^^ The exon intron structure was found to reflect the evolution of these molecules and P 100 to have derived earlier in the stage of evolution than C1r or C1s . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 inhibitor is the main inhibitor of the classical pathway of the complement system ( C1s and C1r ) , of the contact activation system ( factor XIIa and kallikrein ) and of the intrinsic pathway of coagulation ( factor XIa ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r and C1s were secreted at low levels by astrocytes and neuroblastoma cell lines . ^^^ Exposure of cells to IL 1 alpha , IL 1 beta , TNF alpha and to a far lesser extent IL 6 , markedly upregulated C1r , C1s , and C 3 production . ^^^ Thus , C 1 Inh production is refractory to stimulation by plaque associated cytokines , whereas these cytokines do stimulate C1r , C1s , and also C 4 and C 3 secretion by astrocytes and neuronal cells in culture . ^^^ In contrast to the amyloid plaque associated cytokines IL 1 beta , IL 1 alpha , and TNF alpha , the amyloid peptide A beta 1 42 itself did not stimulate C1r and C1s synthesis by astrocytes , microglial cells , or neuroblastoma cell lines . ^^^ The ability of C1q to reassociate with newly formed C1r and C1s upon activation of C 1 and subsequent inactivation by C 1 Inh , may enable ongoing complement activation at sites of amyloid deposition , especially when C 1 Inh is consumed and not replaced . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
It was shown that the C3a receptor C1r and C1s genes form an unexpected complement gene cluster towards the telomeric end of chromosome 6 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
RESULTS : FUT 175 inhibited C1r and C1s with IC50s of 1 . 7x10 ( 6 ) and 3 . 2x10 ( 7 ) M , respectively . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The cleavage of two C1s subunits by a single active C1r reveals substantial flexibility of the C1s C1r C1r C1s tetramer in the C 1 complex . ^^^ The activation of the C1s C1r C1r C1s tetramer in the C 1 complex , which involves the cleavage of an Arg Ile bond in the catalytic domains of the subcomponents , is a two step process . ^^^ First , the autolytic activation of C1r takes place , then activated C1r cleaves zymogen C1s . ^^^ This mutant was used to form a C1q ( C1s C1rQI C1r C1s ) heteropentamer to study the relative position of the C1r and C1s subunits in the C 1 complex . ^^^ After triggering the C 1 by IgG Sepharose , both C1s subunits are cleaved by the single proteolytically active C1r subunit in the C1s C1rQI C1r C1s tetramer . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Structural similarities shared by MBL and C 1 complexes and by the MBL and C1q associated serine proteases , MBL associated serine protease ( MASP ) 1 and MASP 2 , and C1r and C1s , respectively , have led to the expectation that the pathways of complement activation by MBL and C 1 complexes are likely to be very similar . ^^^ We have expressed rMASP 2 and show that , whereas C 1 complex autoactivation proceeds via a two step mechanism requiring proteolytic activation of both C1r and C1s , reconstitution with MASP 2 alone is sufficient for complement activation by MBL . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Interaction of C1q and mannan binding lectin ( MBL ) with C1r , C1s , MBL associated serine proteases 1 and 2 , and the MBL associated protein MAp 19 . ^^^ The proteases C1r and C1s were initially discovered in a complex with C1q , whereas the MBL associated serine proteases 1 and 2 ( MASP 1 and 2 ) were discovered in a complex with MBL . ^^^ There is controversy as to whether MBL can utilize C1r and C1s or , inversely , whether C1q can utilize MASP 1 and 2 . ^^^ In serum , C1r and C1s were found to be associated only with C1q , whereas MASP 1 , MASP 2 , and a third protein , MAp 19 ( 19 kDa MBL associated protein ) , were found to be associated only with MBL . ^^^ The interactions of MASP 1 , MASP 2 , and MAp 19 with MBL differ from those of C1r and C1s with C1q in that both high salt concentrations and calcium chelation ( EDTA ) are required to fully dissociate the MASPs or MAp 19 from MBL . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Cerebral endothelial cells and HUVEC expressed detectable levels of complement gene mRNAs for the C1q B chain , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 7 , C 8 gamma subunit and C 9 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
By binding directly to carbohydrates on the surfaces of potential microbial pathogens , MBP and MBP associated serine proteases ( MASPs ) can replace antibodies and complement components C1q , C1r , and C1s of the classical complement pathway . ^^^ The biophysical properties of the truncated MASPs indicate that the interactions with MBP leading to complement activation differ significantly from those between components C1q , C1r , and C1s of the classical pathway . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 inhibitor ( C 1 INH ) , an inhibitor for C1r and C1s , formed equimolar complexes with MASP 1 and MASP 2 and inhibited their proteolytic activities . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Sequencing of the high pressure liquid chromatography purified peptides yielded the complement components C1r and C1s . ^^^ To confirm that C1r / C1s accounted for the proteolytic activity in the medium , immunoaffinity chromatography was performed . ^^^ Amino acid sequencing confirmed that the 88 kDa band contained only C1r and C1s . ^^^ C1r in the fibroblast medium underwent autoactivation , and the activated form cleaved C1s . ^^^ In summary , human fibroblasts secrete C1r and C1s that actively cleave IGFBP 5 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The complement serine proteases include the closely related C1r , C1s , MASPs 1 3 ( 80 90 kDa ) , C 2 and Factor B ( 100 kDa ) , Factor D ( 25 kDa ) and Factor 1 ( 85 kDa ) . ^^^ The C1r , C1s and MASP group occur as proenzymes . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Molecular cloning of the complement ( C1r / C1s / MASP2 like serine proteases from the common carp ( Cyprinus carpio ) . ^^^ C 1 is a Ca2+ dependent complex of C1q , C1r , and C1s , and analogous to an initiation complex of the lectin pathway of complement , which consists of the mannose binding lectin ( MBL ) homologous to C1q and the MBL associated serine proteases ( MASPs ) homologous to C1r and C1s . ^^^ Thus divergence of Clq and MBL and that of C1r , C1s and the MASPs are considered to be crucial events in the establishment and evolution of the classical complement pathway . ^^^ Here we describe two distinct C1r / C1s / MASP2 like cDNA clones ( C1r / s A , C1r / s B ) isolated from the common carp ( Cyprinus carpio ) . ^^^ They share 83 % identity at the amino acid level and have a domain structure similar to that of C1r / C1s / MASPs from other species . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
This patient ' s complement profile was characterized by the absence of CH 50 activity , C 1 functional activity < 10 % , and undetectable levels of C1s Ag associated with normal levels of C1r and C1q Ags . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The classical pathway of complement is initiated by the C 1 complex , a multimolecular protease comprising a recognition subunit ( C1q ) and two modular serine proteases ( C1r and C1s ) associated as a Ca2+ dependent tetramer ( C1s C1r C1r C1s ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The genes for the classical complement activation pathway proteases , C1r and C1s , are linked on chromosome 12p13 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r and its activated fragments all cleaved C1s , with relative efficiencies in the order C1r < CCP1 / 2 SP < CCP 2 SP , indicating that CCP 1 is not involved in C1s recognition . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Reactivity of the inhibitors toward target ( C1s , C1r , kallikrein , beta factor XIIa , and plasmin ) and nontarget proteases ( alpha thrombin and trypsin ) were studied . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Taken together with previous findings , these and other data strongly support the hypothesis that MASP 2 is the protease that , in association with MBL , triggers complement activation via the MBL pathway , through combined self activation and proteolytic properties devoted to C1r and C1s in the C 1 complex . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Activated C1r then cleaves and activates zymogen C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Using C 1 reconstituted from purified C1q , C1r , and C1s , it was shown that Abeta 1 42 fibrils trigger direct C 1 activation both in the absence of C 1 inhibitor and at C 1 inhibitor : C 1 ratios up to 8 : 0 , i . e . , under conditions consistent with the physiological context in serum . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 , the first protein of the classical pathway of complement activation , is a calcium dependent complex of one molecule of C1q and two molecules each of C1r and C1s , the serine proteases that cleave complement proteins . ^^^ Upon binding of C1q to Ag bound IgG or IgM , C1r and C1s are sequentially activated and initiate the classical pathway of complement . ^^^ Further investigation revealed that the binding of SP A to C1q prevents the association of C1q with C1r and C1s , and therefore the formation of the active C 1 complex required for classical pathway activation . ^^^ This finding suggests that SP A may share a common binding site for C1r and C1s or Clq . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
B 7 alphaCEA was also found to strongly enhance survival and tumor specific activation of T cells expressing an anti CEA TCRzeta based chimeric immune receptor ( CIR ) both when expressed in cis by the T cells themselves as well as in trans , when added to the culture medium . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Each complex has a recognition subunit ( C1q in the classical and mannose binding lectin ( MBL ) in the lectin pathway ) , which associates with serine protease zymogens ( C1q with C1r and C1s , and MBL with MBL associated serine proteases : MASP 1 , MASP 2 ) to form the C 1 and MBL MASPs complexes , respectively . ^^^ Special emphasis will be laid on the serine proteases : the role of the individual domains in the assembly of the C1s C1r C1r C1s tetramer and in the control of the protease activity will be discussed . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r , the enzyme responsible for intrinsic activation of the C 1 complex of complement , is a modular serine protease featuring an overall structural organization homologous to those of C1s and the mannan binding lectin associated serine proteases ( MASPs ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
However , in plaques , the mRNAs for C1r and C1s , the substrates for the C 1 inhibitor , were increased 2 . 35 and 4 . 96 fold , respectively , compared with normal artery ; mRNA for C 4 , the target for C4BP , was elevated l . 34 fold ; and mRNAs for C 7 and C 8 , the targets for CD 59 , were elevated 2 . 61 and 3 . 25 fold , respectively . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Initially it was thought likely that the MBL + MASPs system would resemble very closely the C 1 complex of the complement classical pathway , and that MASP 1 and MASP 2 would have similar activities to their classical pathway homologues C1r and C1s . ^^^ MASP 2 does certainly have similar activities to C1s , but MASP 1 does not have the activities of either C1r or C1s . ^^^ MASP 1 and MASP 2 appear not to have such a narrow specificity as C1r and C1s , and may have significant substrates other than complement proteins . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
This 790 , 000 Da complex is formed from the association of a recognition protein , C1q , and a catalytic subunit , the Ca2+ dependent tetramer C1s C1r C1r C1s comprising two copies of each of the modular proteases C1r and C1s . ^^^ Early studies mainly based on biochemical analysis and electron microscopy of C 1 and its isolated components have allowed for characterization of their domain structure and led to a low resolution model of the C 1 complex in which the elongated C1s C1r C1r C1s tetramer folds into a more compact , `` 8 shaped ' ' conformation upon interaction with C1q . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
This pathway is triggered by C 1 , a multimolecular protease formed from the association of a recognition protein , C1q , and a catalytic subunit , the calcium dependent tetramer C1s C1r C1r C1s , which comprises two copies of each of the modular proteases C1r and C1s . ^^^ All activators of the pathway are recognized by the C1q moiety of C 1 , a process that generates a conformational signal that triggers self activation of C1r , which in turn activates C1s , the enzyme that mediates specific cleavage of C 4 and C 2 , the C 1 substrates . ^^^ Early work based on biochemical and electron microscopy studies has allowed characterization of the domain structure of the C 1 subcomponents and led to a low resolution model of the complex in which the elongated C1s C1r C1r C1s tetramer folds into a compact , figure of 8 shaped conformation upon interaction with C1q . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
In addition , mRNAs for C1r , C1s , C 2 , C 3 , C 4 , C 5 and C 6 were also detected in T98G cells , but very low amount of mRNAs for C1q and MBL . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Complement C1r and C1s genes are duplicated in the mouse : differential expression generates alternative isomorphs in the liver and in the male reproductive system . ^^^ C1r and C1s are the serine proteases that form the catalytic unit of the C 1 complex , the first component of complement . ^^^ In the present study , we found that the genes encoding murine C1r and C1s are duplicated . ^^^ One set of these genes , referred to as c1rA and c1sA , are primarily expressed in the liver and are therefore the homologues of the human C1r and C1s genes . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1r and C1s are highly specific serine proteases that initiate the classical pathway of complement activation . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The MASPs show identical domain structure , shared also with C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Fucoidan binds C1q , likely to its collagen like region through interactions involving lysine residues , and then prevents the association of the C1r ( 2 ) C1s ( 2 ) subunit , required to form the fully active C 1 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The trout translation shows highest homology with carp C1r / s , and lower , equal homologies to mammalian C1r and C1s , and MASPs from other vertebrate species . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Moreover , within the range of concentrations studied , the studied inhibitors did not affect the subsequent C1q binding to the C1r and C1s enzymes . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
RT PCR analysis showed that the oligodendroglial cells expressed detectable levels of complement mRNAs for the C1q B chain , C1r , C1s , C 2 , C 3 , C 4 , C 5 , C 6 , C 7 , C 8 gamma subunit , and C 9 . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Because the IGFBP 5 protease activity that is secreted by fibroblasts has been shown to be due to the complement components C1r and C1s , these studies were undertaken to determine whether smooth muscle cells also secreted these proteases and to identify some of the factors that regulate their secretion by both cell types . ^^^ Both smooth muscle cells and human fibroblasts were shown to release C1r and C1s into conditioned medium . ^^^ Both C1r and C1s were detected as activated forms , as determined by SDS PAGE using reducing conditions . ^^^ The addition of increasing concentrations of either IL 1beta or TNFalpha resulted in increased synthesis of C1s by fibroblasts and smooth muscle cells , and they each increased C1r release . ^^^ In contrast dexamethasone ( 10 ( 7 ) M ) had no effect on C1s release and stimulated C1r release only by smooth muscle cells . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C 1 , the complex that triggers the classical pathway of complement , is assembled from two modular proteases C1r and C1s and a recognition protein C1q . ^^^ The N terminal CUB 1 EGF segments of C1r and C1s are key elements of the C 1 architecture , because they mediate both Ca2+ dependent C1r C1s association and interaction with C1q . ^^^ The C1s structure was used to build a model of the C1r C1s CUB 1 EGF heterodimer , which in C 1 connects C1r to C1s and mediates interaction with C1q . ^^^ A structural model of the C1q / C1r / C1s interface is proposed , where the rod like collagen triple helix of C1q is accommodated into a groove along the transversal axis of the C1r C1s heterodimer . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
In addition , adipsin , which belongs to the alternative pathway , and the classical pathway components C1QB , C1R , and C1S were expressed in both depots . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The MASPs are homologous to the C1q associated proteases , C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
In this study we investigated the exon intron organization of the human C1R gene , which spans 11 kb from the initiation codon to the stop codon , and is very similar in exon intron structure to the C1S gene . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Expression of C1q ( but not IL1beta , TNFalpha or Egr 1 ) remains high after BBB function is restored , and is accompanied by late up regulation of the C1q associated serine proteases , C1r and C1s , suggesting that microglial biosynthesis of the activation complex of the classical pathway may support the removal of cell debris by activation of complement . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
The classical complement pathway , which plays a vital role in preventing infection , is initiated by the action of the serine proteases C1r and C1s . ^^^ When C1s was in complex with C1q and C1r , as would occur under physiological conditions , the same behavior was observed , indicating that this mechanism is relevant in the complement pathway in vivo . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Binding causes activation of a series of serine protease proenzymes , such as C1r , C1s and MASP 2 ( MBL associated serine protease 2 ) , which in turn activate the atypical serine proteases factor B and C 2 , which then activate the major opsonin of the system , C 3 . ^^^ C1r , C1s and the MASPs , in contrast , are regulated more conventionally by the natural serpin , C 1 inhibitor . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Regulation of complement system activation takes place through inactivation of the classical pathway proteases , C1r and C1s , the lectin pathway protease , MASP 2 , and perhaps via inhibition of alternative pathway activation by reversible binding to C3b . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
A novel human complement related protein , C1r like protease ( C1r LP ) , specifically cleaves pro C1s . ^^^ Recombinant C1r LP exhibits esterolytic activity against peptide thioesters with arginine at the P 1 position , but its catalytic efficiency ( kcat / K ( m ) ) is lower than that of C1r and C1s . ^^^ Most importantly , C1r LP also expresses proteolytic activity , cleaving pro C1s into two fragments of sizes identical with those of the two chains of active C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
RESULTS : Complement has been shown to possess approximately 31 proteins , some of which are enzymes ( C1r , C1s , C 2 , factor B , factor D ) , some cofactors , some inhibitors or inactivators , and others composed of membrane integrated proteins . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
It was showed by ELISA that several compounds studied interact with C1q , C1r / C1s components of complement . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Specificities of 13 serine proteases ( activated protein C , plasma kallikrein , factor VIIa , factor IXabeta , factor XIa and factor alpha XIIa , activated complement C1s , C1r , and D , tryptase , trypsin , subtilisin Carlsberg , and cathepsin G ) and 11 papain like cysteine proteases ( cathepsin B , H , K , L , S , and 5 , rhodesain , papain , chymopapain , ficin , and stem bromelain ) were obtained from 103 , 968 separate microarray fluorogenic reactions ( 722 substrates 10 24 different proteases 10 6 replicates ) . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Besides its catalytic protease domain , the procollagen C proteinase contains several C terminal CUB modules ( named after complement factors C1r and C1s , the sea urchin UEGF protein , and BMP 1 ) and EGF like domains . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Genes induced by IFNs ( GBP 1 , GBP 2 , C1S , C1R , MHC2TA , PSMB 8 , TAP 1 , TAP 2 ) showed increased expression during porcine lung infection . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
C1q is the first subcomponent of the classical complement pathway that binds antigen bound IgG or IgM and initiates complement activation via association of serine proteases C1r and C1s . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
None of the mutations significantly altered C1s ability to assemble with C1r and C1q within C 1 . ^^^ Whereas the other mutations had no effect on C1s activation , the Q340E mutant was totally resistant to C1r mediated activation , both in the fluid phase and within the C 1 complex . ^^^ Thus , flexibility of the C1s CCP 1 CCP2 linker plays no significant role in C 1 assembly or C1s activation by C1r inside C 1 but plays a critical role in C 4 cleavage by adjusting positioning of this substrate for optimal cleavage by the C1s active site . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
PURPOSE OF REVIEW : Hereditary angioedema is an autosomal dominant deficiency of C 1 inhibitor a serpin inhibitor of kallikrein , C1r , C1s , factor 12 , and plasmin . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
Whereas C1s ( MASP 2 SP ) was recovered as an active enzyme , C1s ( MASP 2 CCP1 / 2 ) was produced in a proenzyme form and was susceptible to activation by C1r , indicating that the activation properties of the chimeras were dictated by the nature of their SP domain . ^^^ Remarkably , C1s ( MASP 2 CCP1 / 2 ) retained C1s ability to associate with C1r and C1q to form a pseudo C 1 complex and to undergo activation within this complex , indicating that the C1s CCP modules have no direct implication in either function . . ^^^
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA
Interacting proteins: P09871 and P00736	Pubmed	SVM Score :0.0
NA