| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.61266728 |
| Purified protein 4 . 1 binds with 50 fold higher affinity to protein 4 . 1 depleted normal red cell membranes than to protein 4 . 1 depleted red cell membranes of Leach phenotype which lack Glycophorin C ( GPC ) and Glycophorin D ( GPD ) . 0.61266728^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.76696264 |
| In this paper we show that purified protein 4 . 1 binds much less strongly to alkali stripped membranes from erythrocytes of individuals with total glycophorin C and D deficiency ( Leach phenotype ) than to alkali stripped normal membranes . 0.76696264^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.50915006 |
| This network is linked to trans bilayer proteins , through the complex beta spectrin ankyrin anion exchanger ( + protein 4 . 2 ) on the one hand and , on the other hand , through the triangular interaction between protein 4 . 1 , glycophorin C and protein p 55 . 0.50915006^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.50173525 |
| In conjunction with our recent finding that a third protein termed p 55 is also deficient in protein 4 . 1 ( ) and glycophorin C ( ) RBCs , the present data underscore the importance of the membrane associated ternary complex between protein 4 . 1 , glycophorin C , and p 55 during the invasion and growth of malaria parasites into human RBCs . . 0.50173525^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.60379127 |
| Human p 55 , the major palmitoylated protein associated with the cytoplasmic face of the erythrocyte membrane , is believed to modulate interactions between protein 4 . 1 and glycophorin C . 0.60379127^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| The RBCs of the compound heterozygote , containing only the shortened species of protein 4 . 1 , made it possible to analyze without interference the contact between shortened protein 4 . 1 and sialoglycoprotein beta , or glycoconnectin . ^^^ Shortened protein 4 . 1 did not alter the amount of glycoconnectin in the ghosts nor did it change its extractability into the Triton shells . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| The cytoskeleton is bound to the transmembrane proteins : by ankyrin to the internal segment of protein band 3 , and by protein 4 . 1 to a glycoprotein named glycoconnectin . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| First , transfer of a radioactive cross linker ( 125I 2 ( p azido salicylamido ) ethyl 1 3 dithiopropionate ) from purified band 4 . 1 to its binding sites on stripped inside out erythrocyte membrane vesicles ( stripped IOVs ) revealed major labeling of band 3 , glycophorin C , and glycophorin A . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| This does not correspond to any of the known loci of genes for red cell membrane proteins including protein 4 . 1 ( 1p36 . 2 p 34 ) , the anion exchange protein ( AE 1 , band 3 ; 17q21 qter ) , glycophorin C ( 2q14 q 21 ) , and beta actin ( 7pter q 22 ) . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Glycophorin C content of human erythrocyte membrane is regulated by protein 4 . 1 . ^^^ Human erythrocyte transmembrane sialoglycoprotein , glycophorin C , plays a functionally important role in maintaining erythrocyte shape and regulating membrane material properties , possibly through its interaction with protein 4 . 1 . ^^^ Moreover , it has previously been shown that membranes deficient in protein 4 . 1 exhibit decreased content of glycophorin C . ^^^ To further define the relationship between protein 4 . 1 and glycophorin C , a series of studies were performed using both protein 4 . 1 and glycophorin C deficient erythrocytes . ^^^ Quantitation by flow cytometry showed that the glycophorin C content of cells totally deficient in protein 4 . 1 was 9 % of normal and that of cells partially deficient in protein 4 . 1 was 44 % of normal . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Functional role for glycophorin C and its interaction with the human red cell membrane skeletal component , protein 4 . 1 . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Erythrocytes deficient in glycophorin C and band 4 . 1 were also resistant to invasion by both P . falciparum and P . knowlesi . . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| A synthetic peptide , comprising the 28 C terminal residues of glycophorin C , also binds protein 4 . 1 . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Protein 4 . 1 previously has been shown to bind to integral membrane proteins band 3 , glycophorin C , and to negatively charged phospholipids . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Identification of the protein 4 . 1 binding interface on glycophorin C and p 55 , a homologue of the Drosophila discs large tumor suppressor protein . ^^^ In this investigation , synthetically tagged peptides and bacterially expressed proteins were used to map the protein 4 . 1 binding site on human erythroid glycophorin C , a transmembrane glycoprotein , and on human erythroid p 55 , a palmitoylated peripheral membrane phosphoprotein . ^^^ The results show that the 30 kDa domain of protein 4 . 1 binds to a 12 amino acid segment within the cytoplasmic domain of glycophorin C and to a positively charged , 39 amino acid motif in p 55 . ^^^ Our data provide new insights into how protein 4 . 1 , glycophorin C , p 55 , and their non erythroid homologues , interact with the cytoskeleton to exert their physiological effects . . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| In this paper we show that the major attachment site is glycophorin ( GP ) C / D , and that purified protein 4 . 1 can bind to two distinct sites on glycophorin C / D . ^^^ The binding sites for band 3 , glycophorin C / D , and p 55 are all located within the 30 kDa domain of protein 4 . 1 . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Fractionally mobile integral proteins , such as band 3 , and highly mobile receptors , such as CD 59 as well as glycophorin C in protein 4 . 1 deficient cells , appeared to be squeezed out of areas dense in the underlying network and enriched in areas of network dilation . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Absence of high affinity band 4 . 1 binding sites from membranes of glycophorin C and D deficient ( Leach phenotype ) erythrocytes . ^^^ The fact that PIP 2 depletion induced a decrease in band 4 . 1 binding to Leach vesicles shows that glycophorin C or D is not required for the formation of PIP 2 sensitive band 4 . 1 binding sites , and may not be involved in PIP 2 sensitive band 4 . 1 binding sites even when they are present . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| In vitro binding studies suggest a membrane associated complex between erythroid p 55 , protein 4 . 1 , and glycophorin C . p 55 is a palmitoylated peripheral membrane phosphoprotein of human erythrocytes . ^^^ We also provide evidence demonstrating the direct association of the 30 kDa domain of protein 4 . 1 with the cytoplasmic domain of glycophorin C . ^^^ Taken together , these results suggest the existence of a novel ternary complex at the erythroid plasma membrane involving protein 4 . 1 , p 55 , and glycophorin C . ^^^ Since isoforms of protein 4 . 1 , p 55 , and glycophorin C are present in many non erythroid cells , the binding interactions may be prototypical of similar associations that modulate cytoskeletal membrane linkage of broad significance . . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Flowcytometric analysis showed that the glycophorin C content of the patient ' s erythrocytes was reduced but maintained the level of about 70 % of that of normal , indicating that the glycophorin C band 4 . 1 interaction might not be so seriously damaged as to cause elliptocytic shape change . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Evidence that red blood cell protein p 55 may participate in the skeleton membrane linkage that involves protein 4 . 1 and glycophorin C . ^^^ We used naturally mutated red blood cells ( RBCs ) with primary genetic defects resulting in the absence of protein 4 . 1 ( 4 . 1 [ ] hereditary elliptocytosis ) or glycophorin C ( Leach elliptocytosis ) . ^^^ On a stoichiometric basis , the reduction in glycophorin C ( about 80 % ) was concomitant to the lack of p 55 in RBCs devoid of protein 4 . 1 . ^^^ Similarly , the reduction of protein 4 . 1 ( about 20 % ) was equivalent to the absence of p 55 in RBCs devoid of glycophorin C . ^^^ These correlations suggest that p 55 is associated , in precise proportions , with the protein 4 . 1 glycophorin C complex , linking the skeleton and the membrane . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Lateral interactions among these proteins constitute the spectrin based composite structure that is anchored to the bilayer through vertical interactions , one involving beta spectrin , ankyrin and band 3 , and the other through an interaction between protein 4 . 1 and glycophorin C . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| We show that protein 4 . 1 bound to the inside out vesicles could be dissociated from band 3 but not from glycophorin C by IRRRY . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NRX is a transmembrane protein with a cytoplasmic domain homologous to glycophorin C , a protein required for anchoring protein 4 . 1 in the red blood cell . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Taken together with our previous studies , these results complete the identification of interacting domains in the ternary complex between p 55 , glycophorin C , and protein 4 . 1 . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| In this report , we show that the band 3 / red blood cells contain protein 4 . 1 , adducin , dematin , p 55 , and glycophorin C . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Erythrocyte protein 4 . 1 has been hypothesized to link the spectrin actin junctional complex directly to the cytoplasmic domain of glycophorin C , but this bridging function has never been directly demonstrated . ^^^ In contrast , obstruction of protein 4 . 1 binding to its docking site on the cytoplasmic pole of glycophorin C is demonstrated to reduce the same protein 4 . 1 bridging function by approximately 85 % . ^^^ We conclude from these data that ( 1 ) glycophorin C contributes the primary anchoring site of the protein 4 . 1 mediated bridge to the spectrin actin skeleton ; ( 2 ) band 3 is incapable of serving the same function ; and ( 3 ) additional minor protein 4 . 1 bridging sites may exist on the human erythrocyte membrane . . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| The erythrocyte membrane cytoskeletal protein 4 . 1 ( 4 . 1R ) is a structural protein that confers stability and flexibility to erythrocytes via interactions with the cytoskeletal proteins spectrin and F actin and with the band 3 and glycophorin C membrane proteins . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| Protein 4 . 1 of red blood cells ( 4 . 1R ) is a multifunctional protein essential for maintaining erythrocyte shape and membrane mechanical properties , such as deformability and stability , through lateral interactions with spectrin and actin in the skeletal network and vertical interactions with cytoplasmic domains of transmembrane proteins , glycophorin C , and band 3 . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| These results indicate that GPC and GPD together are sufficiently abundant to provide membrane attachment sites for all of the protein 4 . 1 in normal RBCs . . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| We showed that mesangial cells ( MCs ) from diabetic mice exhibited a stable phenotypic switch , consisting of both increased IGF 1 synthesis and proliferation ( Elliot SJ , Striker LJ , Hattori M , Yang CW , He CJ , Peten EP , Striker GE : Mesangial cells from diabetic NOD mice constitutively secrete increased amounts of insulin like growth factor 1 . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| The spatial brightness profiles of emission lines for the K like through He like ionization states of Fe , Ge , and Ni have been measured during a set of experiments in which Fe and Ge were introduced into FTU tokamak plasmas by using the laser blowoff technique . ^^^ The Mazzotta et al . ( for Fe and Ni ) , the Mattioli ( for Ge ) , and the AR 92 ( for Fe only ) rates adequately simulated the He , Li , Be , Na , Mg like ionization states . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| This study was performed to evaluate necrosis , apoptosis and intracellular calcium levels ( [ Ca2+ ] 1 ) in LLC PK 1 ( epithelial cell line from pig kidney ) induced by GE associated with LPS and a low osmolality media , Hexabrix ( HE ) . . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| This study was performed to evaluate necrosis , apoptosis , and intracellular calcium levels ( [ Ca2+ ] 1 ) in LLC PK 1 ( epithelial cell line from pig kidney ) induced by GE associated with LPS and a low osmolality media , Hexabrix ( HE ) . . ^^^ |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04921 and P11171 |
Pubmed |
SVM Score :0.0 |
| NA |
|