| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| These proteins were identified with antibodies and microsequencing as the ER chaperone BiP ( grp 78 ) , grp 94 , calreticulin , a novel 46 kDa protein that binds azido ATP , as well as three members of the thioredoxin superfamily : protein disulfide isomerase , ERp 72 , and a previously reported 50 kDa protein ( p 50 ) . ^^^ The release of grp 94 , protein disulfide isomerase , ERp 72 , calreticulin , and p 50 was stimulated by Ca2+ in the presence of ATP . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| NH 2 terminal sequence and / or Western blot analysis revealed the identity of two of the proteins as the endoplasmic reticulum ( ER ) resident stress proteins GRP 94 and ERp 72 . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| As a result , the synthesis of three ER stress proteins , BiP , the 94 kDa glucose regulated protein ( GRP94 / ERp99 ) , and ERp 72 , was increased as were their mRNA levels . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| Competitive inhibition of a set of endoplasmic reticulum protein genes ( GRP 78 , GRP 94 , and ERp 72 ) retards cell growth and lowers viability after ionophore treatment . ^^^ Integration of about 800 tandem copies of this sequence into the genome of a Chinese hamster ovary cell line ( DG 44 ) results in transfectants with the following phenotypes : ( 1 ) the induction level of GRP 78 by the calcium ionophore A 23187 and tunicamycin is reduced 4 and 2 fold , respectively , ( 2 ) the induction levels of two other ER luminal protein genes , GRP 94 and ERp 72 , are simultaneously down regulated , ( 3 ) the growth rate of these cells is half that of transfectants without the amplified sequence , and ( 4 ) cell viability is decreased by 25 fold after A 23187 treatment . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| We have previously demonstrated that several endoplasmic reticulum ( ER ) proteins , including BiP , ERp 72 , grp 94 , and protein disulfide isomerase , bind to a denatured thyroglobulin ( Tg ) affinity column and can be specifically eluted by ATP ( Nigam , S . ^^^ Using chemical cross linking , we now demonstrate that BiP , ERp 72 , and grp 94 associate with Tg in two types of cultured thyroid cells , FRTL 5 and PCC 13 . ^^^ Whereas BiP could be coimmunoprecipitated with anti Tg antibodies in the absence of cross linking , only trace amounts of ERp 72 and grp 94 were coimmunoprecipitated . ^^^ Likewise , in both cell types , anti BiP antibodies were able to coimmunoprecipitate Tg in the absence of cross linking , though ERp 72 and grp 94 were only minimally present . ^^^ In contrast , after cross linking , there was a large increase in the amount of ERp 72 and grp 94 that coimmunoprecipitated with anti Tg antibodies , although there was only a slight increase in BiP . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| Almost 30 % of the patients had also elevated auto antibody titers against purified rat grp 94 , another resident ER protein of the KDEL protein family , but not against rat ERp 72 ( CaBP 2 ) , an ER resident protein of the proteindisulfide isomerase family . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| Likewise , when cellular ATP was depleted to less than 10 % of control with antimycin A , mRNA levels of BiP , ERp 72 , and grp 94 were increased in kidney and thyroid epithelial cell culture models . ^^^ Furthermore , coimmunoprecipitation studies after antimycin A treatment demonstrated that Tg stably associates with BiP , grp 94 , and ERp 72 . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| By coimmunoprecipitation in rat thyroid cells , we were able to demonstrate that BiP , grp 94 , ERp 72 , and grp 170 , four proteins believed to function as specific molecular chaperones , complex with Tg during its maturation . ^^^ BiP , grp 94 , and ERp 72 were also found to associate with Tg in cells in which misfolding was induced by perturbing ER calcium stores . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| Exposure of Madin Darby canine kidney cells to various proteasome inhibitors , including the peptide aldehydes ( MG 132 , MG 115 , N acetyl leucyl leucyl norleucinal ) and lactacystin , inhibited the degradation of short lived proteins and increased markedly the levels of mRNAs encoding cytosolic heat shock proteins ( Hsp 70 , polyubiquitin ) and ER chaperones ( BiP , Grp 94 , ERp 72 ) , as shown by Northern blot analysis . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| The network of endoplasmic reticulum resident chaperones ( ERp 72 , GRP 94 , calreticulin , and BiP ) interacts with apolipoprotein b regardless of its lipidation state . ^^^ The endoplasmic reticulum ( ER ) resident molecular chaperones GRP 94 , calreticulin , and ERp 72 were co immunoprecipitated with apoB 100 from HepG 2 cell lysates following cross linking of proteins in living cells . ^^^ The interactions between apoB 100 and ERp 72 or GRP 94 persisted for at least 2 h following a 30 min pulse . ^^^ Thus , BiP / GRP78 , calreticulin , ERp 72 , and GRP 94 may participate in critical steps in the folding of apoB before any substantial lipidation occurs . ^^^ ERp 72 and GRP 94 may also mediate the folding of more advanced folding intermediates and / or target the misfolded underlipidated pool of apoB for degradation . . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| In addition to PDI and gp 96 , previously identified as peptide binding chaperones in the ER , we show that ERp 72 , calnexin , and grp 170 interact with TAP translocated peptides . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| The R273W mutation did not affect the ability of VWF to bind to BiP , Grp 94 , ERp 72 , calnexin , and calreticulin in COS 7 cells . ( Blood . 2000 ; 96 : 560 568 ) . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| Five chaperone proteins : BiP ( Grp 78 ) ; calreticulin ( CRT ) ; protein disulfide ( PDI ) ; ERp 72 ; and Grp 94 , demonstrated immunoreactivity in the enlarged PSACH cisternae and the short rER channels of chondrocytes from both in vivo and in vitro samples . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones , GRP 94 , ERp 72 , BiP , calreticulin , and cyclophilin B . ^^^ Immunoprecipitation of apoB followed by Western blotting showed that the luminal pool floated at a density of 1 . 12 g / ml and , like the membrane bound pool , was associated with GRP 94 , ERp 72 , BiP , calreticulin , and cyclophilin B . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| We demonstrate the existence of a large endoplasmic reticulum ( ER ) localized multiprotein complex that is comprised of the molecular chaperones BiP ; GRP 94 ; CaBP 1 ; protein disulfide isomerase ( PDI ) ; ERdj 3 , a recently identified ER Hsp 40 cochaperone ; cyclophilin B ; ERp 72 ; GRP 170 ; UDP glucosyltransferase ; and SDF 2 L1 . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| The expression of the heat shock proteins ( HSP ) , endoplasmic reticulum protein ( ERp 72 ) and glucose regulated protein ( GRp 78 ) , was among the genes whose expression was significantly elevated in the cortex during sleep deprivation , whereas GRp 78 and GRp 94 mRNAs were elevated in the cortex during recovery sleep after sleep deprivation , as confirmed by conventional and quantitative real time polymerase chain reaction and / or Northern analyses . ^^^ A systematic evaluation of the expression of six heat shock protein family members ( ERP 72 , GRp 78 , GRp 94 , HSP 27 , HSP 70 1 , and HSP 84 ) in seven brain regions revealed increased mRNA levels in cortex , basal forebrain , hypothalamus , cerebellum and medulla during sleep deprivation , whereas increased mRNA levels during recovery sleep were limited to the cortex and medulla . ^^^ Immunohistochemical studies identified increased numbers of GRp 78 , GRp 94 , and ERp 72 immunoreactive cells in the dorsal and lateral cortex during sleep deprivation but , during recovery sleep , elevated numbers of these cells were found only in the lateral cortex . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| Because intracellular inclusions , containing either amyloid beta ( Abeta ) or phosphorylated tau , are the characteristic feature of sporadic inclusion body myositis ( s IBM ) muscle biopsies , we studied expression and immunolocalization of five ER chaperones , calnexin , calreticulin , GRP 94 , BiP / GRP78 , and ERp 72 , in s IBM and control muscle biopsies . ^^^ Our studies provide evidence of the UPR in s IBM muscle and demonstrate for the first time that the ER chaperones calnexin , calreticulin , GRP 94 , BiP / GRP78 , and ERp 72 physically associate with AbetaPP in s IBM muscle , suggesting their playing a role in AbetaPP folding and processing . . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| This work reveals that a 65 % reduction in the cellular UDP Glc level causes up regulation of the mitochondrial chaperone GRP 75 and the endoplasmic reticulum ( ER ) resident chaperones GRP 58 , ERp 72 , GRP 78 , GRP 94 , GRP 170 , and calreticulin . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| The results showed both enhanced ERp 29 expression and an interaction with the other ER chaperones such as GRP 94 , BiP , ERp 72 and calnexin . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| In the present study we show that the G544V mutant LDLR associates with the chaperones Grp 78 , Grp 94 , ERp 72 , and calnexin in the ER of transfected Chinese hamster ovary cells . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| Six chaperones , GRP 94 , GRP 78 , ERp 72 , PDI , CaBP1 / P5 and CRT were found to associate with IFN gamma during its steady state folding . ^^^ |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P13667 and P14625 |
Pubmed |
SVM Score :0.0 |
| NA |
|