| Interacting proteins: P04114 and P14625 |
Pubmed |
SVM Score :1.1145373 |
| Together with the finding that GRP 94 was found associated with sialylated apoB , we conclude that correct folding of apoB is dependent on the assistance of molecular chaperone , which play multiple roles in its maturation throughout the secretory pathway including distal compartments such as the trans Golgi network . . 1.1145373^^^ |
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| Interacting proteins: P04114 and P14625 |
Pubmed |
SVM Score :0.0 |
| 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 . . ^^^ |
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| Interacting proteins: P04114 and P14625 |
Pubmed |
SVM Score :0.0 |
| METHODS AND RESULTS : Glucosamine treatment ( 2 . 5 to 10 mmol / L ) of HepG 2 cells increased levels of the ER chaperones , 78 kDa glucose regulated protein ( Grp 78 ) and Grp 94 , in a dose dependent manner and led to significant decreases in both cellular and secreted apoB 100 by up to 97 % ( P < 0 . 01 ) . ^^^ |
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| Interacting proteins: P04114 and P14625 |
Pubmed |
SVM Score :0.0 |
| Knocking down apoB did not alter the expression of cytoplasmic stress proteins ( HSP 70 and HSP 90 ) and their ER homologues ( GRP 78 and GRP 94 ) . ^^^ |
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| Interacting proteins: P04114 and P14625 |
Pubmed |
SVM Score :0.0 |
| NA |
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