| First Author | Hirano N | Year | 1995 |
| Journal | Eur J Biochem | Volume | 234 |
| Issue | 1 | Pages | 336-42 |
| PubMed ID | 8529662 | Mgi Jnum | J:30051 |
| Mgi Id | MGI:77573 | Doi | 10.1111/j.1432-1033.1995.336_c.x |
| Citation | Hirano N, et al. (1995) Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation. Eur J Biochem 234(1):336-42 |
| abstractText | Recently it was shown that putative phospholipase C-alpha cDNA does not code for an isotype of the phospholipase C superfamily but for one of the glucose-regulated proteins (GRPs), ERp57/GRP58. We have isolated human ERp57/GRP58 cDNA from human placenta. Sequence analysis showed that ERp57/GRP58 has two Trp-Cys-Gly-His-Cys-Lys motifs completely conserved among the mammals. Bacterially expressed recombinant ERp57/GRP58 protein contained a thiol-dependent reductase activity which was completely abolished when Ser residues were substituted for Cys residues in both of the two motifs. Furthermore, we have identified a soluble form of ERp57/GRP58 by Western blotting and biosynthetic labeling. In v-onc transformants of normal rat kidney cells, the expression level of ERp57/GRP58 was elevated at the protein level. In NIH3T3 cells transformed with v-src, activated c-src (Y527F) or c-src, the expression level of ERp57/GRP58 was upregulated in proportion to their transforming abilities. These results indicate that a soluble form of ERp57/GRP58 exists and that this protein may control both extracellular and intracellular redox activities through its thiol-dependent reductase activity. Moreover, it is likely that ERp57/GRP58 is involved in the oncogenic transformation. |
