Send to

Choose Destination
Eur J Biochem. 1995 Nov 15;234(1):336-42.

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.

Author information

Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.


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.

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center