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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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.

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.[1]


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