Publication details for Dr Adam BenhamDias-Gunasekara S, Gubbens J, van Lith M, Dunne C, Williams JA, Kataky R, Scoones D, Lapthorn A, Bulleid NJ & Benham AM (2005). Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Erolb. Journal of Biological Chemistry 280(38): 33066-33075.
- Publication type: Journal Article
- ISSN/ISBN: 0021-9258, 1083-351X
- DOI: 10.1074/jbc.M505023200
- Further publication details on publisher web site
- Durham Research Online (DRO) - may include full text
Author(s) from Durham
Endoplasmic reticulum oxidoreductases (Eros) are essential for the formation of disulfide bonds. Understanding disulfide bond catalysis in mammals is important because of the involvement of protein misfolding in conditions such as diabetes, arthritis, cancer, and aging. Mammals express two related Ero proteins, Ero1 and Ero1. Ero1 is incompletely characterized but is of physiological interest because it is induced by the unfolded protein response. Here, we show that Ero1 can form homodimers and mixed heterodimers with Ero1, in addition to Ero-PDI dimers. Ero-Ero dimers require the Ero active site, occur in vivo, and can be modeled onto the Ero1p crystal structure. Our data indicate that the Ero1 protein is constitutively strongly expressed in the stomach and the pancreas, but in a cell-specific fashion. In the stomach, selective expression of Ero1 occurs in the enzyme-producing chief cells. In pancreatic islets, Ero1 expression is high, but is inversely correlated with PDI and PDIp levels, demonstrating that cell-specific differences exist in the regulation of oxidative protein folding in vivo.