Inhibition of the functional interplay between endoplasmic reticulum (ER) Oxidoreduclin-1α (Ero1α) and protein-disulfide isomerase (PDI) by the endocrine disruptor bisphenol A

Abstract

Background: Protein-disulfide isomerase (PDI) has previously been identified to bind bisphenol A (BPA), an endocrine disrupter. Results: BPA inhibited Ero1α-PDI-mediated disulfide bond formation. Conclusion: BPA significantly inhibited the Ero1α and PDI oxidative cycle, probably through closure of the substrate- and Ero1-binding pocket in the PDI bdomain. Significance: BPA may have inhibitory effects on oxidative folding of secretory and membrane proteins.