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

Masaki Okumura, Hiroshi Kadokura, Shoko Hashimoto, Katsuhide Yutani, Shingo Kanemura, Takaaki Hikima, Yuji Hidaka, Len Ito, Kohei Shiba, Shoji Masui, Daiki Imai, Susumu Imaoka, Hiroshi Yamaguchi, Kenji Inaba

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)27004-27018
Number of pages15
JournalJournal of Biological Chemistry
Volume289
Issue number39
DOIs
Publication statusPublished - 2014 Sep 26

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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