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Journal of Biochemistry Advance Access published online on May 31, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn075
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© 2008 The Japanese Biochemical Society

Interaction between bisphenol derivatives and protein disulfide isomerase (PDI) and inhibition of PDI functions: Requirement of chemical structure for binding to PDI

Shoko Hashimoto, Kazushi Okada and Susumu Imaoka

Nanobiotechnology Research Center and Department of Bioscience, School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda 669-1337, Japan

Corresponding author: Dr. Kazushi Okada, Ph.D. Department of Bioscience, School of Science and Technology, Kwansei Gakuin University, 2-1 Gakuen, Sanda 669-1337, Japan. E-mail: bhp46831{at}kwansei.ac.jp, Tel/Fax: +81-79-565-7673

Received April 11, 2008; Accepted May 19, 2008


  Abstract

Bisphenol A (BPA) is an endocrine disrupting chemical and several biological effects have been reported. Previously, protein disulfide isomerase (PDI) was isolated as a target molecule of bisphenol A. In this study, to clarify the effects of BPA on PDI functions, we investigated the relationship between the chemical structure of BPA derivatives and the effects on PDI-mediated isomerase and chaperone activity. We also investigated the effects of changes in the isomerase domain of PDI on the binding of chemicals, using PDI mutants, and oxidized or reduced PDI. Among six chemicals, only chemicals, which have a phenol group, can bind to PDI and these chemicals also have an inhibitory effect on PDI-mediated isomerase activity. Changes in the structure of the PDI isomerase domain did not affect chemical-binding activity. On the other hand, the chemicals used in this study have low effects on chaperone activity of PDI. Substitutions in Cys residues (Cys398 and Cys401) of the isomerase active site changed chaperone activity. The present study indicates that phenolic compounds specifically bind to PDI and inhibit isomerase activity. This study provides useful information to predict the biological effects of chemicals and structural studies of PDI containing the function of chemical binding.

Key Words: bisphenol A, protein disulfide isomerase (PDI), dimethyl bisphenol A, chaperone activity, protein folding


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