scholarly journals Bisphenol A and rotenone induce S-nitrosylation of protein disulfide isomerase (PDI) and inhibit neurite outgrowth of primary cultured cells of the rat hippocampus and PC12 cells

2020 ◽  
Vol 45 (12) ◽  
pp. 783-794 ◽  
Author(s):  
Yukino Kobayashi ◽  
Ami Oguro ◽  
Erina Yagi ◽  
Akira Mitani ◽  
Suguru N. Kudoh ◽  
...  
Keyword(s):  
Bisphenol A ◽  
Neurite Outgrowth ◽  
Pc12 Cells ◽  
Protein Disulfide Isomerase ◽  
Cultured Cells ◽  
Rat Hippocampus ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Endoplasmic Reticulum Protein (ERp) 29 Binds As Strongly As Protein Disulfide Isomerase (PDI) to Bisphenol A

2014 ◽  
Vol 27 (4) ◽  
pp. 501-506 ◽  
Author(s):  
Yuka Miyake ◽  
Shoko Hashimoto ◽  
Yoshie Sasaki ◽  
Tomohiro Kudo ◽  
Ami Oguro ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Bisphenol A ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Endoplasmic Reticulum Protein ◽  
Protein Disulfide

scholarly journals Bisphenol A Binds to Protein Disulfide Isomerase and Inhibits Its Enzymatic and Hormone-Binding Activities

Endocrinology ◽  
2006 ◽  
Vol 147 (6) ◽  
pp. 2773-2780 ◽  
Author(s):  
Toyoko Hiroi ◽  
Kazushi Okada ◽  
Susumu Imaoka ◽  
Mayuko Osada ◽  
Yoshihiko Funae
Keyword(s):  
Bisphenol A ◽  
Protein Disulfide Isomerase ◽  
Hormone Binding ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Over-expression of protein disulfide isomerase reduces the release of growth hormone induced by bisphenol A and/or T3

2007 ◽  
Vol 278 (1-2) ◽  
pp. 44-51 ◽  
Author(s):  
Kazushi Okada ◽  
Susumu Imaoka ◽  
Shoko Hashimoto ◽  
Toyoko Hiroi ◽  
Yoshihiko Funae
Keyword(s):  
Growth Hormone ◽  
Bisphenol A ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Over Expression ◽  
Protein Disulfide

scholarly journals The Associations between Immunological Reactivity to the Haptenation of Unconjugated Bisphenol A to Albumin and Protein Disulfide Isomerase with Alpha-Synuclein Antibodies

Toxics ◽  
2019 ◽  
Vol 7 (2) ◽  
pp. 26
Author(s):  
Datis Kharrazian ◽  
Martha Herbert ◽  
Aristo Vojdani
Keyword(s):  
Bisphenol A ◽  
Human Serum ◽  
Protein Misfolding ◽  
Protein Disulfide Isomerase ◽  
Alpha Synuclein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Disulfide Isomerase ◽  
Substantial Risk ◽  
Protein Disulfide ◽  
Increased Susceptibility

Patients with Parkinson’s disease (PD) have increased susceptibility to bisphenol A (BPA) exposure since they have an impaired biotransformation capacity to metabolize BPA. PD subjects have reduced levels of conjugated BPA compared to controls. Reduced ability to conjugate BPA provides increased opportunity for unconjugated BPA to bind to albumin in human serum and protein disulfide isomerase on neurons. Once unconjugated BPA binds to proteins, it changes the allosteric structure of the newly configured protein leading to protein misfolding and the ability of the newly configured protein to act as a neoantigen. Once this neoantigen is formed, the immune system produces antibodies against it. The goal of our research was to investigate associations between unconjugated BPA bound to human serum albumin (BPA–HSA) antibodies and alpha-synuclein antibodies and between Protein Disulfide Isomerase (PDI) antibodies and alpha-synuclein antibodies. Enzyme–linked immunosorbent assay was used to determine the occurrences of alpha-synuclein antibodies, antibodies to BPA–HSA adducts, and PDI antibodies in the sera of blood donors. Subjects that exhibited high levels of unconjugated BPA–HSA antibodies or PDI antibodies had correlations and substantial risk for also exhibiting high levels of alpha-synuclein antibodies (p < 0.0001). We conclude that there are significant associations and risks between antibodies to BPA–HSA adducts and PDI antibodies for developing alpha-synuclein antibodies.

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