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Int Rev Cell Mol Biol. 2011;290:121-66. doi: 10.1016/B978-0-12-386037-8.00003-X.

Chemical stress on protein disulfide isomerases and inhibition of their functions.

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1
Department of Bioscience, School of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo, Japan.

Abstract

Protein disulfide isomerase (PDI) is a folding assistant in the endoplasmic reticulum (ER) of eukaryotic cells. PDI has multiple roles, acting as a chaperone, a binding partner of other proteins, and a hormone reservoir as well as a disulfide isomerase in the formation of disulfide bonds. PDI only interacts covalently with the cysteines of its substrates, but also binds a variety of peptides/proteins and small chemical ligands such as thyroid hormone. Oxidative stress and nitrosative stress can cause damage to chaperones, protein misfolding, and neurodegenerative disease, by affecting the functional integrity of PDI. There are 20 putative PDI-family members in the ER of human cells, but their functional differentiation is far from complete. This review discusses recent advances in our understanding of the mammalian PDI family of enzymes and focuses on their functional properties and interaction with substrates and small chemical ligands.

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