Novel roles for protein disulphide isomerase in disease states: a double edged sword?

Front Cell Dev Biol. 2015 May 21;3:30. doi: 10.3389/fcell.2015.00030.

Sonam Parakh ¹, Julie D Atkin ²

Affiliations

1 Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University Sydney, NSW, Australia.
2 Department of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University Sydney, NSW, Australia ; Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University Bundoora, VIC, Australia.

PMID: 26052512 DOI: 10.3389/fcell.2015.00030

Abstract

Protein disulphide isomerase (PDI) is a multifunctional redox chaperone of the endoplasmic reticulum (ER). Since it was first discovered 40 years ago the functions ascribed to PDI have evolved significantly and recent studies have recognized its distinct functions, with adverse as well as protective effects in disease. Furthermore, post translational modifications of PDI abrogate its normal functional roles in specific disease states. This review focusses on recent studies that have identified novel functions for PDI relevant to specific diseases.

Keywords

amyotrophic lateral sclerosis; cancer; neurodegnerative diseases; post-translational modifications; protein chaperones; protein disulfide isomerase family.

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