Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms

Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms.

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Item Type: Review
Status: Published
Official URL: https://doi.org/10.1111/bph.15493
Journal or Publication Title: British Journal of Pharmacology
Volume: 178
Number: 15
Page Range: pp. 2911-2930
Date: August 2021
Divisions: ACRF Centenary Cancer Research Centre
Depositing User: General Admin
Identification Number: 10.1111/bph.15493
ISSN: 0007-1188
Date Deposited: 10 Oct 2021 08:52
Abstract:

Protein disulfide isomerase (PDI) is the prototypic member of the thiol isomerase family that catalyses disulfide bond rearrangement. Initially identified in the endoplasmic reticulum as folding catalysts, PDI and other members in its family have also been widely reported to reside on the cell surface and in the extracellular matrix. Although how PDI is exported and retained on the cell surface remains a subject of debate, this unique pool of PDI is developing into an important mechanism underlying the redox regulation of protein sulfhydryls that are critical for the cellular activities under various disease conditions. This review aims to provide an overview of the pathophysiological roles of surface and extracellular PDI and their underlying molecular mechanisms. Understanding the involvement of extracellular PDI in these diseases will advance our knowledge in the molecular aetiology to facilitate the development of novel pharmacological strategies by specifically targeting PDI in extracellular compartments.

Keywords: cell surface; disulfide bond; extracellular space; protein disulfide isomerase; redox reaction.

© 2021 The British Pharmacological Society.

Creators:
Creators
Email
Xu, Xulin
UNSPECIFIED
Chiu, Joyce
UNSPECIFIED
Chen, Shuai
UNSPECIFIED
Fang, Chao
UNSPECIFIED
Last Modified: 10 Oct 2021 08:52
URI: https://eprints.centenary.org.au/id/eprint/1121

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