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

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 surfa...

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Bibliographic Details
Published in:British journal of pharmacology 2021-08, Vol.178 (15), p.2911-2930
Main Authors: Xu, Xulin, Chiu, Joyce, Chen, Shuai, Fang, Chao
Format: Article
Language:English
Subjects:
Catalysts
Cell surface
disulfide bond
Endoplasmic reticulum
Extracellular matrix
extracellular space
Molecular modelling
Protein disulfide-isomerase
Proteins
redox reaction
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Summary: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.
ISSN:0007-1188
1476-5381
DOI:10.1111/bph.15493