Protein disulfide isomerase a multifunctional protein with multiple physiological roles
Protein disulfide isomerase (PDI), is a member of the thioredoxin superfamily of redox proteins. PDI has three catalytic activities including, thiol-disulfide oxireductase, disulfide isomerase and redox-dependent chaperone. Originally, PDI was identified in the lumen of the endoplasmic reticulum an...
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Format: | Article |
Language: | English |
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Frontiers Media S.A.
2014-08-01
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Series: | Frontiers in Chemistry |
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Online Access: | http://journal.frontiersin.org/Journal/10.3389/fchem.2014.00070/full |
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author | Hyder eAli Khan Bulent eMutus |
author_facet | Hyder eAli Khan Bulent eMutus |
author_sort | Hyder eAli Khan |
collection | DOAJ |
description | Protein disulfide isomerase (PDI), is a member of the thioredoxin superfamily of redox proteins. PDI has three catalytic activities including, thiol-disulfide oxireductase, disulfide isomerase and redox-dependent chaperone. Originally, PDI was identified in the lumen of the endoplasmic reticulum and subsequently detected at additional locations, such as cell surfaces and the cytosol. This review will provide an overview of the recent advances in relating the structural features of PDI to its multiple catalytic roles as well as its physiological and pathophysiological functions related to redox regulation and protein folding. |
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format | Article |
id | doaj.art-4e94121e4eec430fb3735098335cfdc8 |
institution | Directory Open Access Journal |
issn | 2296-2646 |
language | English |
last_indexed | 2024-04-13T07:24:37Z |
publishDate | 2014-08-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Chemistry |
spelling | doaj.art-4e94121e4eec430fb3735098335cfdc82022-12-22T02:56:31ZengFrontiers Media S.A.Frontiers in Chemistry2296-26462014-08-01210.3389/fchem.2014.00070103015Protein disulfide isomerase a multifunctional protein with multiple physiological rolesHyder eAli Khan0Bulent eMutus1University of WindsorUniversity of WindsorProtein disulfide isomerase (PDI), is a member of the thioredoxin superfamily of redox proteins. PDI has three catalytic activities including, thiol-disulfide oxireductase, disulfide isomerase and redox-dependent chaperone. Originally, PDI was identified in the lumen of the endoplasmic reticulum and subsequently detected at additional locations, such as cell surfaces and the cytosol. This review will provide an overview of the recent advances in relating the structural features of PDI to its multiple catalytic roles as well as its physiological and pathophysiological functions related to redox regulation and protein folding.http://journal.frontiersin.org/Journal/10.3389/fchem.2014.00070/fullDisulfidesEndoplasmic ReticulumChaperonecell surfaceprotein disulfide isomeraseoxidoreductase |
spellingShingle | Hyder eAli Khan Bulent eMutus Protein disulfide isomerase a multifunctional protein with multiple physiological roles Frontiers in Chemistry Disulfides Endoplasmic Reticulum Chaperone cell surface protein disulfide isomerase oxidoreductase |
title | Protein disulfide isomerase a multifunctional protein with multiple physiological roles |
title_full | Protein disulfide isomerase a multifunctional protein with multiple physiological roles |
title_fullStr | Protein disulfide isomerase a multifunctional protein with multiple physiological roles |
title_full_unstemmed | Protein disulfide isomerase a multifunctional protein with multiple physiological roles |
title_short | Protein disulfide isomerase a multifunctional protein with multiple physiological roles |
title_sort | protein disulfide isomerase a multifunctional protein with multiple physiological roles |
topic | Disulfides Endoplasmic Reticulum Chaperone cell surface protein disulfide isomerase oxidoreductase |
url | http://journal.frontiersin.org/Journal/10.3389/fchem.2014.00070/full |
work_keys_str_mv | AT hyderealikhan proteindisulfideisomeraseamultifunctionalproteinwithmultiplephysiologicalroles AT bulentemutus proteindisulfideisomeraseamultifunctionalproteinwithmultiplephysiologicalroles |