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Novel roles for protein disulphide isomerase in disease states: a double edged sword?
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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4439577/ https://www.ncbi.nlm.nih.gov/pubmed/26052512 http://dx.doi.org/10.3389/fcell.2015.00030 |
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author | Parakh, Sonam Atkin, Julie D. |
author_facet | Parakh, Sonam Atkin, Julie D. |
author_sort | Parakh, Sonam |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4439577 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-44395772015-06-05 Novel roles for protein disulphide isomerase in disease states: a double edged sword? Parakh, Sonam Atkin, Julie D. Front Cell Dev Biol Chemistry 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. Frontiers Media S.A. 2015-05-21 /pmc/articles/PMC4439577/ /pubmed/26052512 http://dx.doi.org/10.3389/fcell.2015.00030 Text en Copyright © 2015 Parakh and Atkin. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Chemistry Parakh, Sonam Atkin, Julie D. Novel roles for protein disulphide isomerase in disease states: a double edged sword? |
title | Novel roles for protein disulphide isomerase in disease states: a double edged sword? |
title_full | Novel roles for protein disulphide isomerase in disease states: a double edged sword? |
title_fullStr | Novel roles for protein disulphide isomerase in disease states: a double edged sword? |
title_full_unstemmed | Novel roles for protein disulphide isomerase in disease states: a double edged sword? |
title_short | Novel roles for protein disulphide isomerase in disease states: a double edged sword? |
title_sort | novel roles for protein disulphide isomerase in disease states: a double edged sword? |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4439577/ https://www.ncbi.nlm.nih.gov/pubmed/26052512 http://dx.doi.org/10.3389/fcell.2015.00030 |
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