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An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases
The endoplasmic reticulum (ER) is the major site of calcium storage and protein folding. It has a unique oxidizing-folding environment due to the predominant disulfide bond formation during the process of protein folding. Alterations in the oxidative environment of the ER and also intra-ER Ca(2+) ca...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3565273/ https://www.ncbi.nlm.nih.gov/pubmed/23263672 http://dx.doi.org/10.3390/ijms14010434 |
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author | Bhandary, Bidur Marahatta, Anu Kim, Hyung-Ryong Chae, Han-Jung |
author_facet | Bhandary, Bidur Marahatta, Anu Kim, Hyung-Ryong Chae, Han-Jung |
author_sort | Bhandary, Bidur |
collection | PubMed |
description | The endoplasmic reticulum (ER) is the major site of calcium storage and protein folding. It has a unique oxidizing-folding environment due to the predominant disulfide bond formation during the process of protein folding. Alterations in the oxidative environment of the ER and also intra-ER Ca(2+) cause the production of ER stress-induced reactive oxygen species (ROS). Protein disulfide isomerases, endoplasmic reticulum oxidoreductin-1, reduced glutathione and mitochondrial electron transport chain proteins also play crucial roles in ER stress-induced production of ROS. In this article, we discuss ER stress-associated ROS and related diseases, and the current understanding of the signaling transduction involved in ER stress. |
format | Online Article Text |
id | pubmed-3565273 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-35652732013-03-13 An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases Bhandary, Bidur Marahatta, Anu Kim, Hyung-Ryong Chae, Han-Jung Int J Mol Sci Review The endoplasmic reticulum (ER) is the major site of calcium storage and protein folding. It has a unique oxidizing-folding environment due to the predominant disulfide bond formation during the process of protein folding. Alterations in the oxidative environment of the ER and also intra-ER Ca(2+) cause the production of ER stress-induced reactive oxygen species (ROS). Protein disulfide isomerases, endoplasmic reticulum oxidoreductin-1, reduced glutathione and mitochondrial electron transport chain proteins also play crucial roles in ER stress-induced production of ROS. In this article, we discuss ER stress-associated ROS and related diseases, and the current understanding of the signaling transduction involved in ER stress. MDPI 2012-12-24 /pmc/articles/PMC3565273/ /pubmed/23263672 http://dx.doi.org/10.3390/ijms14010434 Text en © 2013 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Bhandary, Bidur Marahatta, Anu Kim, Hyung-Ryong Chae, Han-Jung An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases |
title | An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases |
title_full | An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases |
title_fullStr | An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases |
title_full_unstemmed | An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases |
title_short | An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases |
title_sort | involvement of oxidative stress in endoplasmic reticulum stress and its associated diseases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3565273/ https://www.ncbi.nlm.nih.gov/pubmed/23263672 http://dx.doi.org/10.3390/ijms14010434 |
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