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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...

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Autores principales: Bhandary, Bidur, Marahatta, Anu, Kim, Hyung-Ryong, Chae, Han-Jung
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2012
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.
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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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