Int. J. Mol. Sci. 2013, 14(1), 434-456; doi:10.3390/ijms14010434
An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases
1
Department of Pharmacology, School of Medicine, Chonbuk National Univeristy, Jeonju 561-180, South Korea
2
Department of Dental Pharmacology, Dental School, Wonkwang University, Iksan 570-749, South Korea
*
Authors to whom correspondence should be addressed.
Received: 26 October 2012 / Revised: 1 December 2012 / Accepted: 13 December 2012 / Published: 24 December 2012
(This article belongs to the Special Issue Advances in Free Radicals in Biology and Medicine)
Abstract
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 Ca2+ 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. View Full-TextKeywords:
ER stress; ER stress associated disease; ER associated oxidative stress; disulfide bond formation; PDI; ERO-1α; mitochondria electron transport chain
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
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Int. J. Mol. Sci.
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