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An Involvement of Oxidative Stress in Endoplasmic Reticulum Stress and Its Associated Diseases
Authors:Bidur Bhandary  Anu Marahatta  Hyung-Ryong Kim  Han-Jung Chae
Affiliation:1.Department of Pharmacology, School of Medicine, Chonbuk National Univeristy, Jeonju 561-180, South Korea; E-Mails: (B.B.); (A.M.);2.Department of Dental Pharmacology, Dental School, Wonkwang University, Iksan 570-749, South Korea
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.
Keywords:ER stress   ER stress associated disease   ER associated oxidative stress   disulfide bond formation   PDI   ERO-1α   mitochondria electron transport chain
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