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Pharmacological Modulators of Endoplasmic Reticulum Stress in Metabolic Diseases
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Endoplasmic Reticulum Stress and Associated ROS

Department of Pharmacology and New Drug Development Institute, School of Medicine, Chonbuk National University, Jeonju, Chonbuk 561-180, Korea
Department of Dental Pharmacology and Wonkwang Biomaterial Implant Research Institute, School of Dentistry, Wonkwang University, Iksan, Chonbuk 570-749, Korea
Authors to whom correspondence should be addressed.
Academic Editor: Masato Matsuoka
Int. J. Mol. Sci. 2016, 17(3), 327;
Received: 23 December 2015 / Revised: 21 January 2016 / Accepted: 24 February 2016 / Published: 2 March 2016
(This article belongs to the Special Issue Modulators of Endoplasmic Reticulum Stress)
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The endoplasmic reticulum (ER) is a fascinating network of tubules through which secretory and transmembrane proteins enter unfolded and exit as either folded or misfolded proteins, after which they are directed either toward other organelles or to degradation, respectively. The ER redox environment dictates the fate of entering proteins, and the level of redox signaling mediators modulates the level of reactive oxygen species (ROS). Accumulating evidence suggests the interrelation of ER stress and ROS with redox signaling mediators such as protein disulfide isomerase (PDI)-endoplasmic reticulum oxidoreductin (ERO)-1, glutathione (GSH)/glutathione disuphide (GSSG), NADPH oxidase 4 (Nox4), NADPH-P450 reductase (NPR), and calcium. Here, we reviewed persistent ER stress and protein misfolding-initiated ROS cascades and their significant roles in the pathogenesis of multiple human disorders, including neurodegenerative diseases, diabetes mellitus, atherosclerosis, inflammation, ischemia, and kidney and liver diseases. View Full-Text
Keywords: ER stress; reactive oxygen species; Nox4; glutathione; NADPH-dependent p450 reductase; calcium ER stress; reactive oxygen species; Nox4; glutathione; NADPH-dependent p450 reductase; calcium

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Zeeshan, H.M.A.; Lee, G.H.; Kim, H.-R.; Chae, H.-J. Endoplasmic Reticulum Stress and Associated ROS. Int. J. Mol. Sci. 2016, 17, 327.

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