Endoplasmic Reticulum Stress and Associated ROS
AbstractThe 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
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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.
Zeeshan HMA, Lee GH, Kim H-R, Chae H-J. Endoplasmic Reticulum Stress and Associated ROS. International Journal of Molecular Sciences. 2016; 17(3):327.Chicago/Turabian Style
Zeeshan, Hafiz M.A.; Lee, Geum H.; Kim, Hyung-Ryong; Chae, Han-Jung. 2016. "Endoplasmic Reticulum Stress and Associated ROS." Int. J. Mol. Sci. 17, no. 3: 327.
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