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
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
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.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.