Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 14, Issue 1, Pages 434-456Publisher
MDPI
DOI: 10.3390/ijms14010434
Keywords
ER stress; ER stress associated disease; ER associated oxidative stress; disulfide bond formation; PDI; ERO-1 alpha; mitochondria electron transport chain
Funding
- National Research Foundation of Korea [12011000350]
- National Research Foundation of Korea [2012R1A2A1A03001907] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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.
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