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.
| Original language | English |
|---|---|
| Pages (from-to) | 434-456 |
| Number of pages | 23 |
| Journal | International Journal of Molecular Sciences |
| Volume | 14 |
| Issue number | 1 |
| DOIs | |
| State | Published - 2013.01 |
Keywords
- Disulfide bond formation
- ER associated oxidative stress
- ER stress
- ER stress associated disease
- ERO-1a
- Mitochondria electron transport chain
- PDI
Quacquarelli Symonds(QS) Subject Topics
- Computer Science & Information Systems
- Engineering - Petroleum
- Data Science
- Engineering - Chemical
- Chemistry
- Biological Sciences
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