Emerging mechanisms of glutathione-dependent chemistry in biology and disease
- Publication Type:
- Journal Article
- Journal of Cellular Biochemistry, 2013, 114 (9), pp. 1962 - 1968
- Issue Date:
Files in This Item:
|Janssen-Heininger_et_al-2013-Journal_of_Cellular_Biochemistry.pdf||Published Version||487.04 kB|
Copyright Clearance Process
- Recently Added
- In Progress
- Closed Access
This item is closed access and not available.
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease. © 2013 Wiley Periodicals, Inc.
Please use this identifier to cite or link to this item: