期刊
CURRENT OPINION IN PHARMACOLOGY
卷 7, 期 4, 页码 381-391出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.coph.2007.06.003
关键词
-
资金
- NIA NIH HHS [R01 AG 024413, 1F30AG029687, P01 AG 15885] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008803, T32 GM07250] Funding Source: Medline
Reversible protein S-glutathionylation (protein-SSG) is an important post-translational modification, providing protection of protein cysteines from irreversible oxidation and serving to transduce redox signals. Analogous to phosphatases, glutaredoxin (GRx) enzymes catalyze deglutathionylation of proteins, regulating diverse intracellular signaling pathways. Recently, other enzymes have been reported to exhibit deglutathionylating activity, but their contribution to intracellular protein deglutathionylation is uncertain. Currently, no enzyme has been shown to serve as a catalyst of S-glutathionylation in situ, although potential prototypes are reported, including human GRx1 and the pi isoform of glutathione-S-transferase (GST pi). Further insight into cellular mechanisms of protein glutathionylation and deglutathionylation will enrich our understanding of redox signal transduction and potentially identify new therapeutic targets for diseases in which oxidative stress perturbs normal redox signaling. Accordingly, this review focuses primarily on mechanisms of catalysis in mammalian systems.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据