کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5826598 | 1120458 | 2007 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
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موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب سلولی و مولکولی
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چکیده انگلیسی
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 Ï isoform of glutathione-S-transferase (GSTÏ). 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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Current Opinion in Pharmacology - Volume 7, Issue 4, August 2007, Pages 381-391
Journal: Current Opinion in Pharmacology - Volume 7, Issue 4, August 2007, Pages 381-391
نویسندگان
Molly M Gallogly, John J Mieyal,