Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 43, Issue 6, Pages 883-898Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2007.06.014
Keywords
glutathione; oxidative stress; protein thiols; redox regulation; signal transduction; mixed disulficles; GSH/GSSG ratio; reactive thiolate anions; free radicals
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Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and low-pK, cysteinyl residues, not only is a cellular response to mild oxidative/nitrosative stress, but also occurs under basal (physiological) conditions. S-glutathionylation has now emerged as a potential mechanism for dynamic, posttranslational regulation of a variety of regulatory, structural, and metabolic proteins. Moreover, substantial recent studies have implicated S-glutathionylation in the regulation of signaling and metabolic pathways in intact cellular systems. The growing list of S-glutathionylated proteins, in both animal and plant cells, attests to the occurrence of S-glutathionylation in cellular response pathways. The existence of antioxidant enzymes that specifically regulate S-glutathionylation would emphasize its importance in modulating protein function, suggesting that this protein modification too might have a role in cell signaling. The continued development of proteomic and analytical methods for disulfide analysis will help us better understand the full extent of the roles these modifications play in the regulation of cell function. In this review, we describe recent breakthroughs in our understanding of the potential role of protein S-glutathionylation in the redox regulation of signal transduction. (c) 2007 Elsevier Inc. All rights reserved.
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