Redox proteomics: identification and functional role of glutathionylated proteins

Authors: Fratelli, Maddalena; Gianazza, Elisabetta; Ghezzi, Pietro

Source: Expert Review of Proteomics, Volume 1, Number 3, October 2004 , pp. 365-376(12)

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Abstract:

Although radical oxygen and nitrogen species are harmful molecules that destroy cell functions, many operate as mediators of important cell signaling pathways when not in excess. Oxidants can modify protein function through the covalent, reversible addition of glutathione to cysteine. This review addresses different proteomic methods of identifying glutathionylation targets and emphasizes ways of defining their pattern of modification in response to oxidative stimuli in cells. Finally, the literature on nonproteomic studies that investigate the functional changes induced by glutathionylation are reviewed and future studies are commented on.

Keywords: chaperones; cytoskeletal proteins; glutathione; glycolytic enzymes; oxidative stress; post-translational protein modifications; redox signaling; S-glutathiolation; S-thiolation

Document Type: Research article

DOI: http://dx.doi.org/10.1586/14789450.1.3.365

Publication date: 2004-10-01

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Expert Review of Proteomics explores technologies, methods and discoveries from the field of proteomics to advance scientific understanding of the many varied roles protein expression plays in human health and disease.
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