title: Redox proteomics: identification and functional role of glutathionylated proteins.
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.
authors.affiliation: Istituto di Ricerche Farmacologiche Mario Negri, Via Eritrea 62, I-20157 Milan, Italy. maddalena@marionegri.it
authors.forename: Maddalena
authors.initials: M
authors.lastname: Fratelli
authors.forename: Elisabetta
authors.initials: E
authors.lastname: Gianazza
authors.forename: Pietro
authors.initials: P
authors.lastname: Ghezzi
mesh_terms: D000818:Animals; D002460:Cell Line; D004798:Enzymes / Q000302:isolation & purification / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism*; D006801:Humans; D007525:Isoelectric Focusing / Q000379:methods; D010084:Oxidation-Reduction; D011506:Proteins / Q000302:isolation & purification / Q000502:physiology*; D040901:Proteomics / Q000379:methods*
chemical_list: D004798:Enzymes; D011506:Proteins; D005978:Glutathione