Cross-linking protein glutathionylation mediated by O2-arylated bis-diazeniumdiolate "Double JS-K".

ABSTRACT: Attachment of glutathione (GSH) to cysteine residues in proteins (S-glutathionylation) is a reversible post-translational modification that can profoundly alter protein structure and function. Often serving in a protective role, for example, by temporarily saving protein thiols from irreversible oxidation and inactivation, glutathionylation can be identified and semiquantitatively assessed using anti-GSH antibodies, thought to be specific for recognition of the S-glutathionylation modification. Here, we describe an alternate mechanism of protein glutathionylation in which the sulfur atoms of the GSH and the protein's thiol group are covalently bound via a cross-linking agent, rather than through a disulfide bond. This form of thiol cross-linking has been shown to occur and has been confirm

SUBMITTER: Holland RJ 

PROVIDER: S-EPMC3524378 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature