Journal
EUROPEAN JOURNAL OF BIOCHEMISTRY
Volume 267, Issue 16, Pages 4928-4944Publisher
WILEY
DOI: 10.1046/j.1432-1327.2000.01601.x
Keywords
cysteine; glutathione; nitric oxide; reactive nitrogen species; reactive oxygen species
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Protein S-glutathiolation, the reversible covalent addition of glutathione to cysteine residues on target proteins, is emerging as a candidate mechanism by which both changes in the intracellular redox state and the generation of reactive oxygen and nitrogen species may be transduced into a functional response. This review will provide an introduction to the concepts of oxidative and nitrosative stress and outline the molecular mechanisms of protein regulation by oxidative and nitrosative thiol-group modifications. Special attention will be paid to recently published work supporting a role for S-glutathiolation in stress signalling pathways and in the adaptive cellular response to oxidative and nitrosative stress. Finally, novel insights into the molecular mechanisms of S-glutathiolation as well as methodological problems related to the interpretation of the biological relevance of this post-translational protein modification will be discussed.
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