Regulation of protein function by S‐glutathiolation in response to oxidative and nitrosative stress

作者：Peter Klatt, Santiago Lamas · 发表于：European Journal of Biochemistry · 年份：2000 · DOI：10.1046/j.1432-1327.2000.01601.x · 被引用次数：744 · 研究领域：Sulfur Compounds in Biology、Redox biology and oxidative stress、Glutathione Transferases and Polymorphisms

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.