Oxidoreduction of protein thiols in redox regulation.
Protein cysteines can undergo various forms of oxidation, some of them reversible (disulphide formation, glutathionylation and S-nitrosylation). While in the past these were viewed as protein damage in the context of oxidative stress, there is growing interest in oxidoreduction of protein thiols/disulphides as a regulatory mechanism. This review discusses the evolution of the concept of redox regulation from that of oxidative stress and the redox state of protein cysteines in different cellular compartments.
Ghezzi
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Mario Negri Institute, via Eritrea 62, 20157 Milan, Italy. ghezzi@marionegri.it
D000975:Antioxidants; D003545:Cysteine / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry; D054477:Glutaredoxins; D005978:Glutathione / Q000378:metabolism; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010088:Oxidoreductases / Q000378:metabolism; D011506:Proteins / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D013879:Thioredoxins / Q000378:metabolism
D000975:Antioxidants; D004220:Disulfides; D054477:Glutaredoxins; D011506:Proteins; D013438:Sulfhydryl Compounds; D013879:Thioredoxins; D010088:Oxidoreductases; D005978:Glutathione; D003545:Cysteine