Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling.

作者: T. Ida , T. Sawa , H. Ihara , Y. Tsuchiya , Y. Watanabe

DOI: 10.1073/PNAS.1321232111

关键词: Cystathionine gamma-lyaseBiochemistryEffectorReactive oxygen speciesCystathionine beta synthaseChemistryCysteineOxidative stressSulfurtransferaseSmall molecule

摘要: Using methodology developed herein, it is found that reactive persulfides and polysulfides are formed endogenously from both small molecule species proteins in high amounts mammalian cells tissues. These sulfur were biosynthesized by two major sulfurtransferases: cystathionine β-synthase γ-lyase. Quantitation of these indicates concentrations glutathione persulfide (perhydropersulfide >100 μM) other cysteine polysulfide derivatives peptides/proteins produced maintained the plasma, cells, tissues mammals (rodent human). It expected especially nucleophilic reducing. This view was to be case, because they quickly react with H2O2 a recently described biologically generated electrophile 8-nitroguanosine 3′,5′-cyclic monophosphate. results indicate potentially important signaling/effector species, H2S can degradation, much reported biological activity associated may actually persulfides. That is, act primarily as marker for active species.

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