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- W2003014947 abstract "Hydrogen sulfide anion reacts with cellular electrophiles, including 8-nitro-cGMP, and sulfhydration products inhibit S-guanylation–dependent H-Ras activation in cardiac inflammatory injury models. An emerging aspect of redox signaling is the pathway mediated by electrophilic byproducts, such as nitrated cyclic nucleotide (for example, 8-nitroguanosine 3′,5′-cyclic monophosphate (8-nitro-cGMP)) and nitro or keto derivatives of unsaturated fatty acids, generated via reactions of inflammation-related enzymes, reactive oxygen species, nitric oxide and secondary products. Here we report that enzymatically generated hydrogen sulfide anion (HS−) regulates the metabolism and signaling actions of various electrophiles. HS− reacts with electrophiles, best represented by 8-nitro-cGMP, via direct sulfhydration and modulates cellular redox signaling. The relevance of this reaction is reinforced by the significant 8-nitro-cGMP formation in mouse cardiac tissue after myocardial infarction that is modulated by alterations in HS− biosynthesis. Cardiac HS−, in turn, suppresses electrophile-mediated H-Ras activation and cardiac cell senescence, contributing to the beneficial effects of HS− on myocardial infarction–associated heart failure. Thus, this study reveals HS−-induced electrophile sulfhydration as a unique mechanism for regulating electrophile-mediated redox signaling." @default.
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- W2003014947 date "2012-07-01" @default.
- W2003014947 modified "2023-10-17" @default.
- W2003014947 title "Hydrogen sulfide anion regulates redox signaling via electrophile sulfhydration" @default.
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- W2003014947 doi "https://doi.org/10.1038/nchembio.1018" @default.
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