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Hydrogen sulfide as a gasotransmitter
Author(s) -
Gadalla Moataz M.,
Snyder Solomon H.
Publication year - 2010
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2010.06580.x
Subject(s) - cystathionine beta synthase , cystathionine gamma lyase , hydrogen sulfide , nitric oxide , chemistry , biochemistry , s nitrosylation , nitric oxide synthase , enzyme , nitric oxide synthase type iii , nitrosylation , microbiology and biotechnology , enos , cysteine , biology , sulfur , organic chemistry
J. Neurochem. (2010) 10.1111/j.1471‐4159.2010.06580.x Abstract Nitric oxide (NO) and carbon monoxide (CO) are well established as messenger molecules throughout the body, gasotransmitters, based on striking alterations in mice lacking the appropriate biosynthetic enzymes. Hydrogen sulfide (H 2 S) is even more chemically reactive, but until recently there was little definitive evidence for its physiologic formation. Cystathionine β‐synthase (EC 4.2.1.22), and cystathionine γ‐lyase (CSE; EC 4.4.1.1), also known as cystathionine, can generate H 2 S from cyst(e)ine. Very recent studies with mice lacking these enzymes have established that CSE is responsible for H 2 S formation in the periphery, while in the brain cystathionine β‐synthase is the biosynthetic enzyme. Endothelial‐derived relaxing factor activity is reduced 80% in the mesenteric artery of mice with deletion of CSE, establishing H 2 S as a major physiologic endothelial‐derived relaxing factor. H 2 S appears to signal predominantly by S ‐sulfhydrating cysteines in its target proteins, analogous to S ‐nitrosylation by NO. Whereas S ‐nitrosylation typically inhibits enzymes, S ‐sulfhydration activates them. S ‐nitrosylation basally affects 1–2% of its target proteins, while 10–25% of H 2 S target proteins are S ‐sulfhydrated. In summary, H 2 S appears to be a physiologic gasotransmitter of comparable importance to NO and carbon monoxide.