H₂S signalling through protein sulfhydration and beyond.
Hydrogen sulfide (H(2)S) has recently emerged as a mammalian gaseous messenger molecule, akin to nitric oxide and carbon monoxide. H(2)S is predominantly formed from Cys or its derivatives by the enzymes cystathionine β-synthase and cystathionine γ-lyase. One of the mechanisms by which H(2)S signals is by sulfhydration of reactive Cys residues in target proteins. Although analogous to protein nitrosylation, sulfhydration is substantially more prevalent and usually increases the catalytic activity of targeted proteins. Physiological actions of sulfhydration include the regulation of inflammation and endoplasmic reticulum stress signalling as well as of vascular tension.
Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Bindu D
BD
Paul
Solomon H
SH
Snyder
D000818:Animals; D003541:Cystathionine beta-Synthase / Q000737:chemistry / Q000378:metabolism*; D003542:Cystathionine gamma-Lyase / Q000737:chemistry / Q000378:metabolism*; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D059865:Endoplasmic Reticulum Stress / Q000502:physiology; D005740:Gases / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D006862:Hydrogen Sulfide / Q000737:chemistry / Q000378:metabolism*; D007249:Inflammation / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction; D014664:Vasodilation / Q000502:physiology
D005740:Gases; D011506:Proteins; D003541:Cystathionine beta-Synthase; D003542:Cystathionine gamma-Lyase; D003545:Cysteine; D006862:Hydrogen Sulfide