H₂S signalling through protein sulfhydration and beyond

Nat Rev Mol Cell Biol. 2012 Jul 11;13(8):499-507. doi: 10.1038/nrm3391.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Cystathionine beta-Synthase / chemistry
  • Cystathionine beta-Synthase / metabolism*
  • Cystathionine gamma-Lyase / chemistry
  • Cystathionine gamma-Lyase / metabolism*
  • Cysteine* / chemistry
  • Cysteine* / metabolism
  • Endoplasmic Reticulum Stress / physiology
  • Gases / chemistry
  • Gases / metabolism
  • Humans
  • Hydrogen Sulfide / chemistry
  • Hydrogen Sulfide / metabolism*
  • Inflammation / metabolism
  • Proteins* / chemistry
  • Proteins* / metabolism
  • Signal Transduction
  • Vasodilation / physiology

Substances

  • Gases
  • Proteins
  • Cystathionine beta-Synthase
  • Cystathionine gamma-Lyase
  • Cysteine
  • Hydrogen Sulfide