H2S biosynthesis and catabolism: new insights from molecular studies

Cell Mol Life Sci. 2017 Apr;74(8):1391-1412. doi: 10.1007/s00018-016-2406-8. Epub 2016 Nov 14.

Abstract

Hydrogen sulfide (H2S) has profound biological effects within living organisms and is now increasingly being considered alongside other gaseous signalling molecules, such as nitric oxide (NO) and carbon monoxide (CO). Conventional use of pharmacological and molecular approaches has spawned a rapidly growing research field that has identified H2S as playing a functional role in cell-signalling and post-translational modifications. Recently, a number of laboratories have reported the use of siRNA methodologies and genetic mouse models to mimic the loss of function of genes involved in the biosynthesis and degradation of H2S within tissues. Studies utilising these systems are revealing new insights into the biology of H2S within the cardiovascular system, inflammatory disease, and in cell signalling. In light of this work, the current review will describe recent advances in H2S research made possible by the use of molecular approaches and genetic mouse models with perturbed capacities to generate or detoxify physiological levels of H2S gas within tissues.

Keywords: Biosynthesis; Catabolism; Hydrogen sulfide; Molecular models.

Publication types

  • Review

MeSH terms

  • Animals
  • Biosynthetic Pathways*
  • Carbon-Oxygen Lyases / genetics
  • Carbon-Oxygen Lyases / metabolism
  • Cystathionine beta-Synthase / genetics
  • Cystathionine beta-Synthase / metabolism
  • Cysteine Dioxygenase / genetics
  • Cysteine Dioxygenase / metabolism
  • Dioxygenases / genetics
  • Dioxygenases / metabolism
  • Gene Expression Regulation
  • Gene Knockout Techniques / methods
  • Humans
  • Hydrogen Sulfide / metabolism*
  • Mitochondrial Proteins / genetics
  • Mitochondrial Proteins / metabolism
  • Quinone Reductases / genetics
  • Quinone Reductases / metabolism
  • Signal Transduction
  • Sulfurtransferases / genetics
  • Sulfurtransferases / metabolism

Substances

  • Mitochondrial Proteins
  • Dioxygenases
  • ETHE1 protein, mouse
  • Cysteine Dioxygenase
  • Quinone Reductases
  • sulfide quinone reductase
  • O-succinylhomoserine (thiol)-lyase
  • Sulfurtransferases
  • 3-mercaptopyruvate sulphurtransferase
  • Carbon-Oxygen Lyases
  • Cystathionine beta-Synthase
  • Hydrogen Sulfide