Heme oxygenase-1: from biology to therapeutic potential

Trends Mol Med. 2009 Feb;15(2):50-8. doi: 10.1016/j.molmed.2008.12.004. Epub 2009 Jan 21.

Abstract

Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase). Over the past few years it has become apparent that these 'arms' of the HO-1 system can act protectively in a variety of experimental models of disease; there is also evidence that HO-1 and bilirubin have protective actions in humans. Here, we present a model for the beneficial actions of the products of heme degradation, and we discuss the potential clinical applications of enhancing the HO-1 system.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bilirubin / metabolism
  • Biliverdine / metabolism
  • Carbon Monoxide / metabolism
  • Disease*
  • Enzyme Induction
  • Evolution, Molecular
  • Heme / metabolism
  • Heme Oxygenase-1 / chemistry
  • Heme Oxygenase-1 / metabolism*
  • Homeostasis*
  • Humans
  • Models, Molecular
  • Protein Structure, Tertiary

Substances

  • Heme
  • Carbon Monoxide
  • Heme Oxygenase-1
  • Biliverdine
  • Bilirubin