Mechanisms of cell protection by heme oxygenase-1

  • Annu Rev Pharmacol Toxicol. 2010;50:323-54. doi: 10.1146/annurev.pharmtox.010909.105600.
Raffaella Gozzelino  1 ,  Viktoria Jeney ,  Miguel P Soares
Affiliations
  • 1. Instituto Gulbenkian de Ciência, Oeiras, Portugal.
PMID: 20055707 DOI: 10.1146/annurev.pharmtox.010909.105600
Abstract

Heme oxygenases (HO) catabolize free heme, that is, iron (Fe) protoporphyrin (IX), into equimolar amounts of Fe(2+), carbon monoxide (CO), and biliverdin. The stress-responsive HO-1 isoenzyme affords protection against programmed cell death. The mechanism underlying this cytoprotective effect relies on the ability of HO-1 to catabolize free heme and prevent it from sensitizing cells to undergo programmed cell death. This cytoprotective effect inhibits the pathogenesis of a variety of immune-mediated inflammatory diseases.