Mechanisms of cell protection by heme oxygenase-1
Annual review of pharmacology and toxicology, 2010•annualreviews.org
Heme oxygenases (HO) catabolize free heme, that is, iron (Fe) protoporphyrin (IX), into
equimolar amounts of Fe2+, 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.
equimolar amounts of Fe2+, 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.
Heme oxygenases (HO) catabolize free heme, that is, iron (Fe) protoporphyrin (IX), into equimolar amounts of Fe2+, 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.
Annual Reviews