title: Mechanisms of cell protection by heme oxygenase-1.
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.
authors.affiliation: Instituto Gulbenkian de Ciência, Oeiras, Portugal.
authors.forename: Raffaella
authors.initials: R
authors.lastname: Gozzelino
authors.forename: Viktoria
authors.initials: V
authors.lastname: Jeney
authors.forename: Miguel P
authors.initials: MP
authors.lastname: Soares
mesh_terms: D000818:Animals; D017209:Apoptosis / Q000187:drug effects; D001664:Biliverdine / Q000502:physiology; D002248:Carbon Monoxide / Q000502:physiology; D019610:Cytoprotection; D015971:Gene Expression Regulation, Enzymologic; D006418:Heme / Q000378:metabolism / Q000633:toxicity; D051547:Heme Oxygenase-1 / Q000235:genetics / Q000502:physiology*; D006801:Humans; D007249:Inflammation / Q000517:prevention & control; D014409:Tumor Necrosis Factor-alpha / Q000494:pharmacology
chemical_list: D014409:Tumor Necrosis Factor-alpha; D006418:Heme; D002248:Carbon Monoxide; D051547:Heme Oxygenase-1; D001664:Biliverdine