title: Heme oxygenase-1: a metabolic nike.
abstract: CONCLUSIONS
  Heme degradation, which was described more than 30 years ago, is still very actively explored with many novel discoveries on its role in various disease models every year.
  
  
  BACKGROUND
  The heme oxygenases (HO) are metabolic enzymes that utilize NADPH and oxygen to break apart the heme moiety liberating biliverdin (BV), carbon monoxide (CO), and iron. Heme that is derived from hemoproteins can be toxic to the cells and if not removed immediately, it causes cell apoptosis and local inflammation. Elimination of heme from the milieu enables generation of three products that influences numerous metabolic changes in the cell.
  
  
  RESULTS
  CO has profound effects on mitochondria and cellular respiration and other hemoproteins to which it can bind and affect their function, while BV and bilirubin (BR), the substrate and product of BV, reductase, respectively, are potent antioxidants. Sequestration of iron into ferritin and its recycling in the tissues is a part of the homeodynamic processes that control oxidation-reduction in cellular metabolism. Further, heme is an important component of a number of metabolic enzymes, and, therefore, HO-1 plays an important role in the modulation of cellular bioenergetics.
  
  
  CONCLUSIONS
  In this review, we describe the cross-talk between heme oxygenase-1 (HO-1) and its products with other metabolic pathways. HO-1, which we have labeled Nike, the goddess who personified victory, dictates triumph over pathophysiologic conditions, including diabetes, ischemia, and cancer.
authors.affiliation: 1 Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School , Boston, Massachusetts.
authors.forename: Barbara
authors.initials: B
authors.lastname: Wegiel
authors.forename: Zsuzsanna
authors.initials: Z
authors.lastname: Nemeth
authors.forename: Matheus
authors.initials: M
authors.lastname: Correa-Costa
authors.forename: Andrew C
authors.initials: AC
authors.lastname: Bulmer
authors.forename: Leo E
authors.initials: LE
authors.lastname: Otterbein
mesh_terms: D000818:Animals; D053898:Biosynthetic Pathways; D002248:Carbon Monoxide / Q000502:physiology; D019069:Cell Respiration; D003920:Diabetes Mellitus / Q000201:enzymology; D006418:Heme / Q000378:metabolism; D051547:Heme Oxygenase-1 / Q000502:physiology*; D006420:Hemeproteins / Q000378:metabolism; D006801:Humans; D007501:Iron / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D009369:Neoplasms / Q000201:enzymology
chemical_list: D006420:Hemeproteins; D006418:Heme; D002248:Carbon Monoxide; D007501:Iron; C496541:HMOX1 protein, human; D051547:Heme Oxygenase-1