title: Molecular oxygen sensing: implications for visceral surgery.
abstract: BACKGROUND
  Since mammalian cells rely on the availability of oxygen, they have devised mechanisms to sense environmental oxygen tension, and to efficiently counteract oxygen deprivation (hypoxia). These adaptive responses to hypoxia are essentially mediated by hypoxia inducible transcription factors (HIFs). Three HIF prolyl hydroxylase enzymes (PHD1, PHD2 and PHD3) function as oxygen sensing enzymes, which regulate the activity of HIFs in normoxic and hypoxic conditions. Many of the compensatory functions exerted by the PHD-HIF system are of immediate surgical relevance since they regulate the biological response of ischemic tissues following ligation of blood vessels, of oxygen-deprived inflamed tissues, and of tumors outgrowing their vascular supply.
  
  
  OBJECTIVE
  Here, we outline specific functions of PHD enzymes in surgically relevant pathological conditions, and discuss how these functions might be exploited in order to support the treatment of surgically relevant diseases.
authors.affiliation: Department of General, Visceral and Transplantation Surgery, University of Heidelberg, Im Neuenheimer Feld 110, 69120 Heidelberg, Germany.
authors.forename: Judit
authors.initials: J
authors.lastname: Kiss
authors.forename: Johanna
authors.initials: J
authors.lastname: Kirchberg
authors.forename: Martin
authors.initials: M
authors.lastname: Schneider
mesh_terms: D000008:Abdominal Neoplasms / Q000098:blood supply / Q000235:genetics; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D016923:Cell Death / Q000235:genetics / Q000502:physiology; D015687:Cell Hypoxia / Q000235:genetics* / Q000502:physiology*; D049308:Dioxygenases / Q000235:genetics* / Q000502:physiology*; D004734:Energy Metabolism / Q000235:genetics / Q000502:physiology; D006706:Homeostasis / Q000235:genetics / Q000502:physiology; D006801:Humans; D064799:Hypoxia-Inducible Factor-Proline Dioxygenases; D007113:Immunity, Innate / Q000235:genetics / Q000502:physiology; D009687:Nuclear Proteins / Q000235:genetics* / Q000502:physiology*; D011393:Procollagen-Proline Dioxygenase / Q000235:genetics* / Q000502:physiology*; D017382:Reactive Oxygen Species / Q000378:metabolism; D015427:Reperfusion Injury / Q000235:genetics / Q000503:physiopathology; D014157:Transcription Factors / Q000235:genetics* / Q000502:physiology*; D014781:Viscera / Q000098:blood supply* / Q000601:surgery*
chemical_list: D009687:Nuclear Proteins; D017382:Reactive Oxygen Species; D014157:Transcription Factors; D000255:Adenosine Triphosphate; D049308:Dioxygenases; C490190:EGLN1 protein, human; D011393:Procollagen-Proline Dioxygenase; C447780:EGLN2 protein, human; C488894:EGLN3 protein, human; D064799:Hypoxia-Inducible Factor-Proline Dioxygenases