Hepatocyte growth factor protects against hypoxia/reoxygenation-induced apoptosis in endothelial cells

J Biol Chem. 2004 Feb 13;279(7):5237-43. doi: 10.1074/jbc.M309271200. Epub 2003 Nov 18.

Abstract

Hypoxia/reoxygenation causes cellular injury and death associated with a number of pathophysiological conditions, including myocardial ischemia/reperfusion injury and stroke. The cell death pathways induced by hypoxia/reoxygenation and their underlying regulatory mechanisms remain poorly understood. Recent studies have shown that hypoxia/reoxygenation can induce Bax translocation and cytochrome c release. Using murine lung endothelial cells as a model, we found that the induction of apoptosis by hypoxia/reoxygenation involved the activation of both Bax-dependent and death receptor-mediated pathways. We demonstrated the activation of the death-inducing signal complex and Bid pathway after hypoxia/reoxygenation. Hepatocyte growth factor markedly inhibited hypoxia/reoxygenation-induced endothelial cell apoptosis. The cytoprotection afforded by hepatocyte growth factor was mediated in part by the stimulation of FLICE-like inhibiting protein expression, the attenuation of death-inducing signal complex formation, and the inhibition of Bid and Bax activation. Hepatocyte growth factor also prevented cell injury and death by increasing the expression of the antiapoptotic Bcl-XL protein. The inhibition of Bid/Bax-induced cell death by hepatocyte growth factor primarily involved p38 MAPK and in part Akt-dependent pathways but not ERK1/ERK2.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Apoptosis*
  • BH3 Interacting Domain Death Agonist Protein
  • Blotting, Western
  • Carrier Proteins / metabolism
  • Caspase 8
  • Caspases / metabolism
  • Cell Death
  • Cells, Cultured
  • Down-Regulation
  • Endothelial Cells / cytology*
  • Endothelial Cells / pathology
  • Enzyme Activation
  • Enzyme Inhibitors / pharmacology
  • Hepatocyte Growth Factor / metabolism*
  • Hypoxia*
  • Lung / cytology
  • Mice
  • Mitochondria / metabolism
  • Mitogen-Activated Protein Kinase 1 / metabolism
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases / metabolism
  • Oxygen / metabolism*
  • Protein Transport
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • Time Factors
  • Up-Regulation
  • bcl-2-Associated X Protein
  • bcl-X Protein
  • p38 Mitogen-Activated Protein Kinases

Substances

  • BH3 Interacting Domain Death Agonist Protein
  • Bax protein, mouse
  • Bcl2l1 protein, mouse
  • Bid protein, mouse
  • Carrier Proteins
  • Enzyme Inhibitors
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • bcl-2-Associated X Protein
  • bcl-X Protein
  • Hepatocyte Growth Factor
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases
  • Casp8 protein, mouse
  • Caspase 8
  • Caspases
  • Oxygen