Bcl-2 family members and functional electron transport chain regulate oxygen deprivation-induced cell death

Mol Cell Biol. 2002 Jan;22(1):94-104. doi: 10.1128/MCB.22.1.94-104.2002.

Abstract

The mechanisms underlying cell death during oxygen deprivation are unknown. We report here a model for oxygen deprivation-induced apoptosis. The death observed during oxygen deprivation involves a decrease in the mitochondrial membrane potential, followed by the release of cytochrome c and the activation of caspase-9. Bcl-X(L) prevented oxygen deprivation-induced cell death by inhibiting the release of cytochrome c and caspase-9 activation. The ability of Bcl-X(L) to prevent cell death was dependent on allowing the import of glycolytic ATP into the mitochondria to generate an inner mitochondrial membrane potential through the F(1)F(0)-ATP synthase. In contrast, although activated Akt has been shown to inhibit apoptosis induced by a variety of apoptotic stimuli, it did not prevent cell death during oxygen deprivation. In addition to Bcl-X(L), cells devoid of mitochondrial DNA (rho degrees cells) that lack a functional electron transport chain were resistant to oxygen deprivation. Further, murine embryonic fibroblasts from bax(-/-) bak(-/-) mice did not die in response to oxygen deprivation. These data suggest that when subjected to oxygen deprivation, cells die as a result of an inability to maintain a mitochondrial membrane potential through the import of glycolytic ATP. Proapoptotic Bcl-2 family members and a functional electron transport chain are required to initiate cell death in response to oxygen deprivation.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Antineoplastic Agents / pharmacology
  • Apoptosis / physiology*
  • Caspase 9
  • Caspases / metabolism
  • Cell Fractionation
  • Cell Line
  • Cytochrome c Group / metabolism
  • Doxorubicin / pharmacology
  • Electron Transport / physiology*
  • Glucose / metabolism
  • Humans
  • Membrane Potentials / physiology
  • Mitochondria / physiology
  • Oxygen / metabolism*
  • Protein Serine-Threonine Kinases*
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-akt
  • Proto-Oncogene Proteins c-bcl-2 / genetics
  • Proto-Oncogene Proteins c-bcl-2 / metabolism*
  • Rats
  • Reactive Oxygen Species / metabolism
  • bcl-X Protein

Substances

  • Antineoplastic Agents
  • BCL2L1 protein, human
  • Bcl2l1 protein, rat
  • Cytochrome c Group
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Reactive Oxygen Species
  • bcl-X Protein
  • Doxorubicin
  • Adenosine Triphosphate
  • AKT1 protein, human
  • Akt1 protein, rat
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt
  • CASP9 protein, human
  • Casp9 protein, rat
  • Caspase 9
  • Caspases
  • Glucose
  • Oxygen