Bcl-2 and the outer mitochondrial membrane in the inactivation of cytochrome c during Fas-mediated apoptosis

J Biol Chem. 1997 Aug 29;272(35):21878-82. doi: 10.1074/jbc.272.35.21878.

Abstract

Fas-driven apoptosis in Jurkat cells results in the inactivation of cytochrome c with cessation of oxygen consumption. Overexpression of Bcl-2 was found to protect against acidification and apoptosis mediated by Fas ligation in these cells. Bcl-2 is present in the outer mitochondrial membrane, but the molecular mechanism by which it protects cells is unknown. Because Bcl-2 projects into the mitochondrial intermembrane space and cytochrome c is located in the intermembrane space, we considered the possibility that Bcl-2 might protect cytochrome c from inactivation during Fas-mediated apoptosis. The present study shows that 1) in Jurkat cells, cytochrome c inactivation during Fas-driven apoptosis requires the permeabilization of the outer mitochondrial membrane; and 2) the post-mitochondrial fraction from CEM cells that overexpress Bcl-2 both prevents and reverses cytochrome c inactivation.

Publication types

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

MeSH terms

  • Apoptosis*
  • Cytochrome c Group / antagonists & inhibitors*
  • Electron Transport
  • Humans
  • Hydrogen-Ion Concentration
  • Intracellular Membranes / metabolism*
  • Jurkat Cells
  • Mitochondria / metabolism*
  • Oxygen Consumption
  • Permeability
  • Proto-Oncogene Proteins c-bcl-2 / metabolism*
  • fas Receptor / metabolism*

Substances

  • Cytochrome c Group
  • Proto-Oncogene Proteins c-bcl-2
  • fas Receptor