Mitochondrial control of apoptosis: the role of cytochrome c

Mitochondrial control of apoptosis: the role of cytochrome c Mitochondrial cytochrome c (cyt c ) has been found to have dual functions in controlling both cellular energetic metabolism and apoptosis. Through interaction with apoptotic protease activating factors (Apaf), cyt c can initiate the activation cascade of caspases once it is released into the cytosol. The loss of a component of the mitochondrial electron transport chain also triggers the generation of superoxide. Although cyt c can be released independent of the mitochondrial permeability transition (MPT), the accompanying cellular redox change can trigger the MPT. Since another apoptotic protease, AIF, is released by MPT, the two separate pathways provide redundancy that ensures effective execution of the cell death program. Anti-apoptotic Bcl-2 family proteins function as gatekeepers to prevent the release of both cyt c and AIF. In spite of their stabilization effect on the mitochondrial outer membrane, Bcl-2 proteins may also be involved in the direct binding of Apaf molecules as regulatory elements further downstream from the mitochondrial apoptotic signals. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biochimica et Biophysica Acta (BBA) - Bioenergetics Elsevier

Mitochondrial control of apoptosis: the role of cytochrome c

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Publisher
Elsevier
Copyright
Copyright © 1998 Elsevier Science B.V.
ISSN
0005-2728
DOI
10.1016/S0005-2728(98)00109-1
Publisher site
See Article on Publisher Site

Abstract

Mitochondrial cytochrome c (cyt c ) has been found to have dual functions in controlling both cellular energetic metabolism and apoptosis. Through interaction with apoptotic protease activating factors (Apaf), cyt c can initiate the activation cascade of caspases once it is released into the cytosol. The loss of a component of the mitochondrial electron transport chain also triggers the generation of superoxide. Although cyt c can be released independent of the mitochondrial permeability transition (MPT), the accompanying cellular redox change can trigger the MPT. Since another apoptotic protease, AIF, is released by MPT, the two separate pathways provide redundancy that ensures effective execution of the cell death program. Anti-apoptotic Bcl-2 family proteins function as gatekeepers to prevent the release of both cyt c and AIF. In spite of their stabilization effect on the mitochondrial outer membrane, Bcl-2 proteins may also be involved in the direct binding of Apaf molecules as regulatory elements further downstream from the mitochondrial apoptotic signals.

Journal

Biochimica et Biophysica Acta (BBA) - BioenergeticsElsevier

Published: Aug 10, 1998

References

  • Biochim. Biophys. Acta
    Jones, D.P.
  • Lancet
    Linnane, A.W.; Marzuki, S.; Ozawa, T.; Tanaka, M.
  • J. Biol. Chem.
    Li, F.; Srinivasan, A.; Wang, Y.; Armstrong, R.C.; Tomaselli, K.J.; Fritz, L.C.

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