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- W1987126302 endingPage "149" @default.
- W1987126302 startingPage "139" @default.
- W1987126302 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." @default.
- W1987126302 created "2016-06-24" @default.
- W1987126302 creator A5026533834 @default.
- W1987126302 creator A5035904189 @default.
- W1987126302 creator A5060243172 @default.
- W1987126302 date "1998-08-01" @default.
- W1987126302 modified "2023-10-16" @default.
- W1987126302 title "Mitochondrial control of apoptosis: the role of cytochrome c" @default.
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