Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

Article Abstract:

Bcl-2 family proteins may target voltage-dependent anion channel (VDAC) directly in order to modulate channel activity. It is probable that Bax/Bak prompts a conformational change in VDAC, thus allowing the cytochrome c to pass through the channel. However, it is also possible that Bax/Bak and VDAC could together create a larger channel. It appears that the Bcl-2 family of proteins target VDAC to regulate apoptosis-associated mitochondrial changes that play a key role in determining cell survival or death.

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Prevention of hypoxia-induced cell death by Bcl-2 and Bcl-xL

Article Abstract:

Bcl-2 and Bcl-xL controls the proteases present in the cell which might be how they prevent death due to oxygen withdrawal. In this type of cell death the amount of free oxygen radicals formed becomes less which affects the oxidation of lipids, proteins and DNA in the cell. The prevention of hypoxia-induced death by Bcl-2 and Bcl-xL is not because of their action on reactive oxygen species (ROS) since ROS is not involved even in very small amounts.

Proto-oncogenes

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Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation

Article Abstract:

Apoptosis is distinguished by changes including nuclear chromatin condensation and nuclear fragmentation, but the molecular basis of these events is still unclear. A new nuclear factor, named Acinus, has been identified which is necessary for apoptotic chromatin condensation, but not for DNA fragmentation. The new factor is present in the nucleus and activated through cleavage during apoptosis.

Chromatin, Proteases

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