apoptosome


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apoptosome

(ă-pop'tō-sōm),
A heptameric apoptotic protease activating factor 1 (Apaf-1)-cytochrome-c complex. The apoptosome recruits and activates caspases that cleave intracellular substrates and ultimately lead to cell death by apoptosis. Release of mitochondrial cytochrome-c into the cytoplasm results in binding with monomers of Apaf-1, thereby inducing a conformational change that permits a stable association with (deoxy)adenosine triphosphate and formation of the heptameric complex.
See also: apoptosis.
[apoptosis + -some]
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If cytochrome c is released from mitochondria due to formation of a channel, in the outer mitochondrial membrane during the apoptosis process, it binds to apoptotic protease activating factor-1 (Apaf-1) and ATP, which then bind to pro-caspase-9 creating a protein complex known as apoptosome (Dejean et al.
In the Intrinsic pathway, the release of cytochrome c from the mitochondria into the cytosol is fundamental to apoptosome formation and downstream caspase activation.
If cytochrome c is released from mitochondria due to formation of a channel in the outer mitochondrial membrane during the apoptosis process, it binds to apoptotic protease activating factor-1 (Apaf-1) and ATP, which then bind to procaspase-9 creating a protein complex known as apoptosome (Dejean et al.
In the absence of apoptosis stimulation, intrinsic activation of apoptosis can be achieved by the initiation of caspase 9 and apoptosome formation which triggers the activation of downstream caspases.
After treatment of cells with apoptotic agents including H202, cytochrome c is released from mitochondrial intermembrane space and binds to the apoptosis protease activation factor (APAf-1) to forms an apoptosome complex.
The mitochondria-mediated pathway involves the release of cytochrome c, and then followed by the formation of apoptosome, a 140-kDa cytoplasmic complex, consisting of Apaf-1 (apoptotic protease-activation factor-1), dATP, cytochrome c, and procaspase-9, which results in activation of caspase-9 and in turn, activating caspase-3 and final fragmentation of DNA.
In cytoplasm, cytochrome c is known to become associated with caspase-9, Apaf-1 and dATP to form the apoptosome complex (Chinnaiyan, 1999), which in turn activates caspase- 9, -3 and -7.
Interaction of Cyt c with a cytosolic apoptosis protease activating factor, Apaf-1, induces recruitment of procaspase 9 into a high-molecular-weight complex, termed the apoptosome, which gives rise to activated caspase-9 and -3.
The released cytochrome c binds to, and activates the adaptor protein Apaf-1, which in turn activates caspase-9, leading to the formation of an apoptosome and subsequent activation of downstream caspases, such as caspase-3 (Wang, 2001).
2000) Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome.
The study, entitled "Variants in Apaf-1 Segregating with Major Depression Promote Apoptosome Function," is to be published in the scientific journal, Molecular Psychiatry, Vol.

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