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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A molecular view on signal transduction by the apoptosome.
In general, intrinsic apoptosis is a mitochondrion-centered cell death that is mediated by mitochondrial outer membrane permeabilization, and results in apoptosome formation, activation of caspase-9, and subsequent activation of effector caspases.
Consequently, pores are formed to leak the components of apoptosome from mitochondrial intermembrane space [93].
Scientists from Australia, Europe, the US, and Canada address the biochemical and morphological changes that occur during apoptosis, autophagy, necrosis, and other forms of cell death, and provide 69 protocols that use flow cytometry, imaging and microscopy, RNAi, western blotting, enzymatic activity measurements, and other tools to assess DNA fragmentation, lysosomal membrane permeabilization, autophagic flux, apoptosome or ripotosome formation, caspase activation, and cytochrome c release for in vitro systems and in vivo models, including mice, C.
HSP70 blocks apoptosis by binding apoptosis activating factor-1 (Apaf-1), thereby preventing the formation of the apoptosome complex (Ravagnan et al.
Cytochrome c recruits Apaf-1 and pro-caspase-9 to compose the apoptosome, which triggers a caspase 9/3 signaling cascade, culminating in apoptosis.
Cytochrome C combines with apoptosis activating factor 1 and the initiator caspase-9, to form apoptosome.
Once assembled, the apoptosome processes and activates procaspase-9 as the initiator caspase, which in turn proteolytically activates the executioner procaspase-3 and procaspase-7.
The mitochondrion plays an important role in apoptosis through the release of cytochrome c, the formation of an apoptosome, and subsequent activation of caspases (27), as well as through caspase independent mechanisms.
2000) Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome.

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