procaspases


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procaspases

(prō'kas-pās-ĕz),
Inactive precursors of caspases.
See also: caspases.
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The DISC facilitates the autoproteolytic rupture of procaspase 8, which is responsible for its enzymatic activity and its release that leads to the activation of downstream caspases in the signaling pathway (caspases 3, 6, and 7).
The formation of this complex is highly regulated by mutual ubiquitination and phosphorylation of proteins RIP1 and RIP3, which are part of this complex, as well as FADD, TRADD, and procaspase 8 [84].
Caspase-8 then activates other procaspases, culminating in cleavage of cellular substrates, and apoptosis.
2-(4-benzylpiperazin-1-yl)-N-[(2-hydroxy-3-prop-2-enyl phenyl) methylideneamino] acetamide (procaspase activating compound-1 or PAC-1) plays a role to activate procaspase-3 indiscriminately.
Apoptogenic factors are released from the mitochondrial intermembrane fraction, including 2 caspase activators (cytochrome c and Smac/Diablo), an apoptosis-inducing factor, and procaspase 2, 3, and 9.
(101-115) Heat shock protein 7 inhibits apoptosis by binding directly to Apaf-1 and blocking the assembly of the apoptosome composed of cytochrome c, procaspase 9, adenosine triphosphate, and Apaf-1.