CASP9

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CASP9

A gene on chromosome 1p36.21 that encodes a ubiquitous protein belonging to the cysteine-aspartic acid protease (caspase) family which, once activated by proteolytic processing, plays a central role in the execution phase of cell apoptosis. CASP9 is an initiator-type caspase, which is activated by, and interacts with, upstream adaptor molecules through CARD and DED protein–protein interaction domains; it is processed by APAF1, an early step in the caspase activation cascade. It is highly expressed in the heart.
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The intrinsic pathway is begun by changes in mitochondrial permeability and the activation of caspase-9 and caspase-3.
In addition, trifolin increased the levels of the death receptor involving the Fas/Fas ligand (FasL) and Fas-associated protein with the death domain (FADD), which consequently activated caspase-8, caspase-9, caspase-3, and the proteolytic cleavage of poly (ADP-ribose) polymerase (PARP).
Caspase-3 is activated by the upstream caspase-8 and caspase-9, and accordingly it serves as a convergence point for different signaling pathways [1].
Sal protects against MPTP-induced toxicity in part through the regulation of the PI3K/Akt/GSK3[beta] signaling pathway, the upregulation of Bcl-2/Bax ratio, and the inhibition of the cleavage of caspase-3, caspase-6, and caspase-9.
Antibodies against disulfidebond A oxidoreductase-like protein (DsbA-L) and CTRP9 were bought from Santa Cruz Biotechnology (Santa Cruz, CA, USA); antibodies against CHOP, GRP-78, TNF-[alpha], Caspase-3, Caspase-9, Caspase-12, and GAPDH were from Cell Signaling Technology (Beverly, MA, USA).
Additionally, polysaccharide extracted induced intrinsic apoptosis via up-regulation of caspase-3, caspase-9 and Bax along with down-regulation of Bcl-2 in HeLa cells.
Apoptosis is classically signalled by two major apoptotic pathways (12) (Figure 2): the extrinsic pathway (also called the death receptor caspase-8 mediated pathway) and the intrinsic pathway (also called mitochondria-initiated caspase-9 pathway).
As a consequence, cleaved caspase-9 and cleaved caspase-7 levels were significantly downregulated, indicating negative regulation of apoptosis by COC extract.
Enucleated eyes were preserved for histological analysis, immunohistochemical analysis of caspase-3, caspase-8, caspase-9, Fas/Fas L, VEGF and VEGF receptors (Flt-1, Flk-1), and TUNEL staining.
Mitochondrial proteins that cause caspase-dependent cell death include cytochrome C (Cyt C), which triggers caspase-9 activation by binding and activating the apoptotic protease activating factor-1 (Apaf-1), and Smac/Diablo, which potentiates caspase activation by binding inhibitor of apoptosis proteins (IAP) and blocking their caspase-inhibitory activity.
The findings provide the first example of a protein factor regulating the expression of the protein caspase-9, a main player in apoptosis, or programmed cell death.
This procaspase-9 comes and activates caspase-9 and simultaneously this activates procaspase-3 and then activates caspase-3.

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