CASP8

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CASP8

A gene on chromosome 2q33-q34 that encodes a 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, as well as various stages of embryological development. CASP8 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 involved in the programmed cell death induced by Fas and various apoptotic stimuli. It is highly expressed in peripheral blood leukocytes and in the spleen, thymus and liver.

Molecular pathology
CASP8 has been detected in the insoluble fraction of affected brain regions in Huntington disease, suggesting a role in neurodegenerative diseases.
References in periodicals archive ?
The investigators discovered this second role for caspase-8 while studying a genetic condition known to exist in only two people--a brother and sister found to have a mutation in both copies of their caspase8 genes.
The repeats, consisting of multiple copies of the amino acid glutamine, convert caspase-8 into an active form, according to test tube studies performed by the researchers.
Expression of the A88V and G11R mutants resulted in elevated levels of the cleaved forms of caspase-3, caspase-8, caspase-9, and PARP, which are all markers of apoptotic activation while the same markers were unchanged in cells transfected with the negative control virus or the wild-type GJB6 gene.
Activity of caspase-3 (CASP3), caspase-8 (CASP8), and caspase-9 (CASP9) was measured using the Green Caspase Staining Kit (Promokine, Heidelberg, Germany) according to the manufacturer's protocol.
Upon binding with its specific ligand, TRAIL, TRAIL-R2 initiates the recruitment of Fas-associated protein with death domain (FADD) and signaling molecules (such as caspase-8) to form the death-inducing signaling complex (DISC).
Cell counting kit 8 (CCK-8) and caspase-3, caspase-8, and caspase-9 fluorescence metric assay kits were purchased from KeyGen BioTECH (Jiangsu, China).
To confirm that the subG1 portion observed in Hep3B cells shown in Figure 1 was due to apoptosis, caspase-3, caspase-8, and caspase-9 activities were analyzed by flow cytometry.
Zhuo, "HMGB1 promotes the activation of NLRP3 and caspase-8 inflammasomes via NF-[kappa]B pathway in acute glaucoma," Journal of Neuroinflammation, vol.
Recently, NleF has been reported to inhibit the catalytic activity of caspase-4, caspase-8, and caspase-9 [25].
In parallel, honokiol induced activations of caspase-8, -9, and -3, apoptosis, and G1 cell cycle arrest.
Basically, there are two main signaling pathways for cellular apoptosis: a) the mitochondrial or intrinsic pathway that responds to intracellular stimuli and results in cytochrome c release from the mitochondria leading to the activation of Caspase-9; and b) the extrinsic death receptor pathway initiated by ligand binding to extracellular cell death receptors resulting in caspase-8 activation.
Studies have indicated that Caspase-8 in external pathway and Caspase-9 in internal pathway act as crucial caspases.

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