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 ?
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).
The resulting events pursue in cascades that caspase-8 induces activation of caspase-3 [11].
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].
According to literature, knockdown of caspase-8 in L929 cells triggers TNF[alpha]-induced necroptosis due to the absence of caspase-8-mediated inactivation of RIP1 and RIP3 [43].
Caspase-8 triggers the production of inflammatory proteins that typically allow mammals to fight microbial infections.
The aim of this study was to evaluate the expression of proteins: FHIT, E-cadherin, [alpha]-catenin, [gamma]-catenin, cathepsin B, EGF, HER-2, MMP-9, MCM-2, Bak, Bax, BID, Bcl-XL, p53, FasL, Bcl-2, caspase-8, procaspase-3 in gastric cancer cells, depending on the type of tumor by Lauren classification.
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).
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.
Oligomerization of procaspase-8 in the DISC leads to self activation with release of active caspase-8 in to the cytosol.
Cleaved caspase-8 levels decreased significantly at all times, while cleaved caspase-3 was significantly decreased at 45 minutes.
In the extrinsic pathway, binding of the death receptors causes activation of caspase-8, an initiator caspase.

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