CASP10

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CASP10

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. CASP10 is an initiator-type caspase which is activated by, and interacts with, upstream adaptor molecules through CARD and DED protein–protein interaction domains. It cleaves and activates caspase-3, -4, -6, -7, -8 and -9, is recruited to Fas- and TNFR-1 receptors in a FADD-dependent manner, and may participate in the granzyme B apoptotic pathways. It is expressed in most tissues. CASP10 is also a less preferred gene symbol for what is now designated PPIG, see there. 

Molecular pathology
Defects in CASP10 have been linked to gastric cancer, non-Hodgkin lymphoma and autoimmune lymphoproliferative syndrome type 2A.
References in periodicals archive ?
However, the expression of Caspase-10 was found to be only 2.86 folds as compared with the normal control group.
Granzyme B, the prototype of serine proteases, promote cleavage and activate several caspases, including caspase-3, caspase-6, caspase-7, caspase-8, caspase-9, and caspase-10 [9].
Executioner caspases (caspase-3, caspase-6, and caspase-7) and upstream effector caspases (caspase-2, caspase-8, caspase-9, and caspase-10) are well known as mediators in AD brains [23].
In this experimental setting, we used, in addition to a pan-caspase inhibitor (Z-VAD-FMK), inhibitors of CASP8 (Z-IETD-FMK), CASP9 (Z-LEHD-FMK), and caspase-10 (CASP10; Z-AEVD-FMK) (R&D Systems, Minneapolis, MN, USA).
Together with caspase-10 it belongs to the so-called initiator caspase group, and is important effector activation competent.
The extrinsic pathway is triggered when death ligands bind to their respective cell surface death receptors through recruitment of FAS-associated death domain (FADD) protein, procaspase-8 through the formation of a complex that induces cell death and activation of the caspases (caspase-8 and caspase-10).
FasL expression was up-regulated by taiwanin A at both the transcriptional and translational levels, following the activation of caspase initiator caspase-10 and effector caspase-7.
To evaluate the involvement of caspases in PCL-induced cell death, five caspase inhibitors, z-DEVD-fmk (caspase-3 inhibitor), z-IETD-fmk (caspase-8 inhibitor), z-LEHD-fmk (caspase-9 inhibitor), z-AEVD-fmk (caspase-10) and z-VAD-fmk (pan-caspase inhibitor) were applied.
In the extrinsic way, the apoptotic signal begins by the union of extra cellular ligands to the surface of cell receptors, resulting in a recruitment of the cytosolic adapter of proteins, that activates the caspase-8 or caspase-10 initiator, and subsequently, the caspases effectors -3, -7 and possibly -6.
The cells were incubated with z-DEVD-fmk (caspase-3 inhibitor, 20 [micro]mol/1), z-IETD-fmk (caspase-8 inhibitor, 20 [micro]mol/[1.sup.-1]), z- LEHD-fmk (caspase-9 inhibitor, 20 [micro]mol/1), z-AEVD-fmk (caspase-10 inhibitor, 20 [micro]mol/1) and z-VAD-fmk (pan-caspase inhibitor, 20 [micro]mol/1) for 1 h, and then treated with SFL for 24 h.

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