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Caspase-10 is a negative regulator of cell death and a facilitator of gene induction separates the function of cFLIP (show CFLAR Proteins) and caspase-10 in the death-inducing signaling complex.
caspase-10 was dispensable for enhancement of cisplatin/LA-12 and TRAIL combination-induced cell death and stimulation of Bid (show BID Proteins) cleavage
This study reveals an essential role of SUMOylated FADD (show FADD Proteins) in Drp1 (show CRMP1 Proteins)- and caspase-10-dependent necrosis.
Three cases of autoimmune lymphoproliferative syndrome due to somatic FAS (show FAS Proteins) mutation (ALPS-sFAS) combined with a germline CASP10 variation have been described.
Levels of caspase-9 (show CASP9 Proteins), caspase-10, MAVS (show MAVS Proteins), and pIRF7 in mononuclear cells and the disease activity index (SLEDAI) in the systemic lupus erythematosus patients were determined.
Results showed miR (show MLXIP Proteins)-221/222 promote cell proliferation and repress apoptosis, through suppressing caspase-10, in prostate cancer cells.
We have also demonstrated that these correlations are tissue specific being reduced (CASP9 (show CASP9 Proteins) and CASP10) or different (CASP2 (show CASP2 Proteins)) in the liver
proinflammatory (caspase 1 (show CASP1 Proteins)) and initiator (caspases 8 and 10) caspases in the syncytiotrophoblast and capillary endotheliocytes of the terminal villi are higher in induced pregnancies.
Single nucleotide polymorphisms in CASP10 gene is associated with gastric cancer.
While myeloma cells require a basal level of autophagy for survival, caspase-10 tempers this response to avoid cell death.
This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 3 and 7, and the protein itself is processed by caspase 8. Mutations in this gene are associated with type IIA autoimmune lymphoproliferative syndrome, non-Hodgkin lymphoma and gastric cancer. Alternatively spliced transcript variants encoding different isoforms have been described for this gene.
, caspase 10, apoptosis-related cysteine protease
, FADD-like ICE2
, FAS-associated death domain protein interleukin-1B-converting enzyme 2
, ICE-like apoptotic protease 4
, apoptotic protease MCH-4
, interleukin-1B-converting enzyme 2