EC Number   |
Application |
Reference |
|---|
   3.4.22.63 | medicine |
in HL-60 cells that are treated with chemotherapy drugs combined with a caspase-10 inhibitor, the rate of survival decreases significantly compared with HL?60 cells treated with chemotherapy drugs alone. The rate of survival of Jurkat cells treated with chemotherapy drugs combined with the caspase-10 inhibitor increases significantly compared with Jurkat cells treated with chemotherapy drugs alone. Caspase-10 may be associated with autophagy in acute myeloid leukemia cells, but not in acute lymphatic leukemia cells |
754943 |
| 3.4.22.63 | medicine |
silencer of death domain and caspase-10 are frequently over-expressed in ALL. Interfering with these proteins may provide another strategy for the treatment of this and potentially other cancers |
732763 |
| 3.4.22.63 | medicine |
the apoptosis-inducing complex FADDosome is driven by ATR-dependent caspase-10 upregulation. During FADDosome-induced apoptosis, FLICE-inhibitory protein cFLIPL is ubiquitinated by TRAF2, leading to its degradation and subsequent adaptor protein FADD-dependent caspase-8 activation. Cancer cells lacking caspase-10, TRAF2 or ATR switch from this cell-autonomous suicide to a more effective, autocrine/paracrine mode of apoptosis initiated by a different complex, the FLIPosome. It leads to processing of cFLIPL to cFLIPp43, TNF-alpha production and consequently, contrary to the FADDosome, p53-independent apoptosis |
753179 |
| 3.4.22.63 | medicine |
two patients that are combined heterozygous for single nucleotide substitutions in the Fas and caspase-10 genes. The first patient carries a splice site defect suppressing allele expression in the Fas gene and the P501L substitution in caspase-10. The second has a mutation causing a premature stop codon (Q47X) in the Fas gene and the Y446C substitution in caspase-10. Fas expression is reduced and caspase-10 activity is decreased in both patients. In both patients, the mutations are inherited from distinct healthy parents. Co-transmission of these mutation is responsible for autoimmune lymphoproliferative syndrome |
678936 |
| 3.4.22.63 | pharmacology |
tumour necrosis factor-related apoptosis-inducing ligand and SMs effectively kill head and neck squamous cancer cell lines and therefore represent potential targeted therapeutics for head and neck cancer. Distinct molecular mechanisms determine the sensitivity to each agent, with levels of TNF-alpha, caspase-8, Bid and caspase-10 providing important predictive biomarkers of response to these agents |
731561 |
