EC Number   |
General Information |
Reference  |
|---|
   3.4.22.55 | physiological function |
caspases-2 and -8 are involved in the presenilin1/gamma-secretase-dependent cleavage of amyloid precursor protein after the induction of apoptosis |
709626 |
| 3.4.22.55 | physiological function |
The increased expression of PIDD (p53-induced protein with a death domain) induced by p53 forms a complex with RAIDD and caspase-2 (termed a PIDDosome), which activates the protease. The processed caspase-2 acts as a canonical caspase in the mitochondrial-mediated pathway triggering cytochrome c release. Once released to the cytoplasm, cytochrome c binds to APAF-1 to form a wheel-like complex, the apoptosome, resulting in the activation of caspase-9 and subsequent cleavage of downstream caspases including caspase-3. |
710625 |
| 3.4.22.55 | physiological function |
apoptosis induced by doxorubicin and 5-fluorouracil is caspase-2-dependent |
710904 |
| 3.4.22.55 | physiological function |
overview on the function of caspase-2 in cell death signaling |
711697 |
| 3.4.22.55 | physiological function |
discussion of the role of caspase-2 and potential contribution of the enzyme to the pathology of human diseases |
712556 |
| 3.4.22.55 | physiological function |
caspase-2 activation is commonly associated with induction of IFN-beta-induced apoptosis in IFN-beta-sensitive melanoma cells |
712665 |
| 3.4.22.55 | malfunction |
Casp2-null animals develop normally, and thymocytes and neurons derived from them seem to undergo similar levels of apoptosis to those from wild-type littermates. Nevertheless, several subtle phenotypes are associated with the Casp2-knockout mice: Casp2-knockout females have a slight increase in the number of oocytes and Casp2/ oocytes show reduced apoptosis in response to treatment with doxorubicin. The neurons derived from Casp2-null mice are resistant to beta-amyloid-mediated death, which suggests a role for caspase 2 in neuronal death. Casp2-deficient mice also show signs of premature ageing, including accumulation of oxidative damage. Mouse embryonic fibroblasts from Casp2-deficient animals show a reduced or delayed apoptotic response to some cytotoxic drugs, have an aberrant DNA damage and cell cycle response and are readily transformed when they are challenged by oncogene expression. |
713092 |
| 3.4.22.55 | physiological function |
caspase 2 is thought be a downstream caspase |
713092 |
| 3.4.22.55 | physiological function |
caspase 2 represses transcription of the survivin gene, a general regulator of cell division and cytoprotection in tumors. This pathway involves caspase 2 proteolytic cleavage of the nuclearfactor kappaB (NFkappaB) activator, RIP1. Loss of RIP1 abolishes transcription of NFkappaB target genes, including survivin, resulting in deregulated mitotic transitions, enhanced apoptosis and suppression of tumorigenicityin vivo. Caspase 2 functions as an endogenous inhibitor of NFkappaB-dependent cell survival. |
713154 |
| 3.4.22.55 | physiological function |
critical role of caspase-2 in mediating rough Brucella abortus induced macrophage cell death |
713348 |
