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Related to CASPASE: Caspase 3, Caspase 9
CASPASECysteine Aspartic Acid Specific Protease
CASPASECleaving At Cysteine-Aspartic Residues
References in periodicals archive ?
Caspase activation and neuroprotection in caspase-3-deficient mice after in vivo cerebral ischemia and in vitro oxygen glucose deprivation.
Consequently, the apoptosis mechanism by extrinsic pathways was mediated by Caspase 8 and 9.
The caspases as a novel group of 10 cysteine proteases are the major enzymes involved in the process of apoptosis [21] and are responsible for execution of apoptosis [22].
Another immunocytochemical marker for apoptosis is cleaved caspase-3: Each caspase family protease becomes active when the precursor is cleaved into a large subunit with a molecular mass of ~20 kDa and a small subunit with a molecular mass of ~10 kDa, which then forms a tetramer consisting of two large and two small units [27,28].
Accordingly we examined the expression of P53 and Caspase 3 in the livers of mice having transperitoneally injected Ehrlich Ascites carcinoma cells and treated with Tetrodotoxin.
Administration of broad-spectrum caspase inhibitors reduces myocardial infarct size in mice following ischemia reperfusion [46-48].
Amer explains that these findings represent a paradigm shift in caspase research.
This can result from decreased proliferation or increased cell death, which is why the investigators also looked at caspase 8 and caspase 9.
Various methods to inhibit apoptosis including the cell surface Fas receptor pathway inhibitors, caspase inhibitors, over-expression of anti-apoptotic genes and small interfering ribonucleic acid therapy are discussed.
Caspase-8 lies at the apex of an apoptotic cascade and initiates mitochondrial activation of downstream caspase family members.
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