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Caspase deficiency has been identified as a cause of tumor development. Tumor growth can occur by a combination of factors, including a mutation in a cell cycle gene which removes the restraints on cell growth, combined with mutations in apoptotic proteins such as caspases that would respond by inducing cell death in abnormally growing cells. [5]
Caspase Dronc is a Drosophila melanogaster protein codified by the Dronc gene. It belongs to the cysteine-aspartic proteases family, as it is a protease enzyme that takes part in programmed cell death processes.
In a healthy cell, caspase-1 activation helps to fight infection caused by Salmonella and Shigella by introducing cell death to restrict pathogen growth. [6] When the "danger" signal is sensed, the quiescent cells will be activated to undergo pyroptosis and produce inflammatory cytokines IL-1β and IL-18.
Caspase-2 is an important enzyme in the cysteine aspartate protease family, known as caspases, which are central to the regulation of apoptosis and, in certain cases, inflammation. While many caspases are mainly involved in the initiation and execution of cell death, caspase-2 has a broader range of functions.
The death-effector domain (DED) is a protein interaction domain found only in eukaryotes that regulates a variety of cellular signalling pathways. [2] The DED domain is found in inactive procaspases (cysteine proteases) and proteins that regulate caspase activation in the apoptosis cascade such as FAS-associating death domain-containing protein ().
Caspase-3 is activated in the apoptotic cell both by extrinsic (death ligand) and intrinsic (mitochondrial) pathways. [ 12 ] [ 22 ] The zymogen feature of caspase-3 is necessary because if unregulated, caspase activity would kill cells indiscriminately. [ 23 ]
Degradation of nuclear DNA into nucleosomal units is one of the hallmarks of apoptotic cell death. It occurs in response to various apoptotic stimuli in a wide variety of cell types. Molecular characterization of this process identified a specific DNase (CAD, caspase-activated DNase) that cleaves chromosomal DNA in a caspase-dependent manner.
The death-inducing signaling complex (DISC) is a multi-protein complex formed by members of the death receptor family of apoptosis-inducing cellular receptors. [1] A typical example is FasR, which forms the DISC upon trimerization as a result of its ligand binding. The DISC is composed of the death receptor, FADD, and caspase 8. It transduces a ...