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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.
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 ().
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 ...
Regarding the activation of caspases, there exists a gene called ced-9 in C. elegans that protects against cell death that is a part of the Bcl-2 family. ced-9 encodes a protein that is structurally similar to Bcl-2 that binds to another protein ced-4, a homolog of APAF-1 in humans, and prevents it from activating caspase ced-3, which is necessary for killing of the cell. [4]
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.
Caspase-8 is a caspase protein, encoded by the CASP8 gene. It most likely acts upon caspase-3 . CASP8 orthologs [ 5 ] have been identified in numerous mammals for which complete genome data are available.