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Caspase-1 therefore plays a fundamental role in the innate immune system. The enzyme is responsible for processing cytokines such as pro-ILβ and pro-IL18, as well as secreting them. [22] Caspase-4 and -5 in humans, and Caspase-11 in mice have a unique role as a receptor, whereby it binds to LPS, a molecule abundant in gram negative bacteria ...
A very rare genetic disorder of the immune system can also be caused by mutations in this gene. This disease, called CEDS, stands for “ Caspase eight deficiency state .” CEDS has features similar to ALPS , another genetic disease of apoptosis , with the addition of an immunodeficient phenotype.
Caspase-9 is an enzyme that in humans is encoded by the CASP9 gene.It is an initiator caspase, [5] critical to the apoptotic pathway found in many tissues. [6] Caspase-9 homologs have been identified in all mammals for which they are known to exist, such as Mus musculus and Pan troglodytes.
In normal cells, CDV activates caspase-8 first, which works as the initiator protein followed by the executioner protein caspase-3. [93] However, apoptosis induced by CDV in HeLa cells does not involve the initiator protein caspase-8. HeLa cell apoptosis caused by CDV follows a different mechanism than that in vero cell lines. [93]
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-6 is an enzyme that in humans is encoded by the CASP6 gene. [ 5 ] [ 6 ] CASP6 orthologs [ 7 ] have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds , lizards , lissamphibians , and teleosts .
When caspases are activated, they break down a variety of specific protein substrates, triggering the distinct features of apoptosis, such as DNA fragmentation, chromatin condensation, and plasma membrane blebbing. Caspase-2, known as the most evolutionarily conserved caspase, holds a unique role in both apoptotic and non-apoptotic functions.
CARDs were originally characterized based on their involvement in the regulation of caspase activation and apoptosis. [2] The basic six-helix structure of the domain appears to be conserved as far back as the ced-3 and ced-4 genes in C. elegans, the organism in which several components of the apoptotic machinery were first characterized.