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Caspase is a generic term for the interleukin-1 β enzyme (ICE) family. Caspase (cysteine aspartate-special proteases) means that the active site of this type of protease is a highly conserved cysteine residue (taking the first letter "c"). The aspartic acid which specifically cleaves the substrate is represented by "aspase", so it is referred to as caspase for short. This enzyme plays a key role in the process of apoptosis. At least 14 caspases have been discovered, all of which are in the form of inactive zymogens, including one N-terminal prodomain and two large and small subunits. According to the length of the prodomain, caspase family members can be divided into long pre-domain and short pre-domain. The former includes caspase -1, 2, 4, 5, 8, 9, and 10. The latter include caspase -3, 6, 7, 11.
Caspase-dependent apoptosis has a complex regulatory mechanism, and regulation by various variants is an important approach. Caspase selectively cleaves certain proteins, causing cell death. In normal cells, each caspase is present in an inactive state, and this peptide chain is longer than the active period. By cutting off the excess, it turns into an active caspase.
Cell death is a new type of programmed cell death that has been found and confirmed in recent years, depending on caspase-1 or caspase-11. When the cell death occurs, the cell membrane ruptures with the release of a large number of pro-inflammatory factors. The morphological characteristics, occurrence and regulation mechanism of cell death are different from other cell death modes such as apoptosis and necrosis. Cellular caliber is widely involved in the development of infection, atherosclerosis and nervous system related diseases. Therefore, Caspase related peptides are associated with cell death. Flood et al found that Caspase-4/Caspase-5 increased expression in intestinal epithelial cells of colorectal cancer tumor tissues. Therefore, Caspase-4/Caspase-5 is a potential drug target for intestinal inflammation. This also indicates that Caspase-4/Caspase-5 expressed in intestinal epithelial cells can serve as a molecular marker for the diagnosis and treatment of potential colorectal cancer diseases.
Reference
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