caspase

Source:http://linkedlifedata.com/resource/umls/id/C0010656

MSH: A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.,NCI: Caspases are a family of intracellular cysteine proteinases involved in inflammation and apoptosis. These enzymes appear to be involved in the initial signaling events, as well as the downstream proteolytic cleavages, that result in apoptotic cell death. They are specific for aspartic acid at the P1 position and are divided into two classes based on the lengths of their N-terminal pro-domains. Caspases-1, -2, -4, -5, -8, and -10 have long pro-domains; caspases-3, -6, -7, and -9 have short pro-domains. (from Science 1998. 281:1312

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