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• W1972486502 abstract "Members of the caspase family of cysteine proteases coordinate the highly disparate processes of apoptosis and inflammation. However, although hundreds of substrates for the apoptosis effector caspases (caspase-3 and caspase-7) have been identified, only two confirmed substrates for the key inflammatory protease (caspase-1) are known. Whether this reflects intrinsic differences in the substrate specificity of inflammatory <i>versus</i> apoptotic caspases or their relative abundance <i>in vivo</i> is unknown. To address this issue, we have compared the specificity of caspases-1, -3, and -7 toward peptide and protein substrates. Contrary to expectation, caspase-1 displayed concentration-dependent promiscuity toward a variety of substrates, suggesting that caspase-1 specificity is maintained by restricting its abundance. Although endogenous concentrations of caspase-1 were found to be similar to caspase-3, processed caspase-1 was found to be much more labile, with a half-life of ∼9 min. This contrasted sharply with the active forms of caspase-3 and caspase-7, which exhibited half-lives of 8 and 11 h, respectively. We propose that the high degree of substrate specificity displayed by caspase-1 is maintained through rapid spontaneous inactivation of this protease." @default.
• W1972486502 created "2016-06-24" @default.
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• W1972486502 date "2011-09-01" @default.
• W1972486502 modified "2023-09-26" @default.
• W1972486502 title "Caspase-1 Promiscuity Is Counterbalanced by Rapid Inactivation of Processed Enzyme" @default.
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• W1972486502 doi "https://doi.org/10.1074/jbc.m111.225862" @default.
• W1972486502 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3173193" @default.
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