Caspase-1/Interleukin-1 converting enzyme (ICE) is an evolutionarily conserved enzyme that proteolytically cleaves other proteins, such as the precursors of the inflammatory cytokinesinterleukin 1β and interleukin 18 as well as the pyroptosis inducer Gasdermin D, into active mature peptides.[5][6][7] It plays a central role in cell immunity as an inflammatory response initiator. Once activated through formation of an inflammasome complex, it initiates a proinflammatory response through the cleavage and thus activation of the two inflammatory cytokines, interleukin 1β (IL-1β) and interleukin 18 (IL-18) as well as pyroptosis, a programmed lytic cell death pathway, through cleavage of Gasdermin D.[8] The two inflammatory cytokines activated by Caspase-1 are excreted from the cell to further induce the inflammatory response in neighboring cells.[9]
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^Cerretti DP, Kozlosky CJ, Mosley B, Nelson N, Van Ness K, Greenstreet TA, et al. (April 1992). "Molecular cloning of the interleukin-1 beta converting enzyme". Science. 256 (5053): 97–100. Bibcode:1992Sci...256...97C. doi:10.1126/science.1373520. PMID1373520.
^Cite error: The named reference pmid15190255 was invoked but never defined (see the help page).