Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins , such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD) , into active mature peptides . Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex , it initiates a pro-inflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18 , releasing the mature cytokines which are involved in a variety of inflammatory processes . Cleaves a tetrapeptide after an Asp residue at position P1 . Also initiates pyroptosis , a programmed lytic cell death pathway , through cleavage of GSDMD . In contrast to cleavage of interleukins IL1B and IL1B , recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D , C-terminal (GSDMD-CT) part . Upon inflammasome activation , during DNA virus infection but not RNA virus challenge , controls antiviral immunity through the cleavage of CGAS , rendering it inactive . In apoptotic cells , cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly . ; [Isoform Delta]: Apoptosis inactive. ; [Isoform Epsilon]: Apoptosis inactive.
展开内容