Caspase-1 is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, p20 and p10, that dimerize to form the active enzyme. This protein was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. Caspase-1 has been shown to induce cell apoptosis and may function in various developmental stages (1).
MAPK signaling pathway
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