Caspase-1, originally designated ICE (for IL-1 converting enzyme), is a member of the group of caspases with large prodomains. Caspase-1 promotes maturation of interleukin IL-1β and interleukin18 (IL-18) by proteolytic cleavage of precursor forms into biologically active pro-inflamatory cytokines. Active caspase-1, a (p20/p10)2 tetramer, is necessary and sufficient for cleavage of precursor IL-1 as well as for induction of apoptosis in some cell lines. The highly conserved family of caspases mediate many of the morphological and biochemical features of apoptosis, including structural dismantling of cell bodies and nuclei, fragmentation of genomic DNA, destruction of regulatory proteins and propagation of other pro-apoptotic molecules. The human Caspase-1 gene maps to chromosome 2q14 and encodes a cytoplasmic protein expressed in liver, heart, skeletal muscle kidney and testis. Caspase-1 has been implicated in inflammation, septic shock, and other situations such as wound healing and the growth of certain leukemias.