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.
Background References
1. Thornberry N A et al. A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356:768-774 (1992).
2. Alnemri E S et al. Cloning and expression of four novel isoforms of human interleukin-1 beta converting enzyme with different apoptotic activities. J Biol Chem 270:4312-4317 (1995).
Sequence Similarity
Belongs to the peptidase C14A family.
Tissue Specificity
Expressed in larger amounts in spleen and lung. Detected in liver, heart, small intestine, colon, thymus, prostate, skeletal muscle, peripheral blood leukocytes, kidney and testis. No expression in the brain.
Post-translational Modification
The two subunits are derived from the precursor sequence by an autocatalytic mechanism.