Abstract
Caspases are a family of cysteine proteases which have important roles in activation of cytokines and in apoptosis. Caspase-1, or interleukin-lβ converting enzyme (ICE), promotes maturation of inter-leukin-lβ (IL-1β) and interleukin-18 (IL-18) by prote-olytic cleavage of precursor forms to generate biologically active peptides. We report the cloning and sequencing of equine caspase-1 cDNA. Equine caspase-1 is 405 amino acids in length and has 72% and 63% identity to human and mouse caspase-1, respectively, at the amino acid level. Sites of proteo-lytic cleavage and catalytic activity as identified in human caspase-1, are conserved.
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