IL-1 is a name that designates two pleiotropic cytokines, IL-1α (IL-1F1) and IL-1β (IL-1F2), which are the products of distinct genes. IL-1α and IL-1β are structurally related polypeptides that share approximately 26% amino acid (aa) identity in rat. Both proteins are produced by a wide variety of cells in response to inflammatory agents, infections, or microbial endotoxins. While IL-1α and IL-1β are regulated independently, they bind to the same receptor and exert identical biological effects. IL-1 RI binds directly to IL-1α or IL-1β and then associates with IL-1 R accessory protein (IL-1 R3/IL-1 R AcP) to form a high-affinity receptor complex that is competent for signal transduction. IL-1 RII has high affinity for IL-1β but functions as a decoy receptor and negative regulator of IL-1β activity. IL-1ra functions as a competitive antagonist by preventing IL-1α and IL-1β from interacting with IL-1 RI (1 - 4). The rat IL-1β cDNA encodes a 268 aa precursor. A 116 aa propeptide is cleaved intracellularly by the cysteine protease IL-1β-converting enzyme (Caspase-1/ICE) to generate the active cytokine (5, 6). The 17 kDa mature rat IL-1β shares 90% aa sequence identity with cotton rat and mouse and 65% - 77% with canine, equine, feline, human, porcine, and rhesus IL-1β.
1. Allan, S.M. et al., 2005, Nat. Rev. Immunol. 5:629.
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