Abstract
Interleukin-1 (IL-1) is a cytokine that has been implicated in the pathogenesis of acute and chronic inflammatory diseases (1). IL-1 has two isoforms, IL-1α and IL-1β of which IL-1β is the predominant form released by human monocytes in culture. IL-1β is synthesized as a 31-kDa precursor devoid of a conventional signal sequence and is processed to its active 17-kDa form by an enzyme called IL-1β converting enzyme (ICE) which has an unique cleavage specificity for Asp-X (2–4). The purification and cloning of this enzyme have been described (5,6). ICE is synthesized primarily as an inactive 45-kDa precursor and auto-processed to 20- and 10-kDa subunits. The crystal structure of ICE reveals that the active enzyme is composed of two 20-kDa and two 10-kDa subunits to form a tetramer (7,8).
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Kuida, K., Lippke, J.A., Su, M.SS., Flavell, R.A. (1998). Mice Deficient in Interleukin-1β Converting Enzyme. In: Durum, S.K., Muegge, K. (eds) Cytokine Knockouts. Contemporary Immunology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-4757-2753-1_11
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