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A Novel Heterodimeric Cysteine Protease Is Required For Interleukin-1βprocessing In Monocytes
Nancy A. Thornberry, Herbert G. Bull, Jimmy R. Calaycay, K. Chapman, A. Howard, Matthew J. Kostura, D. Miller, Susan M. Molineaux, J. Weidner, J. Auniņš, Keith O. Elliston, J. Ayala, Francesca J. Casano, J. Chin, Gloria J.-F. Ding, Linda A. Egger, E. Gaffney, G. Limjuco, Oksana C. Palyha, S. M. Raju, Anna M. Rolando, J. Salley, Ting-ting D Yamin, Terry D. Lee, John E. Shively, Malcolm Maccross, R. Mumford, John A. Schmidt, Michael J. Tocci
Published 1992 · Biology, Medicine
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Interleukin-1β (IL-1β)-converting enzyme cleaves the IL-1β precursor to mature IL-1β, an important mediator of inflammation. The identification of the enzyme as a unique cysteine protease and the design of potent peptide aldehyde inhibitors are described. Purification and cloning of the complementary DNA indicates that IL-lβ-converting enzyme is composed of two nonidentical subunits that are derived from a single proenzyme, possibly by autoproteolysis. Selective inhibition of the enzyme in human blood monocytes blocks production of mature IL-1β, indicating that it is a potential therapeutic target.
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