A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. |
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| Authors: | N A Thornberry H G Bull J R Calaycay K T Chapman A D Howard M J Kostura D K Miller S M Molineaux J R Weidner J Aunins |
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| Affiliation: | Department of Biochemistry, Merck Research Laboratories, Rahway, New Jersey 07065. |
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| Abstract: | Interleukin-1 beta (IL-1 beta)-converting enzyme cleaves the IL-1 beta precursor to mature IL-1 beta, 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-1 beta-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-1 beta, indicating that it is a potential therapeutic target. |
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