Nature 1992-04-30

A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes.

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

Index: Nature 356 , 768, (1992)

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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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