Nature. 1992 Apr 30;356(6372):768-74.

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

Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, Kostura MJ, Miller DK, Molineaux SM, Weidner JR, Aunins J, et al.

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Department of Biochemistry, Merck Research Laboratories, Rahway, New Jersey 07065.

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.

PMID:: 1574116; [PubMed - indexed for MEDLINE]

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