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

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

  • Nature. 1992 Apr 30;356(6372):768-74. doi: 10.1038/356768a0.
N A Thornberry 1,  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
Affiliations

Affiliation

  • 1 Department of Biochemistry, Merck Research Laboratories, Rahway, New Jersey 07065.
PMID: 1574116 DOI: 10.1038/356768a0
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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