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

A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

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References (35)

Publisher
Springer Journals
Copyright
Copyright © 1992 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/356768a0
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

NatureSpringer Journals

Published: Apr 30, 1992

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