Article

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

Department of Biochemistry, Merck Research Laboratories, Rahway, New Jersey 07065.
Nature (Impact Factor: 42.35). 04/1992; 356(6372):768-774. DOI: 10.1038/356768a0

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.

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Kevin Tyler Chapman