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A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes.
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| Author |
Thornberry, N A, et al. |
| Citation Information |
Nature, 356: 768-74 (1992), : (1992) |
| Related Products |
01-151, 12-341 |
| Pub Med ID |
1574116 |
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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.