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

      Nature

      Amino Acid Sequence, Base Sequence, Binding, Competitive, drug effects, Caspase 1, Chromatography, Affinity, Chromatography, DEAE-Cellulose, Chromatography, High Pressure Liquid, Chromosome Mapping, Cloning, Molecular, Diazomethane, analogs & derivatives, pharmacology, Electrophoresis, Polyacrylamide Gel, Humans, Interleukin-1, metabolism, Metalloendopeptidases, chemistry, genetics, isolation & purification, physiology, Molecular Sequence Data, Monocytes, enzymology, Open Reading Frames, Protein Processing, Post-Translational, Sequence Homology, Nucleic Acid, Substrate Specificity

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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.

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          Journal
          1574116
          10.1038/356768a0

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