Interleukin-1βconverting enzyme: A novel cysteine protease required for IL-1β production and implicated in programmed cell death

Authors

  • Nancy A. Thornberry,

    Corresponding author
    1. Department of Enzymology, Merck Research Laboratories, Rahway, New Jersey 07065
    • Merck Research Labo-ratories, R80W-243, P.O. Box 2000, Rahway, New Jersey 07065
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  • Susan M. Molineaux

    1. Department of Molecular Immunology, Merck Research Laboratories, Rahway, New Jersey 07065
    Current affiliation:
    1. Pharmaceutical Peptides, Inc., Hampshire Street, Cambridge, Massachusetts 02139
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Abstract

Interleukin-1β converting enzyme is the first member of a new class of cysteine proteases. The most distinguishing feature of this family is a nearly absolute specificity for cleavage at aspartic acid. This enzyme has been the subject of intense research because of its role in the production of IL-1β, a key mediator of inflammation. These studies have culminated in the design of potent inhibitors and determination of its crystal structure. The structure secures the relationship of the enzyme to CED-3, the product of a gene required for programmed cell death in Caenorhabditis elegans, suggesting that members of this family function in cell death in vertebrates.

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