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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-04

AUTHORS

Nancy A. Thornberry, Herbert G. Bull, Jimmy R. Calaycay, Kevin T. Chapman, Andrew D. Howard, Matthew J. Kostura, Douglas K. Miller, Susan M. Molineaux, Jeffrey R. Weidner, John Aunins, Keith O. Elliston, Julia M. Ayala, Francesca J. Casano, Jayne Chin, Gloria J.-F. Ding, Linda A. Egger, Erin P. Gaffney, Guadalupe Limjuco, Oksana C. Palyha, S. M. Raju, Anna M. Rolando, J. Paul Salley, Ting-Ting Yamin, Terry D. Lee, John E. Shively, Malcolm MacCross, Richard A. Mumford, John A. Schmidt, Michael J. Tocci

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. More... »

PAGES

768-774

Journal

TITLE

Nature

ISSUE

6372

VOLUME

356

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/356768a0

    DOI

    http://dx.doi.org/10.1038/356768a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1005852416

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1574116


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