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

Autor: John A. Schmidt, Matthew J. Kostura, Anna M. Rolando, Richard A. Mumford, Ting-Ting Yamin, Guadalupe A. Limjuco, Keith O. Elliston, Jeffrey R. Weidner, J. Paul Salley, Jayne Chin, Susan M. Molineaux, S.M. Raju, John G. Aunins, Gloria J.-F. Ding, Douglas K. Miller, John E. Shively, Oksana C. Palyha, Julia M. Ayala, Nancy A. Thornberry, Michael J. Tocci, Malcolm MacCross, Francesca J. Casano, Herbert G. Bull, Andrew D. Howard, Linda A. Egger, Kevin T. Chapman, Jimmy R. Calaycay, Erin P. Gaffney, Terry D. Lee
Rok vydání: 1992
Předmět:
Zdroj: Nature. 356:768-774
ISSN: 1476-4687
0028-0836
DOI: 10.1038/356768a0
Popis: 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.
Databáze: OpenAIRE