The Journal of Immunology, Vol 149, Issue 10 3254-3259, Copyright © 1992 by American Association of Immunologists

ARTICLES

Molecular cloning of the murine IL-1 beta converting enzyme cDNA

MA Nett, DP Cerretti, DR Berson, J Seavitt, DJ Gilbert, NA Jenkins, NG Copeland, RA Black and DD Chaplin
Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110.

IL-1 beta is a potent modulator of immune and inflammatory responses. Murine IL-1 beta is initially synthesized as an inactive 33-kDa pro- molecule that is activated by proteolytic cleavage between Asp-117 and Val-118 to generate the 17-kDa mature IL-1 beta protein. This cleavage is catalyzed by a specific protease that has been designated the IL-1 beta converting enzyme (or IL-1 beta convertase). We have used a human IL-1 beta convertase cDNA to isolate murine convertase cDNA from a WEHI- 3 library. These cDNA predicted that the murine convertase is a 402- residue protein. Overall, the murine convertase showed 71% nucleotide and 62% predicted amino acid sequence identity with the human convertase. Southern blot analysis of interspecific backcross mice indicated that the murine IL-1 beta convertase is encoded by a single copy gene located on murine chromosome 9. The murine convertase showed broad constitutive expression, being detected in mononuclear phagocyte and T lymphocyte cell lines as well as in spleen, heart, brain, and adrenal glands. The expression of the murine convertase in mononuclear phagocytes was up-regulated by treatment with LPS or rIFN-gamma. These studies establish that the IL-1 beta convertase is an evolutionarily conserved, widely expressed enzyme that can be regulated at a pretranslational level.

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