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

M. A. Nett, D. P. Cerretti, D. R. Berson, J. Seavitt, D. J. Gilbert, Nancy A. Jenkins, Neal G. Copeland, R. A. Black, D. D. Chaplin

Research output: Contribution to journalArticlepeer-review

70 Scopus citations


IL-1β is a potent modulator of immune and inflammatory responses. Murine IL-1β 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-1β protein. This cleavage is catalyzed by a specific protease that has been designated the IL-1β converting enzyme (or IL-1β convertase). We have used a human IL-1β 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-1β 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-γ. These studies establish that the IL-1β convertase is an evolutionarily conserved, widely expressed enzyme that can be regulated at a pretranslational level.

Original languageEnglish (US)
Pages (from-to)3254-3259
Number of pages6
JournalJournal of Immunology
Issue number10
StatePublished - Jan 1 1992

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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