Molecular cloning and identification of murine caspase-8

Marc Van De Craen, Geert Van Loo, Wim Declercq, Peter Schotte, Ilse Van Den Brande, Susanna Mandruzzato, Pierre Van Der Bruggen, Walter Fiers, Peter Vandenabeele

Research output: Contribution to journalArticlepeer-review


Several caspases are mediators of apoptotic cell death. We describe a novel murine member of this growing protein family. Based on homology and especially on the substrate specificity, this new procaspase is identified as the murine counterpart of human procaspase-8. The protein exhibits a rather low similarity (76%) and identity (70%) to human procaspase-8. Procaspase-8 mRNA is expressed in all adult mouse tissues examined, the highest levels being reached in kidney, liver and lung. Procaspase-8 mRNA expression is highest in seven-day old embryos, but also during later stages of development the expression was fairly high. Both human and murine procaspase-8 are very weak substrates for granzyme B as compared to procaspase-3. Murine procaspases-1, 2, 3, 6, 7, 8, 11/4 and 12 are processed by recombinant murine caspase-8, suggesting a key role in the procaspase activation cascade. In addition, murine caspase-8 induced cell death that was inhibited both by cytokine response modifier A and p35. In vitro experiments demonstrated that p35 inhibits caspase-8 directly.

Original languageEnglish
Pages (from-to)1017-1026
Number of pages10
JournalJournal of Molecular Biology
Issue number4
Publication statusPublished - Dec 11 1998


  • Apoptosis
  • Caspase-8
  • Granzyme B
  • p35

ASJC Scopus subject areas

  • Virology


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