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Publication : Molecular cloning and identification of murine caspase-8.

First Author  Van de Craen M Year  1998
Journal  J Mol Biol Volume  284
Issue  4 Pages  1017-26
PubMed ID  9837723 Mgi Jnum  J:51525
Mgi Id  MGI:1316864 Doi  10.1006/jmbi.1998.2226
Citation  Van de Craen M, et al. (1998) Molecular cloning and identification of murine caspase-8. J Mol Biol 284(4):1017-26
abstractText  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. Copyright 1998 Academic Press.
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