TY - JOUR
T1 - Molecular cloning and identification of murine caspase-8
AU - Van De Craen, Marc
AU - Van Loo, Geert
AU - Declercq, Wim
AU - Schotte, Peter
AU - Van Den Brande, Ilse
AU - Mandruzzato, Susanna
AU - Van Der Bruggen, Pierre
AU - Fiers, Walter
AU - Vandenabeele, Peter
PY - 1998/12/11
Y1 - 1998/12/11
N2 - 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.
AB - 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.
KW - Apoptosis
KW - Caspase-8
KW - FLICE
KW - Granzyme B
KW - p35
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UR - http://www.scopus.com/inward/citedby.url?scp=0032509132&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1998.2226
DO - 10.1006/jmbi.1998.2226
M3 - Article
C2 - 9837723
AN - SCOPUS:0032509132
VL - 284
SP - 1017
EP - 1026
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 4
ER -