| First Author | Sakamaki K | Year | 1998 |
| Journal | Eur J Biochem | Volume | 253 |
| Issue | 2 | Pages | 399-405 |
| PubMed ID | 9654089 | Mgi Jnum | J:47358 |
| Mgi Id | MGI:1203341 | Doi | 10.1046/j.1432-1327.1998.2530399.x |
| Citation | Sakamaki K, et al. (1998) Molecular cloning and characterization of mouse caspase-8. Eur J Biochem 253(2):399-405 |
| abstractText | Fas (APO-1/CD95) is a transmembrane receptor protein which induces apoptosis upon activation. In apoptosis triggered by Fas, a subset of cysteine proteases designated caspases is activated, playing a central role as effector molecules. Among these caspases, human caspase-8 (FLICE/MACH/Mch5) has been isolated and shown to be indispensable for Fas-mediated apoptotic signaling. In this study, we isolated the mouse homologue to human caspase-8 from a BaF3 cell cDNA library. This molecule conserved the death effector domain (DED) and protease domain as detected in human caspase-8, and was capable of inducing apoptosis in KB and Rat-1 cells when overexpressed. Expression of caspase-8 was detected in the various tissues of adult mouse and in embryos at 9.5 days and 17.5 days of development by Northern-blot analysis. Further, we isolated a chromosomal gene for caspase-8 from a mouse genomic library and analyzed the genomic structure of the isolated gene. This gene consisted of eight exons and seven introns spanning about 26 kb in the coding region. |
