FLICE Is Predominantly Expressed as Two Functionally Active Isoforms, Caspase-8/a and Caspase-8/b
Journal of Biological ChemistryPublished 1 October 1997Open access
Carsten Scaffidi, Jan Paul Medema, Peter H. Krammer, Marcus E. Peter
Citations395
SJR quartileQ1
SJR score1.71
SNIP1.00
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TL;DR
A panel of monoclonal antibodies directed against all functional domains of FLICE showed that only two of the FLICE isoforms were predominantly expressed in cells of different origin and could be detected in significant amounts at the protein level.
Abstract
Induction of apoptosis by the cell surface receptor CD95 (APO-1/Fas) has been shown to involve activation of a family of cysteine proteases (caspases). Recently, a new member of this family has been identified, designated FLICE (caspase-8/MACH/Mch5). FLICE is part of the CD95 death-inducing signaling complex and is therefore the most upstream caspase in the CD95 apoptotic pathway. A total of eight different isoforms of FLICE (caspase-8/a-h) have been described. To determine which isoforms are expressed in different cells we have generated a panel of monoclonal antibodies directed against all functional domains of FLICE. Using these antibodies we could show that only two of the FLICE isoforms (caspase-8/a and caspase-8/b) were predominantly expressed in cells of different origin. Both isoforms were recruited to the CD95 death-inducing signaling complex and were activated upon CD95 stimulation with similar kinetics. Taken together, only two of the eight published caspase-8 isoforms could be detected in significant amounts at the protein level.
Keywords
Immunology and MicrobiologyMedicineBiochemistry, Genetics and Molecular Biology
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