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Blood, Vol. 94 No. 5 (September 1), 1999:
pp. 1727-1737
Modulation of Caspase-8 and FLICE-Inhibitory Protein
Expression as a Potential Mechanism of Epstein-Barr Virus Tumorigenesis
in Burkitt's Lymphoma
Clifford G. Tepper and
Michael F. Seldin
From the Rowe Program in Genetics, Departments of Biological
Chemistry and Medicine, UC Davis School of Medicine, Davis, CA.
Ligation of the Fas receptor induces death-inducing signaling
complex (DISC) formation, caspase activation, and subsequent apoptotic
death of several cell types. Epstein-Barr virus (EBV)-positive group
III Burkitt's lymphoma (BL) cell lines have a marked resistance to
Fas-mediated apoptosis, although expressing each of the DISC components, Fas/ APO-1-associated death domain protein
(FADD), and caspase-8 (FLICE/MACH/Mch5). The apoptotic
pathway distal to the DISC is intact because ceramide analogs,
staurosporine, and granzyme B activate caspase-3 and induce apoptosis.
Fas resistance was not explained by the putative death-attenuating
caspase-8 isoforms. However, while Fas-activated cytosolic extracts
from sensitive cells were capable of processing both procaspase-8 and procaspase-3 into active subunit forms, resistant cell extracts did not
possess either of these activities. Accordingly, reverse transcriptase-polymerase chain reaction (RT-PCR) analysis showed higher
transcript levels for the FLICE-inhibitory protein (FLIPL) in resistant cells and the ratio of caspase-8 to FLIPL
measured by competition RT-PCR analysis directly correlated with
susceptibility to Fas-mediated apoptosis of all cell lines. In
addition, modification of the caspase-8/FLIPL ratio by
caspase-8 or FLIPL overexpression was able to alter the
susceptibility status of the cell lines tested. Our results imply that
the relative levels of caspase-8 and FLIPL are an important
determinant of susceptibility to Fas-mediated apoptosis.
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