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Blood, 1 March 2001, Vol. 97, No. 5, pp. 1378-1387
NEOPLASIA
Activation of caspase-8 in drug-induced apoptosis of B-lymphoid
cells is independent of CD95/Fas receptor-ligand interaction
and occurs downstream of caspase-3
Thomas Wieder,
Frank Essmann,
Aram Prokop,
Karin Schmelz,
Klaus Schulze-Osthoff,
Rudi Beyaert,
Bernd Dörken, and
Peter T. Daniel
From the Department of Hematology, Oncology and Tumor
Immunology, University Medical Center Charité, Campus
Berlin-Buch, and the Department of Pediatric Hematology/Oncology,
University Medical Center Charité, Campus Virchow, Humboldt
University of Berlin, Germany; the Department of Immunology and Cell
Biology, University of Münster, Germany; the Department of
Molecular Biology, Flanders Interuniversity Institute for
Biotechnology, and University of Gent, Belgium.
The activation of caspase-8, a crucial upstream mediator of death
receptor signaling, was investigated in epirubicin- and Taxol-induced
apoptosis of B-lymphoma cells. This study was performed because the
CD95/Fas receptor-ligand interaction, recruitment of the Fas-associated
death domain (FADD) adaptor protein, and subsequent activation of
procaspase-8 have been implicated in the execution of drug-induced
apoptosis in other cell types. Indeed, active caspase-8 was readily
detected after treatment of mature and immature B-lymphoid cells with
epirubicin or Taxol. However, neither constitutive nor drug-induced
expression of the CD95/Fas ligand was detectable in B-lymphoma cells.
Furthermore, overexpression of a dominant-negative FADD mutant (FADDdn)
did not block caspase-8 processing and subsequent DNA fragmentation,
indicating that drug-induced caspase-8 activation was mediated by a
CD95/Fas-independent mechanism. Instead, caspase-8 cleavage was
slightly preceded by activation of caspase-3, suggesting that
drug-induced caspase-8 activation in B-lymphoma cells is a downstream
event mediated by other caspases. This assumption was confirmed in 2 experimental systems zDEVD-fmk, a cell-permeable inhibitor of
caspase-3-like activity, blocked drug-induced caspase-8 cleavage, and
depletion of caspase-3 from cell extracts impaired caspase-8
cleavage after in vitro activation with dATP and cytochrome c. Thus,
these data indicate that drug-induced caspase-8 activation in
B-lymphoma cells is independent of death receptor signaling and is
mediated by postmitochondrial caspase-3 activation.
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