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Blood, Vol. 95 No. 1 (January 1), 2000:
pp. 301-308
Functional CD95 ligand and CD95 death-inducing signaling complex
in activation-induced cell death and doxorubicin-induced apoptosis
in leukemic T cells
Simone Fulda,
Gudrun Strauss,
Eric Meyer, and
Klaus-Michael Debatin
From the University Children's Hospital, Ulm, Germany.
Activation-induced cell death (AICD) in T cells is mediated by CD95
ligand (CD95L)/receptor interaction, which has also been implicated in
apoptosis induction by some anticancer agents. In this article we
show that both anti-CD3-triggering (AICD) and doxorubicin treatment
led to the production of a functionally active CD95L in the
CD3+/T-cell receptor-positive (TCR+) T leukemia cell line H9.
CD95L-expressing H9 cells killed CD95-sensitive J16 or CEM target
cells, but not CD95-resistant CEM or J16 cells overexpressing dominant
negative FADD (J16/FADD-DN). By immunoprecipitation, CD95L
was physically bound to CD95, suggesting that AICD and
doxorubicin-induced apoptosis involve CD95L-mediated CD95 aggregation,
thereby triggering the CD95 death pathway. CD95 aggregation was
associated with the recruitment of FADD and caspase-8 to the CD95
receptor to form the CD95 death-inducing signaling complex (DISC),
resulting in caspase-8 activation and cleavage of the effector
caspase-3 and PARP. Blocking of the CD95L/receptor interaction by
antagonistic antibodies to CD95 or to CD95L also blocked AICD and
inhibited the early phase of doxorubicin-induced apoptosis, though cell death induced by doxorubicin eventually proceeded in a CD95-independent manner. These findings may explain some conflicting data on the role of
death receptor systems in drug-induced apoptosis. Thus, in cells with
an inducible CD95 receptor/ligand system, drug-induced apoptosis may be
mediated by CD95L-initiated DISC formation and activation of downstream
effector programs similar to AICD in T cells. (Blood.
2000;95:301-308)
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