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J Biol Chem, Vol. 274, Issue 11, 7245-7252, March 12, 1999
From the Department of Tumor Cell Biology, St. Jude Children's
Research Hospital, Memphis, Tennessee 38101
Cycloheximide (CHX) can contribute to apoptotic
processes, either in conjunction with another agent
(e.g. tumor necrosis factor-
Cycloheximide-induced T-cell Death Is Mediated by a
Fas-associated Death Domain-dependent Mechanism
) or on its own. However,
the basis of this CHX-induced apoptosis has not been clearly
established. In this study, the molecular mechanisms of CHX-induced
cell death were examined in two different human T-cell lines. In
T-cells undergoing CHX-induced apoptosis (Jurkat), but not in T-cells
resistant to the effects of CHX (CEM C7), caspase-8 and caspase-3 were
activated. However, the Fas ligand was not expressed in Jurkat cells
either before or after treatment with CHX, suggesting that the
activation of these caspases does not involve the Fas receptor. To
determine whether CHX-induced apoptosis was mediated by a
Fas-associated death domain (FADD)-dependent mechanism, a
FADD-DN protein was expressed in cells prior to CHX treatment. Its
expression effectively inhibited CHX-induced cell death, suggesting
that CHX-mediated apoptosis primarily involves a
FADD-dependent mechanism. Since CHX treatment did not
result in the induction of Fas or FasL, and neutralizing anti-Fas and anti-tumor necrosis factor receptor-1 antibodies did not block CHX-mediated apoptosis, these results may also indicate that FADD functions in a receptor-independent manner. Surprisingly, death effector filaments containing FADD and caspase-8 were observed during
CHX treatment of Jurkat, Jurkat-FADD-DN, and CEM C7 cells, suggesting
that their formation may be necessary, but not sufficient, for cell death.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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