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Department of Surgery, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261 [D-W. S., J. L., M-H. S., S-Y. P., T. R. B.], and BASF Bioresearch Corporation, Worcester, Massachusetts 01605 [R. V. T.]
Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) is
a TNF family member and potent apoptosis inducer. In contrast to
TNF-
or Fas ligand, relatively little is known about the signaling
events activated by TRAIL. In particular, the initial caspase(s)
required for TRAIL-induced apoptosis remains to be determined.
Caspase-3-like protease but not caspase-1-like protease (YVADase)
activity rapidly increased in HeLa cells in response to TRAIL
treatment. The increase in protease activity correlated with the
profile of apoptotic cell death that was inhibited by the pan-caspase
inhibitor Z-VAD-fmk. In response to TRAIL, caspase-8, an initiator
caspase in death receptor-mediated apoptosis, was activated within
1 h in association with Bid cleavage, cytochrome c
release, caspase-3 activation, and DNA fragmentation factor 45
cleavage. Z-IETD-fmk, a caspase-8 inhibitor, completely blocked
caspase-8 activation and resulted in inhibition of caspase-3 (a
caspase-3-like protease) activation and apoptotic cell death.
Overexpression of a caspase-8 dominant negative mutant inhibited
apoptosis induced by TRAIL. Caspase-8-deficient Jurkat cells were
resistant to both TRAIL- and Fas-induced apoptosis, whereas wild-type
Jurkat cells were susceptible to both TRAIL- and Fas-induced apoptosis.
The caspase-8-reintroduced caspase-8-deficient Jurkat cells acquired
normal susceptibility to both TRAIL and agonistic Fas antibody. Reverse
transcription-PCR and sequence analyses have revealed that these
caspase-8-deficient Jurkat cells express wild-type caspase-10.
Therefore, our data indicate that caspase-8 is required for
TRAIL-induced apoptosis and suggest that caspase-10 may play a minor
role, if any, in TRAIL-induced apoptosis.
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