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Prepublished online as a Blood First Edition Paper on December 27, 2002; DOI 10.1182/blood-2002-06-1770.
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Blood, 1 May 2003, Vol. 101, No. 9, pp. 3658-3667
NEOPLASIA
TNF-related apoptosis-inducing ligand (TRAIL) frequently
induces apoptosis in Philadelphia chromosome-positive leukemia
cells
Kanako Uno,
Takeshi Inukai,
Nobuhiko Kayagaki,
Kumiko Goi,
Hiroki Sato,
Atsushi Nemoto,
Kazuya Takahashi,
Keiko Kagami,
Noriko Yamaguchi,
Hideo Yagita,
Ko Okumura,
Toshiko Koyama-Okazaki,
Toshio Suzuki,
Kanji Sugita, and
Shinpei Nakazawa
From the Department of Pediatrics, School of Medicine,
University of Yamanashi, Japan; the Department of
Immunology, Juntendo University School of Medicine, Tokyo,
Japan; and the Laboratory of Immunology, Saitama
Shakaihoken Hospital, Saitama, Japan.
Tumor necrosis factor (TNF)-related apoptosis-inducing
ligand (TRAIL) and Fas ligand (FasL) have been implicated in antitumor immunity and therapy. In the present study, we investigated the sensitivity of Philadelphia chromosome (Ph1)-positive leukemia cell
lines to TRAIL- or FasL-induced cell death to explore the possible
contribution of these molecules to immunotherapy against Ph1-positive
leukemias. TRAIL, but not FasL, effectively induced apoptotic cell
death in most of 5 chronic myelogenous leukemia-derived and 7 acute
leukemia-derived Ph1-positive cell lines. The sensitivity to TRAIL was
correlated with cell-surface expression of death-inducing receptors DR4
and/or DR5. The TRAIL-induced cell death was caspase-dependent and
enhanced by nuclear factor  B inhibitors. Moreover, primary leukemia
cells from Ph1-positive acute lymphoblastic leukemia patients were also
sensitive to TRAIL, but not to FasL, depending on DR4/DR5 expression.
Fas-associated death domain protein (FADD) and caspase-8,
components of death-inducing signaling complex (DISC), as well
as FLIP (FLICE [Fas-associating protein with death domain-like
interleukin-1-converting enzyme]/caspase-8 inhibitory protein), a negative regulator of caspase-8, were expressed
ubiquitously in Ph1-positive leukemia cell lines irrespective of their
differential sensitivities to TRAIL and FasL. Notably, TRAIL could
induce cell death in the Ph1-positive leukemia cell lines that were
refractory to a BCR-ABL-specific tyrosine kinase inhibitor imatinib
mesylate (STI571; Novartis Pharma, Basel, Switzerland). These
results suggested the potential utility of recombinant TRAIL as a novel
therapeutic agent and the possible contribution of endogenously
expressed TRAIL to immunotherapy against Ph1-positive leukemias.
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