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Blood, Vol. 94 No. 10 (November 15), 1999:
pp. 3523-3530
Defective Apoptotic Signal Transduction Pathway Downstream of Caspase-3
in Human B-Lymphoma Cells: A Novel Mechanism of Nuclear Apoptosis
Resistance
Yoshinari Kawabata,
Makoto Hirokawa,
Atsushi Kitabayashi,
Takahiro Horiuchi,
Jun Kuroki, and
Akira B. Miura
From the Department of Internal Medicine III, Akita University School
of Medicine, Akita, Japan.
Mitochondria play a central role in controlling apoptosis, and
activation of the caspase cascade appears to be crucial event during
the apoptotic process. Human B lymphoma Raji cells are resistant to
nuclear apoptosis induced by various stimuli. Using this cell line, we
have asked whether reduction of the mitochondrial transmembrane
potential and activation of caspase-3 are sufficient to induce DNA
fragmentation during the apoptotic process. After stimulation with
cell-permeable C2-ceramide or mitochondrial permeability transition
(PT) inducers, not only apoptosis-sensitive cell lines (HL-60, Jurkat,
and Daudi cells), but also Raji cells showed reduction of the
mitochondrial transmembrane potential (  m), activation of
caspase-3, and loss of clonogenic potential. However, Raji cells did
not show detectable levels of nuclear apoptosis (DNA degradation). In a
cell-free system, cell lysates from tetra-butylhydroperoxide (t-BHP)-treated HL-60 cells induced DNA degradation of Raji nuclei, whereas cell lysates from t-BHP-treated Raji cells failed to induce DNA degradation in either apoptosis-sensitive cell lines or
apoptosis-resistant Raji cells. Cleavage of DFF-45, which is a
downstream target molecule for caspase-3, was observed in Raji cells as
well as in apoptosis-sensitive Daudi cells. These results indicate that
there is a defective apoptotic pathway in the cytoplasm downstream of
caspase-3 in Raji cells.
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