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J Biol Chem, Vol. 273, Issue 30, 18984-18991, July 24, 1998
From the Phosphorylation of Bcl-2 protein is a
post-translational modification of unclear functional consequences. We
studied the correlation between Bcl-2 phosphorylation, mitotic arrest,
and apoptosis induced by the anti-tubulin agent paclitaxel. Continuous
exposure of human cervical carcinoma HeLa cells to 50 ng/ml paclitaxel
resulted in mitotic arrest with a symmetrical bell-shaped curve over
time. The number of mitotic cells was highest at 24 h (82%), then
declined as arrested cells progressed into apoptosis, and barely no
mitotic cells were present at 48-60 h. The time curves of
paclitaxel-induced cyclin B1 accumulation and stimulation of
Cdc2/cyclin B1 kinase activity were identical and superimposable to
that of M phase arrest. In contrast, apoptosis was first detected at
12 h and steadily increased thereafter until the termination of
the experiments at 48-60 h, when about 80-96% of cells were
apoptotic. Bcl-2 phosphorylation was closely associated in time with M
phase arrest, accumulation of cyclin B1, and activation of Cdc2/cyclin
B1 kinase, but not with apoptosis. At 24 h, when about 82% of the
cells were in mitosis, almost all Bcl-2 protein was phosphorylated,
whereas at 48 h, when 70-90% of the cells were apoptotic, all
Bcl-2 protein was unphosphorylated. Similar results were obtained with
SKOV3 cells, indicating that the association of paclitaxel-induced M
phase arrest and Bcl-2 phosphorylation is not restricted to HeLa cells. We used short exposure to nocodazole and double thymidine to
synchronize HeLa cells and investigate the association of Bcl-2
phosphorylation with mitosis. These studies demonstrated that Bcl-2
phosphorylation occurs in tight association with the number of mitotic
cells in experimental conditions that do not lead to apoptosis.
However, a continuous exposure to nocodazole resulted in a pattern of
Bcl-2 phosphorylation, M phase arrest, and apoptosis similar to that observed with paclitaxel. The phosphatase inhibitor okadaic acid was
found to inhibit the dephosphorylation of phosphorylated Bcl-2 and to
delay the progression of nocodazole M phase-arrested cells into
interphase. In contrast, the serine/threonine kinase inhibitor staurosporine, but not the tyrosine kinase inhibitor genistein, led to
rapid dephosphorylation of phosphorylated Bcl-2 and accelerated the
progression of nocodazole M phase-arrested cells into interphase. Immune complex kinase assays in cell-free systems demonstrated that
Bcl-2 protein can be a substrate of Cdc2/cyclin B1 kinase isolated from
paclitaxel-treated cells arrested in M phase. Taken together, these
studies suggest that Bcl-2 phosphorylation is tightly associated with
mitotic arrest and fail to demonstrate that it is a determinant of
progression into apoptosis after mitotic arrest induced by anti-tubulin
agents.
Phosphorylation of Bcl-2 Is a Marker of M Phase Events and
Not a Determinant of Apoptosis
,
Department of Thoracic/Head and Neck Medical
Oncology,
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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