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Overexpression of Protein Kinase C Isoform  but not  in
Human Interleukin-3-Dependent Cells Suppresses Apoptosis and
Induces bcl-2 Expression
E. Gubina,
M.S. Rinaudo,
Z. Szallasi,
P.M. Blumberg, and
R.A. Mufson
From the Department of Immunology, Holland Laboratory/American Red
Cross, Rockville, MD; Laboratory of Cellular Carcinogenesis and Tumor
Promotion, National Cancer Institute, Bethesda, MD; and Department of
Pharmacology, Uniformed Services University of the Health Sciences,
Bethesda, MD.
Hematopoietic progenitor cells die by apoptosis after removal of the
appropriate colony-stimulating factor (CSF). Recent pharmacologic data
have implicated protein kinase C (PKC) in the suppression of apoptosis
in interleukin-3 (IL-3) and granulocyte-macrophage (GM)-CSF-dependent
human myeloid cells. Because IL-3 and GM-CSF induce increases in
diacylglycerol without mobilizing intracellular Ca++,
it seemed that one of the novel Ca++ independent
isoforms of PKC was involved. We report here that overexpression of
PKC in factor-dependent human TF-1 cells extends cell survival in
the absence of cytokine. Overexpression of PKC does not have this
effect. By 72 to 96 hours after cytokine withdrawal, the PKC
transfectants remain distributed in all phases of the cell cycle, as
shown by fluorescence-activated cell sorting (FACS) analysis, while
little intact cellular DNA is detectable in vector or PKC
transfectants. PKC induces bcl-2 protein expression fivefold to
sixfold over the levels in empty vector transfectants, whereas the
levels in PKC transfectants are similar to those in vector controls.
Blood, Vol. 91 No. 3 (February 1), 1998:
pp. 823-829
© 1998 by The American Society of Hematology.
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