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J. Biol. Chem., Vol. 276, Issue 34, 31752-31759, August 24, 2001
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From the Department of Biochemistry, Wake Forest University School
of Medicine, Winston-Salem, North Carolina 27157-1016
Human acute myelogenous leukemia cells (HL-60
cells) can be induced to differentiate to neutrophils by exposure to
dibutyryl-cyclic AMP. The differentiation of HL-60 cells allowed
the mitogen-activated protein kinases p38 and p44/p42 to be rapidly and
transiently activated upon stimulation with
N-formyl-methionyl-leucyl-phenylalanine (fMLP). Western
blot analysis using phosphospecific p38 and p44/p42 mitogen-activated
protein kinase antibodies showed that increasing concentrations of
ethanol or 1-butanol but not 2-butanol (0.05-0.5%) inhibited
fMLP-induced p38 activation but did not inhibit p44/p42 activation.
These data indicated that activation of phospholipase D (PLD) was
required for activation of p38 but not p44/p42. We compared the effect
of fMLP with those of tumor necrosis factor
Phospholipase D Is Required in the Signaling Pathway Leading to
p38 MAPK Activation in Neutrophil-like HL-60 Cells, Stimulated
by N-Formyl-methionyl-leucyl-phenylalanine*
(TNF) and
granulocyte-macrophage colony-stimulating factor (GM-CSF). We found
that ethanol did not inhibit p38 phosphorylation upon stimulation with
either GM-CSF or TNF. These results suggested that in cells
stimulated with fMLP, PLD was upstream of p38. To further test the
involvement of PLD, we used antisense inhibition of human PLD1
expression. Treatment with antisense oligonucleotides inhibited p38 but
not p44/p42 phosphorylation. These data supported a role for human PLD1
in fMLP-induced p38 activation in neutrophil-like HL-60 cells. In
addition, the results obtained with TNF and GM-CSF demonstrated that
p38 activation occurred independently of PLD activation.
*
This work was supported by National Institutes of Health
(NIH) Grants AI-38949 and CA-72730. The DNA synthesis core laboratory and the Cell Culture Laboratory of the Comprehensive Cancer Center of
Wake Forest University were supported by NCI, NIH, Grant CA-12197.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biochemistry,
Wake Forest University School of Medicine, Winston-Salem, North
Carolina, NC 27157-1016. Tel.: 336-716-3623; Fax: 336-716-7671; E-mail: ldaniel@wfubmc.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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