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(Received for publication, November 17, 1994) Phospholipase D (PLD) has been implicated in signal transduction
and membrane traffic. We have previously shown that
phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P
Volume 270,
Number 10,
Issue of March 10, 1995 pp. 5130-5135
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
)
stimulates in vitro partially purified brain membrane PLD
activity, defining a novel function of PtdIns-4,5-P as a
PLD cofactor. In the present study we extend these observations to
permeabilized U937 cells. In these cells, the activation of PLD by
guanosine 5`-3-O-(thio)triphosphate (GTP
S) is greatly
potentiated by MgATP. We have utilized this experimental system to test
the hypothesis that MgATP potentiates PLD activation by G proteins
because it is required for PtdIns-4,5-P synthesis by
phosphoinositide kinases. As expected, MgATP was absolutely required
for maintaining elevated phosphatidylinositol 4-phosphate (PtdIns-4-P)
and PtdIns-4,5-P levels in the permeabilized cells. In the
presence of MgATP, GTPS further elevated the levels of the
phosphoinositides. The importance of PtdIns-4,5-P for PLD
activation was examined by utilizing a specific inhibitory antibody
directed against phosphatidylinositol 4-kinase (PtdIns 4-kinase), the
enzyme responsible for the first step in the synthesis of
PtdIns-4,5-P. Anti-PtdIns 4-kinase completely inhibited
PtdIns 4-kinase activity in vitro and reduced by 75-80%
PtdIns-4-P and PtdIns-4,5-P levels in the permeabilized
cells. In parallel, the anti-PtdIns 4-kinase fully inhibited the
activation of PLD by GTPS and caused a 60% inhibition of PLD
activation by the phorbol ester
12-O-tetradecanoylphorbol-13-acetate, indicating that elevated
PtdIns-4,5-P levels are required for PLD activation. This
conclusion is supported by the fact that neomycin, a high affinity
ligand of PtdIns-4,5-P, also blocked PLD activation.
Furthermore, the activity of PLD in U937 cell lysate was stimulated by
PtdIns-4,5-P in a dose-dependent manner. The current
results indicate that PtdIns-4,5-P synthesis is required
for PLD activation in permeabilized U937 cells and strongly support the
proposed function of PtdIns-4,5-P as a cofactor for PLD. In
addition, the results further establish PtdIns-4,5-P as a
key component in the generation of second messengers via multiple
pathways including phosphoinositidephospholipase C, phosphoinositide
3-kinase and PLD.
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