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J. Biol. Chem., Vol. 267, Issue 11, 7199-7202, Apr, 1992
KM Conricode, KA Brewer and JH Exton
The role of protein kinase C (PKC) in the regulation of
phosphatidylcholine-hydrolyzing phospholipase D (PLD) was investigated. In
membranes from Chinese hamster lung fibroblasts that had been incubated
with [14C]choline to label endogenous phosphatidylcholine, phorbol
12-myristate 13-acetate (PMA) failed to stimulate production of
[14C]choline. However, stimulation was observed if fibroblast cytosolic
fraction or PKC partially purified from this fraction was added. When
incubated with membranes in the presence of PMA, pure PKC from rat brain
stimulated [14C]choline production in a concentration-dependent manner,
with a maximal 2-3-fold effect. PMA similarly stimulated
[14C]phosphatidylpropanol formation from propanol using membranes from
[14C]myristic acid-prelabeled cells, confirming the activation of PLD. None
of the effects described required exogenous ATP. To probe the role of
phosphorylation in the PKC effect, we included high concentrations of
apyrase in the assay. This ATPase had no effect on the ability of PKC to
activate PLD, but under exactly the same conditions, it eliminated
autophosphorylation of PKC. The results provide conclusive evidence for the
involvement of PKC in the activation of PLD and suggest that ATP-dependent
phosphorylation is not required.
Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism
Howard Hughes Medical Institute, Nashville, Tennessee.
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