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Originally published In Press as doi:10.1194/jlr.M600077-JLR200 on May 1, 2006

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Journal of Lipid Research, Vol. 47, 1449-1456, July 2006
Copyright © 2006 by American Society for Biochemistry and Molecular Biology

Regulation of de novo phosphatidylinositol synthesis

Samer J. Nuwayhid*, Martha Vega{dagger}, Paul D. Walden*,§ and Marie E. Monaco1,{dagger},**

* Department of Urology, New York University School of Medicine, New York, NY 10016
{dagger} Department of Physiology and Neuroscience, New York University School of Medicine, New York, NY 10016
§ Department of Biochemistry, New York University School of Medicine, New York, NY 10016
** Research Service, Department of Veterans Affairs New York Harbor Healthcare System, New York, NY 10010

Published, JLR Papers in Press, May 1, 2006.

1 To whom correspondence should be addressed. e-mail: mem6{at}nyu.edu

Mechanisms that function to regulate the rate of de novo phosphatidylinositol (PtdIns) synthesis in mammalian cells have not been elucidated. In this study, we characterize the effect of phorbol ester treatment on de novo PtdIns synthesis in C3A human hepatoma cells. Incubation of cells with 12-O-tetradecanoyl phorbol 13-acetate (TPA) initially (1–6 h) results in a decrease in precursor incorporation into PtdIns; however, at later times (18–24 h), a marked increase is observed. TPA-induced glucose uptake from the medium is not required for observation of the stimulation of PtdIns synthesis, because the effect is apparent in glucose-free medium. Inhibition of the activation of arachidonic acid substantially blocks the synthesis of PtdIns but has no effect on the synthesis of phosphatidylcholine (PtdCho). Increasing the concentration of cellular phosphatidic acid by blocking its conversion to diacylglycerol, on the other hand, enhances the synthesis of PtdIns and inhibits the synthesis of PtdCho. The TPA-induced stimulation of PtdIns synthesis is not the result of the concomitant TPA-induced G1 arrest, because G1 arrest induced by mevastatin has no effect on PtdIns synthesis. Inhibition of protein kinase C activity blocks the stimulatory action of TPA on de novo synthesis of PtdIns but has no effect on TPA-induced inhibition. Potential sites of enzymatic regulation are discussed.

Supplementary key words phorbol ester • cell cycle • protein kinase C • arachidonic acid • phosphatidic acid.


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