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A more recent version of this article appeared on October 1, 2003

Papers In Press, published online ahead of print July 1, 2003
J. Lipid Res., doi:10.1194/jlr.M300188-JLR200
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Submitted on May 6, 2003
Revised on June 23, 2003
Accepted on June 24, 2003

Role of phospholipase D in agonist stimulated Lysophosphatidic acid synthesis by ovarian cancer cells

Celine Luquain, Anuurag Singh, Lixin Wang, Vishwanathan Natarajan, and Andrew J. Morris

Cell and Developmental Biology, UNC-Chapel Hill, Chapel Hill, NC 27516

Corresponding Author: ajmorris{at}med.unc.edu

Lysophosphatidic acid (LPA) is a receptor active lipid mediator with a broad range of biological effects. Ovarian cancer cells synthesize LPA, which promotes their motility, growth and survival. We show that a murine homolog of a human protein previously reported to hydrolyze LPA is a highly selective detergent-stimulated LPA phosphatase that can be used to detect and quantitate LPA. Use of this protein in novel enzymatic assay demonstrates that SK-OV-3 ovarian cancer cells release physiologically relevant levels of biologically active LPA into the extracellular space. LPA release is markedly increased by nucleotide agonists acting through a P2Y4 purinergic receptor. Promotion of LPA formation by nucleotides is accompanied by stimulation of Phospholipase D (PLD) activity. Overexpression of both PLD1 and PLD2 in SK-OV-3 cells produces active enzymes but only overexpression of PLD2 results in significant amplification of both nucleotide stimulated PLD activity and LPA production. SK-OV-3 cells express and secrete a phospholipase A2 activity that can generate LPA from the lipid product of PLD, phosphatidic acid (PA). Our results identify a novel role for nucleotides in regulation of ovarian cancer cells and suggest an indirect but critical function for PLD2 in agonist stimulated LPA production.


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