Abstract
Lipid phosphate phosphatases: more than one way to put the brakes on LPA signaling?
Highlights
Lipid phosphate phosphatases (LPPs, encoded by the PPAP2 genes) are broad specificity enzymes that can dephosphorylate lipid phosphate esters such as phosphatidic acid (PA), lysophosphatidic acid (LPA), and sphingosine1- phosphate (S1P) that serve as critical intermediates in intracellular pathways of lipid metabolism and signaling (Fig. 1) [1]
There is a broad consensus that manipulating LPP expression can alter cellular signaling responses to bioactive lipid phosphate mediators in some systems and often in a manner that depends on catalytic activity of the enzymes, these effects could be mediated by directly limiting the agonist actions of the mediators by degradation of extracellular or cell-surface associated lipids, by postreceptor effects on downstream lipid signaling pathways, or a combination of both (Fig. 1)
Increased ecto LPA and S1P phosphatase activity in these cells was associated with decreased growth and migration in response to LPA and serum
Summary
Lipid phosphate phosphatases (LPPs, encoded by the PPAP2 genes) are broad specificity enzymes that can dephosphorylate lipid phosphate esters such as phosphatidic acid (PA), lysophosphatidic acid (LPA), and sphingosine1- phosphate (S1P) that serve as critical intermediates in intracellular pathways of lipid metabolism and signaling (Fig. 1) [1]. Manipulations of LPP expression have been shown to alter levels of cell-associated LPP substrates and products including PA and its dephosphorylation product diacylglycerol (DG) that are well established to regulate intracellular signaling pathways.
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