Phosphatidic acid phosphatase type 2 (PAP2) was originally identified as a plasma membrane enzyme that catalyses the dephosphorylation of the putative second messenger, phosphatidic acid (PA) to diacylglycerol (DG) . Subsequently, multiple isoforms of PAP2 were cloned [2-5]. It was found that these enzymes dephosphorylate a number of lipid phosphates in vitro other than PA, including the potent bioactive lipids, lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P). Therefore, they have been renamed lipid phosphate phosphatases (LPPs). Currently, there are four members of this family called LPP1, LPP1a, LPP2 and LPP3 . _x000B_ S1P  and LPA  regulate the proliferation, differentiation, apoptosis and migration of cells by binding to a family of G protein-coupled receptors. Thus, EDG1/S1P1, EDG3/S1P3, EDG5/S1P2/AGR16/H218, EDG6/S1P4 and EDG8/S1P5/nrg-1 are high affinity S1P receptors  whereas EDG2/LPA1, EDG4/LPA2 and EDG7/LPA3 have high affinity for LPA . _x000B_ Recently, the over-expression of LPP1 was shown to limit LPA-stimulated signalling in Rat2 fibroblasts  and LPA-stimulated DNA synthesis in HEK 293 cells . Similarly, over-expression of LPP1, LPP1a and LPP2 attenuate S1P-signalling to the p42/p44 mitogen activated protein kinase cascade .
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