Lipid Phosphate Phosphatase-1 Regulates Lysophosphatidate-induced Fibroblast Migration by Controlling Phospholipase D2-dependent Phosphatidate Generation
作者： Carlos Pilquil , Jay Dewald , Anton Cherney , Irina Gorshkova , Gabor Tigyi
关键词:
摘要: Lysophosphatidate (LPA) stimulates cell migration and division through a family of G-protein-coupled receptors. Lipid phosphate phosphatase-1 (LPP1) regulates the degradation extracellular LPA as well intracellular accumulation lipid phosphates. Here we show that increasing catalytic activity LPP1 decreased pertussis toxin-sensitive stimulation fibroblast by an LPA-receptor agonist could not be dephosphorylated. Conversely, knockdown endogenous increased LPA-induced migration. However, did affect PDGF- or endothelin-induced fibroblasts in Transwell chamber "wound healing" assays. Thus, addition to degrading exogenous LPA, controls signaling downstream Consistent with this conclusion, expression phospholipase D (PLD) PDGF, phosphatidate accumulation. This effect was upstream PLD activation possible metabolism diacylglycerol. PLD(2) necessary for LPA-, but PDGF-induced Increased also important proteins involved These included ERK Rho, basal activities Rac Cdc42. Rho were targets activity. We conclude actions play functions regulating PLD2. formation. results shed new light on roles controlling wound healing growth metastasis tumors.
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