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Lipid phosphate phosphatase-1 dephosphorylates exogenous lysophosphatidate and thereby attenuates its effects on cell signalling

The serum-derived phospholipid growth factor, lysophosphatidate (LPA), activates cells through a family of G-protein-coupled EDG receptors. The present article examines the role of lipid phosphate phosphatase-1 (LPP-1, or phosphatidate phosphate 2A) in regulating cell activation by LPA. Over-express...

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Bibliographic Details
Published in:Prostaglandins & other lipid mediators 2001-04, Vol.64 (1), p.83-92
Main Authors: Pilquil, Carlos, Singh, Indrapal, Zhang, Qiu-Xia, Ling, Zong-Chao, Buri, Katherine, Stromberg, Lana M., Dewald, Jay, Brindley, David N.
Format: Article
Language:English
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Summary:The serum-derived phospholipid growth factor, lysophosphatidate (LPA), activates cells through a family of G-protein-coupled EDG receptors. The present article examines the role of lipid phosphate phosphatase-1 (LPP-1, or phosphatidate phosphate 2A) in regulating cell activation by LPA. Over-expressing LPP-1 approximately doubled the rate of dephosphorylation of exogenous LPA by Rat2 fibroblasts. The amount of LPA dephosphorylation was restricted to less than 10% of the total exogenous LPA. Over-expression of LPP-1 attenuated cell activation as indicated by diminished responses including cAMP, Ca 2+, activation of phospholipase D and ERK, DNA synthesis and cell division. LPP-1 therefore provides a novel level of regulation for controlling cell signalling by exogenous LPA.
ISSN:1098-8823
DOI:10.1016/S0090-6980(01)00101-0