Journal
BRITISH JOURNAL OF PHARMACOLOGY
Volume 134, Issue 1, Pages 6-9Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.bjp.0704278
Keywords
phosphatidate; lysophosphatidate; kinases; G-protein; signalling
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Several different molecular species of phosphatidic acid (PA) bind to a G-protein coupled receptor (GPCR) to induce activation of the p42/p44 mitogen-activated protein kinase (p42/p44 MAPK) pathway in HEK 293 cells. PA is active at low nanomolar concentrations and the response is sensitive to pertussis toxin (which uncouples GPCRs from G(i o)). The de-acylated product of PA, lysophosphatidic acid (LPA), which binds to members of the endothelial differentiation gene (EDG) family of receptors also stimulated p42/p44 MAPK in a pertussis toxin sensitive manner, but with an similar to 100-1000 fold lower potency compared with the different molecular species of PA. RT-PCR using gene-specific primers showed that HEK 293 cells express EDG2 and PSP24, the latter being a lipid binding GPCR out with the EDG cluster. We conclude that PA is a novel high potency GPCR agonist.
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