Sphingosylphosphorylcholine is a ligand for ovarian cancer G-protein-coupled receptor 1
Y Xu, K Zhu, G Hong, W Wu, LM Baudhuin, Y Xiao… - Nature cell …, 2000 - nature.com
Y Xu, K Zhu, G Hong, W Wu, LM Baudhuin, Y Xiao, DS Damron
Nature cell biology, 2000•nature.comSphingosylphosphorylcholine (SPC) is a bioactive lipid that acts as an intracellular and
extracellular signalling molecule in numerous biological processes. Many of the cellular
actions of SPC are believed to be mediated by the activation of unidentified G-protein-
coupled receptors. Here we show that SPC is a high-affinity ligand for an orphan receptor,
ovarian cancer G-protein-coupled receptor 1 (OGR1). In OGR1-transfected cells, SPC binds
to OGR1 with high affinity (K d= 33.3 nM) and high specificity and transiently increases …
extracellular signalling molecule in numerous biological processes. Many of the cellular
actions of SPC are believed to be mediated by the activation of unidentified G-protein-
coupled receptors. Here we show that SPC is a high-affinity ligand for an orphan receptor,
ovarian cancer G-protein-coupled receptor 1 (OGR1). In OGR1-transfected cells, SPC binds
to OGR1 with high affinity (K d= 33.3 nM) and high specificity and transiently increases …
Abstract
Sphingosylphosphorylcholine (SPC) is a bioactive lipid that acts as an intracellular and extracellular signalling molecule in numerous biological processes. Many of the cellular actions of SPC are believed to be mediated by the activation of unidentified G-protein-coupled receptors. Here we show that SPC is a high-affinity ligand for an orphan receptor, ovarian cancer G-protein-coupled receptor 1 (OGR1). In OGR1-transfected cells, SPC binds to OGR1 with high affinity (K d= 33.3 nM) and high specificity and transiently increases intracellular calcium. The specific binding of SPC to OGR1 also activates p42/44 mitogen-activated protein kinases (MAP kinases) and inhibits cell proliferation. In addition, SPC causes internalization of OGR1 in a structurally specific manner.
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