%0 Journal Article %1 Koppen1996 %A van Koppen, C. %A zu Heringdorf, M. Meyer %A Laser, K. T. %A Zhang, C. %A Jakobs, K. H. %A Bunemann, M. %A Pott, L. %D 1996 %J J Biol Chem %K & *Lysophospholipids 3T3 5'-O-(3-Thiotriphosphate)/metabolism Acid/pharmacology Adenylate Animals Bordetella/pharmacology CHO Calcium/metabolism Cell Cercopithecus Channel Channels/physiology Cricetinae Cultured Cyclase Egtazic Factors, Forskolin/pharmacology GTP-Binding Gating Guanosine Guinea Heart/physiology Humans Ion Mice Muscarinic/physiology Pertussis Pigs Potassium Rats Signal Sphingosine/*analogs Surface/*metabolism Toxin Transduction Virulence aethiops derivatives/physiology Receptor Proteins/metabolism %N 4 %P 2082-7 %T Activation of a high affinity Gi protein-coupled plasma membrane receptor by sphingosine-1-phosphate %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8567663 %V 271 %X Sphingosine-1-phosphate (SPP) has attracted much attention as a possible second messenger controlling cell proliferation and motility and as an intracellular Ca(2+)-releasing agent. Here, we present evidence that SPP activates a G protein-coupled receptor in the plasma membrane of various cells, leading to increase in cytoplasmic Ca2+ concentration (Ca2+i), inhibition of adenylyl cyclase, and opening of G protein-regulated potassium channels. In human enbryonic kidney (HEK) cells, SPP potently (EC50, 2 nM) and rapidly increased Ca2+i in a pertussis toxin-sensitive manner. Pertussis toxin-sensitive increase in Ca2+i was also observed with sphingosylphosphorylcholine (EC50, 460 nM), whereas other sphingolipids, including ceramide-1-phosphate, N-palmitoyl-sphingosine, psychosine, and D-erythro-sphingosine at micromolar concentrations did not or only marginally increased Ca2+i. Furthermore, SPP inhibited forskolin-stimulated cAMP accumulation in HEK cells and increased binding of guanosine 5'3-O-(thio) triphosphate to HEK cell membranes. Rapid Ca2+i responses were also observed in human transitional bladder carcinoma (J82) cells, monkey COS-1 cells, mouse NIH 3T3 cells, Chinese hamster ovary (CHO-K1) cells, and rat C6 glioma cells, whereas human HL-60 leukemia cells and human erythroleukemia cells failed to respond to SPP. In guinea pig atrial myocytes, SPP activated Gi protein-regulated inwardly rectifying potassium channels. Activation of these channels occurred strictly when SPP was applied at the extracellular face of atrial myocyte plasma membrane as measured in cell-attached and inside-out patch clamp current recordings. We conclude that SPP, in addition to its proposed direct action on intracellular Ca2+ stores, interacts with a high affinity Gi protein-coupled receptor in the plasma membrane of apparently many different cell types.

@article{Koppen1996, abstract = {Sphingosine-1-phosphate (SPP) has attracted much attention as a possible second messenger controlling cell proliferation and motility and as an intracellular Ca(2+)-releasing agent. Here, we present evidence that SPP activates a G protein-coupled receptor in the plasma membrane of various cells, leading to increase in cytoplasmic Ca2+ concentration ([Ca2+]i), inhibition of adenylyl cyclase, and opening of G protein-regulated potassium channels. In human enbryonic kidney (HEK) cells, SPP potently (EC50, 2 nM) and rapidly increased [Ca2+]i in a pertussis toxin-sensitive manner. Pertussis toxin-sensitive increase in [Ca2+]i was also observed with sphingosylphosphorylcholine (EC50, 460 nM), whereas other sphingolipids, including ceramide-1-phosphate, N-palmitoyl-sphingosine, psychosine, and D-erythro-sphingosine at micromolar concentrations did not or only marginally increased [Ca2+]i. Furthermore, SPP inhibited forskolin-stimulated cAMP accumulation in HEK cells and increased binding of guanosine 5'3-O-(thio) triphosphate to HEK cell membranes. Rapid [Ca2+]i responses were also observed in human transitional bladder carcinoma (J82) cells, monkey COS-1 cells, mouse NIH 3T3 cells, Chinese hamster ovary (CHO-K1) cells, and rat C6 glioma cells, whereas human HL-60 leukemia cells and human erythroleukemia cells failed to respond to SPP. In guinea pig atrial myocytes, SPP activated Gi protein-regulated inwardly rectifying potassium channels. Activation of these channels occurred strictly when SPP was applied at the extracellular face of atrial myocyte plasma membrane as measured in cell-attached and inside-out patch clamp current recordings. We conclude that SPP, in addition to its proposed direct action on intracellular Ca2+ stores, interacts with a high affinity Gi protein-coupled receptor in the plasma membrane of apparently many different cell types.}, added-at = {2010-12-14T18:12:02.000+0100}, author = {van Koppen, C. and zu Heringdorf, M. Meyer and Laser, K. T. and Zhang, C. and Jakobs, K. H. and Bunemann, M. and Pott, L.}, biburl = {https://www.bibsonomy.org/bibtex/289420321d68e4bdc472c0b714b0ff784/pharmawuerz}, endnotereftype = {Journal Article}, interhash = {f50e5f967595948ff77b14f3c9c44577}, intrahash = {89420321d68e4bdc472c0b714b0ff784}, issn = {0021-9258 (Print) 0021-9258 (Linking)}, journal = {J Biol Chem}, keywords = {& *Lysophospholipids 3T3 5'-O-(3-Thiotriphosphate)/metabolism Acid/pharmacology Adenylate Animals Bordetella/pharmacology CHO Calcium/metabolism Cell Cercopithecus Channel Channels/physiology Cricetinae Cultured Cyclase Egtazic Factors, Forskolin/pharmacology GTP-Binding Gating Guanosine Guinea Heart/physiology Humans Ion Mice Muscarinic/physiology Pertussis Pigs Potassium Rats Signal Sphingosine/*analogs Surface/*metabolism Toxin Transduction Virulence aethiops derivatives/physiology Receptor Proteins/metabolism}, month = {Jan 26}, note = {van Koppen, C Meyer zu Heringdorf, M Laser, K T Zhang, C Jakobs, K H Bunemann, M Pott, L Research Support, Non-U.S. Gov't United states The Journal of biological chemistry J Biol Chem. 1996 Jan 26;271(4):2082-7.}, number = 4, pages = {2082-7}, shorttitle = {Activation of a high affinity Gi protein-coupled plasma membrane receptor by sphingosine-1-phosphate}, timestamp = {2010-12-14T18:21:43.000+0100}, title = {Activation of a high affinity Gi protein-coupled plasma membrane receptor by sphingosine-1-phosphate}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8567663}, volume = 271, year = 1996 }