Source:http://linkedlifedata.com/resource/pubmed/id/10818438
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2000-6-5
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pubmed:abstractText |
The bioactive lipid sphingosine-1-phosphate (SPP) is abundantly formed and released during the activation of platelets by thrombotic stimuli. Once exported, SPP interacts with the G-protein-coupled receptors (GPCR) of the EDG-1 family. SPP binds to EDG-1 with the dissociation constant of approximately 8 nM and induces signal transduction events such as mitogen-activated protein kinase (MAP kinase) activation, decrease of cAMP levels, remodeling of the actin cytoskeleton, among others. EDG-1 is a prototypical member of a large family of GPCRs that interact with glycero- and sphingolysolipid phosphates, namely, SPP and lysophosphatidic acid (LPA). Three other GPCRs, trivially termed EDG-3, EDG-5, and EDG-8, are also high-affinity receptors for SPP. The four SPP receptor subtypes regulate different intracellular signal transduction pathways. In vascular endothelial cells, cooperative signaling between EDG-1 and EDG-3 subtypes of SPP receptors results in adherens junction assembly, cell survival, morphogenesis into capillary-like networks, and angiogenesis. SPP acts distinctly, albeit cooperatively, with polypeptide angiogenic factors, resulting in the formation of mature neovessels. Thus SPP signaling as an extracellular mediator via the EDG-1 family of GPCRs may be a heretofore unrecognized mechanism for the regulation of angiogenesis and vascular endothelial cell function.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lysophospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lysophospholipid,
http://linkedlifedata.com/resource/pubmed/chemical/Sphingosine,
http://linkedlifedata.com/resource/pubmed/chemical/sphingosine 1-phosphate
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0077-8923
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
905
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16-24
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10818438-Evolution, Molecular,
pubmed-meshheading:10818438-GTP-Binding Proteins,
pubmed-meshheading:10818438-Humans,
pubmed-meshheading:10818438-Immediate-Early Proteins,
pubmed-meshheading:10818438-Lysophospholipids,
pubmed-meshheading:10818438-Receptors, Cell Surface,
pubmed-meshheading:10818438-Receptors, G-Protein-Coupled,
pubmed-meshheading:10818438-Receptors, Lysophospholipid,
pubmed-meshheading:10818438-Signal Transduction,
pubmed-meshheading:10818438-Sphingosine
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pubmed:year |
2000
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pubmed:articleTitle |
Sphingosine-1-phosphate signaling via the EDG-1 family of G-protein-coupled receptors.
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pubmed:affiliation |
Department of Physiology, University of Connecticut Health Center, Farmington 06030-3501, USA. hla@sun.uchc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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