Source:http://linkedlifedata.com/resource/pubmed/id/10727522
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2000-5-4
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pubmed:abstractText |
Two G protein-coupled receptors (Edg-2) and (Edg-4) for the lysolipid phosphoric acid mediator lysophosphatidic acid have been described by molecular cloning. However, the calcium-mobilizing receptor Edg-4 is not expressed in some cell lines that exhibit robust calcium responses to this ligand, thus predicting the existence of additional receptor subtypes. We report here on the characterization of a third human lysophosphatidic acid receptor subtype, Edg-7, which mediates lysophosphatidic acid-evoked calcium mobilization. In a rat hepatoma Rh7777 cell line that lacks endogenous responses to lysophosphatidic acid, this lipid mediator, but not others, evokes calcium transients when the cells have been transfected with Edg-7 or Edg-4 DNAs. Furthermore, frog oocytes exhibit a calcium-mediated chloride conductance in response to mammalian-selective lysophosphatidic acid mimetics after injection of Edg-7 mRNA. Edg-7-expressing Rh7777 cells do not show inhibition of forskolin-driven rises in cAMP in response to lysophosphatidic acid. However, membranes from HEK293T cells cotransfected with Edg-7 and G(i2)alpha protein DNAs show lysophosphatidic acid dose-dependent increases in [gamma-(35)S]GTP binding with an EC(50) value of 195 nM. When we used this assay to compare various synthetic LPA analogs at Edg-2, Edg-4, and Edg-7 receptors, we found that ethanolamine-based compounds, which are full LPA mimetics at Edg-2 and Edg-4, exhibit little activity at the Edg-7 receptor. Edg-7 RNA was detected in extracts of several rat and human tissues including prostate. Together, our data indicate that Edg-7 is a third lysophosphatidic acid receptor that couples predominantly to G(q/11)alpha proteins.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0026-895X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
753-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10727522-Amino Acid Sequence,
pubmed-meshheading:10727522-Animals,
pubmed-meshheading:10727522-Base Sequence,
pubmed-meshheading:10727522-Cells, Cultured,
pubmed-meshheading:10727522-Cloning, Molecular,
pubmed-meshheading:10727522-DNA,
pubmed-meshheading:10727522-Humans,
pubmed-meshheading:10727522-Male,
pubmed-meshheading:10727522-Molecular Sequence Data,
pubmed-meshheading:10727522-Prostate,
pubmed-meshheading:10727522-Rats,
pubmed-meshheading:10727522-Receptors, Cell Surface,
pubmed-meshheading:10727522-Receptors, G-Protein-Coupled,
pubmed-meshheading:10727522-Receptors, Lysophosphatidic Acid,
pubmed-meshheading:10727522-Sequence Homology, Amino Acid
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pubmed:year |
2000
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pubmed:articleTitle |
Molecular cloning and characterization of a lysophosphatidic acid receptor, Edg-7, expressed in prostate.
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pubmed:affiliation |
Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, Virginia, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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