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Vol. 57, Issue 4, 753-759, April 2000
Departments of Pharmacology (D.-S.I., C.E.H., K.R.L.) and Urology
and Molecular Physiology and Biological Physics (M.A.H., D.T.),
University of Virginia School of Medicine, Charlottesville, Virginia;
and Department of Pharmacology (S.R.G., B.F.O.), University of Toronto,
Toronto, Ontario, Canada
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 Gi2
protein DNAs show
lysophosphatidic acid dose-dependent increases in
[
-35S]GTP binding with an EC50 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
Gq/11 proteins.
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