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Vol. 54, Issue 5, 881-888, November 1998
Departments of Medicine and Microbiology-Immunology, University of
California, San Francisco, California 94143-0711
Mobilization of intracellular Ca2+ is a critical cellular
response to lysophosphatidic acid (LPA) in many cell types. Recent identification of endothelial differentiation gene (Edg) 2 and Edg4 as
subtypes of G protein-coupled receptors for LPA allowed examination of
the Ca2+ mobilization mediated specifically by each
subtype. To reduce endogenous background levels while enhancing
recombinant receptor-specific signals, the aequorin luminescence method
was used to quantify cytoplasmic Ca2+ levels. In TAg-Jurkat
T cells transiently co-transfected with apoaequorin and human Edg2 or
Edg4 cDNA, LPA dose-dependently increased light emission triggered by
increased Ca2+ bound to aequorin.
N-Palmitoyl-L-serine-phosphoric acid and
N-palmitoyl-L-tyrosine-phosphoric acid,
which had been previously shown to be antagonists for Xenopus laevis LPA receptors, did not antagonize the
Ca2+-mobilizing effects of Edg2 and Edg4. Surprisingly,
they acted as agonists or partial agonists for Edg2 and Edg4. The
Ca2+ mobilization by Edg2 and Edg4 was further
characterized in stable transfectants of rat HTC4 hepatoma cells. By
using the fura-2 fluorescence method, a difference in the kinetics of
Ca2+ flux with Edg2 and Edg4 was observed. With Edg2, but
not Edg4, the initial increase in the Ca2+ concentration
was followed by a sustained influx of extracellular Ca2+.
The coincident production of inositol phosphates and the inhibition of
Ca2+ mobilization by the phospholipase C inhibitor U73122
strongly suggested that Edg2 and Edg4 mobilize Ca2+ through
inositol trisphosphate generated by phospholipase C activation. Pertussis toxin almost completely blocked LPA-induced Ca2+
mobilization by Edg2 but only partially blocked that by Edg4, which
suggests that Edg2 transduces Ca2+ mobilization largely
through pertussis toxin-sensitive Gi proteins, whereas Edg4
requires both Gi and Gq.
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