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J Biol Chem, Vol. 274, Issue 39, 27351-27358, September 24, 1999
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From the Sphingosine 1-phosphate (S1P) is one of several
bioactive phospholipids that exert profound mitogenic and morphogenic
actions. Originally characterized as a second messenger, S1P is now
recognized to achieve many of its effects through cell surface, G
protein-coupled receptors. We used a subunit-selective
[35S]GTP Department of Pharmacology, University of
Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, the
§ Department of Physiology, University of Connecticut School
of Medicine, Farmington, Connecticut 06030, and the
¶ Department of Medicine, University of California at San
Francisco, San Francisco, California 94143
S binding assay to investigate whether
the variety of actions exerted through Edg-1, a recently identified
receptor for S1P, might be achieved through multiple G proteins. We
found, employing both Sf9 and HEK293 cells, that Edg-1 activates
only members of the Gi family, and not Gs,
Gq, G12, or G13. We additionally
established that Edg-1 activates Gi in response not only to
S1P but also sphingosylphosphorylcholine; no effects of
lysophosphatidic acid through Edg-1 were evident. Our assays further
revealed a receptor(s) for S1P endogenous to HEK293 cells that mediates
activation of G13 as well as Gi. Because several of the biological actions of S1P are assumed to proceed through
the G12/13 family, we tested whether Edg-3 and H218/Edg-5, two other receptors for S1P, might have a broader coupling profile than
Edg-1. Indeed, Edg-3 and H218/Edg-5 communicate not only with
Gi but also with Gq and G13. These
studies represent the first characterization of S1P receptor activity
through G proteins directly and establish fundamental differences in coupling.
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