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J Biol Chem, Vol. 275, Issue 19, 14573-14578, May 12, 2000
From the Departments of Medicine and Microbiology-Immunology and
¶ Veterans Affairs Medical Center, University of California, San
Francisco, California 94143-0711 and § Department of
Medicine, Hematology Division, Brigham and Women's Hospital, Harvard
Medical School, Boston, Massachusetts 02115
Lysophosphatidic acid (LPA) in biological fluids
binds to serum albumin and other proteins that enhance its effects on
cellular functions. The actin-severing protein gelsolin binds LPA with an affinity (Kd = 6 nM) similar to that
of the G protein-coupled LPA receptors encoded by endothelial
differentiation genes 2, 4, and 7 (Edg-2, -4, and -7 receptors) and
greater than that of serum albumin (Kd = 360 nM). At concentrations of 10% or less of that in plasma,
which are observed in fluids of injured tissues, purified and
recombinant gelsolin augment LPA stimulation of nuclear signals and
protein synthesis in rat cardiac myocytes (RCMs) that express Edg-2 and
-4 receptors. At concentrations of 20% or more of that in plasma,
gelsolin suppresses LPA stimulation of RCMs. The lack of effect of
gelsolin on RCM responses to monoclonal anti-Edg-4 receptor antibody
plus a phorbol ester without LPA attests to its specificity for LPA
delivery and the absence of post-receptor effects. Inhibition of
gelsolin binding and cellular delivery of LPA by
L-
Gelsolin Binding and Cellular Presentation of
Lysophosphatidic Acid*
,
-phosphatidylinositol-4,5-bisphosphate (PIP2) and
peptides constituting the two PIP2 binding domains of gelsolin suggests
competition between LPA and PIP2 for the same sites. Thus, delivery of
LPA to RCMs is affinity-coupled to Edg receptors by gelsolin in a
PIP2-regulated process.
*
This work was supported in part by National Institutes of
Health Grants HL31809 (to E. J. G.) and HL54253 (to T. P. S.) and a
Merit Review grant from the Department of Veterans Affairs Research Service (to J. S. K.). These data were presented in part at the 1999 annual meeting of the American Society for Biochemistry and Molecular
Biology (41).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: University of
California, UB8B, Box 0711, 533 Parnassus, San Francisco, CA
94143-0711. Tel.: 415-476-5339; Fax: 415-476-6915; E-mail:
egoetzl@itsa.ucsf.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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