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Blood, Vol. 93 No. 9 (May 1), 1999:
pp. 2984-2990
Sphingosine 1-Phosphate Stimulates Fibronectin Matrix
Assembly Through a Rho-Dependent Signal Pathway
Qinghong Zhang,
Olivier Peyruchaud,
Kelly J. French,
Magnus K. Magnusson, and
Deane F. Mosher
From the Departments of Medicine and Biomolecular Chemistry,
University of Wisconsin-Madison, Madison, WI.
Fibronectin matrix assembly is a cell-dependent process mediated by
cell surface binding sites for the 70-kD N-terminal portion of
fibronectin. We have shown that Rho-dependent cytoskeleton reorganization induced by lysophosphatidic acid (LPA) or the
microtubule-disrupting agent nocodazole increases fibronectin binding
(Zhang et al, Mol Biol Cell 8:1415, 1997).
Sphingosine 1-phosphate (S1P) is a bioactive sphingolipid implicated in
mitogenesis and cytoskeletal remodelling. Both LPA and S1P are present
in increased amounts in serum as compared with plasma as a result of
platelet activation. Addition of S1P to human osteosarcoma MG63 cells
or human foreskin fibroblasts increased cell-mediated binding and
assembly of fibronectin. MG63 cells expressed the Edg-2 and Edg-4
G-protein-coupled receptors for bioactive lipids, whereas foreskin
fibroblasts expressed Edg-2, Edg-3, and Edg-4. The stimulatory effect
of S1P on the binding of fibronectin or the N-terminal 70-kD fragment
of fibronectin was dynamic and due to increases in both the number and
affinity of binding sites. The stimulation of 70-kD fragment binding by nanomolar S1P, like stimulation of binding by LPA or nocodazole, was
blocked by inactivation of Rho with C3 exotoxin but not by pertussis
toxin-mediated inactivation of Gi. These results indicate a common
signal pathway leading to control of cellular fibronectin matrix
assembly by bioactive lipids generated during blood coagulation.
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