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Papers In Press, published online ahead of print January 9, 2001
Center for Vascular Biology, Dept of Physiology, Univ. Connecticut Health Center, Farmington, CT 06030
Corresponding Author: hla{at}sun.uchc.edu
Sphingosine-1-phosphate (SPP), a platelet-derived bioactive lysophospholipid, is a regulator of angiogenesis. However, molecular mechanisms involved in SPP-induced angiogenic responses are not fully defined. Here we report the molecular mechanisms involved in SPP-induced human umbilical vein endothelial cell (HUVEC) adhesion and migration. SPP-induced HUVEC migration is potently inhibited by antisense phosphothioate oligonucleotides (PTO) against EDG-1 as well as EDG-3 receptors. In addition, C3 exotoxin blocked SPP-induced cell attachment, spreading and migration on fibronectin-, vitronectin- and Matrigel-coated surfaces, suggesting that EDG receptor signaling via the Rho pathway is critical for SPP-induced cell migration. Indeed, SPP induced Rho activation in an adherence-independent manner whereas Rac activation was dispensible for cell attachment and focal contact formation. Interestingly, both EDG-1 and -3 receptors were required for Rho activation. Since integrins are critical for cell adhesion, migration and angiogenesis, we examined the effects of blocking antibodies against avb3 or b1 or ß3 integrins. SPP induced Rho-dependent integrin clustering into focal contact sites, which was essential for cell adhesion, spreading and migration. Blockage of avb3 or b1-containing integrins inhibited SPP-induced HUVEC migration. Together our results suggest that EDG receptor-mediated Rho signaling is required for the activation of integrin avb3 as well as b1-containing integrins, leading to the formation of initial focal contacts and endothelial cell migration.
J. Biol. Chem, 10.1074/jbc.M009422200
Submitted on October 16, 2000
Revised on January 8, 2001
Accepted on January 9, 2001
Sphingosine-1-phosphate induced endothelial cell migration requires the expression of EDG-1 and EDG-3 receptors and Rho-dependent activation of avß3 and ß1-containing integrins
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