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Titolo:
G(i)-mediated Cas tyrosine phosphorylation in vascular endothelial cells stimulated with sphingosine 1-phosphate - Possible involvement in cell motility enhancement in cooperation with Rho-mediated pathways
Autore:
Ohmori, T; Yatomi, Y; Okamoto, H; Miura, Y; Rile, G; Satoh, K; Ozaki, Y;
Indirizzi:
Yamanashi Med Univ, Dept Lab Med, Yamanashi 4093898, Japan Yamanashi Med Univ Yamanashi Japan 4093898 Med, Yamanashi 4093898, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 7, volume: 276, anno: 2001,
pagine: 5274 - 5280
SICI:
0021-9258(20010216)276:7<5274:GCTPIV>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
FOCAL ADHESION KINASE; MULTIPLE SIGNALING PATHWAYS; G-PROTEIN; C-SRC; LYSOPHOSPHATIDIC ACID; MONOCLONAL-ANTIBODY; SURFACE-RECEPTOR; HUMAN PLATELETS; V-SRC; P130(CAS);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Yatomi, Y Yamanashi Med Univ, Dept Lab Med, Yamanashi 4093898, Japan Yamanashi Med Univ Yamanashi Japan 4093898 ashi 4093898, Japan
Citazione:
T. Ohmori et al., "G(i)-mediated Cas tyrosine phosphorylation in vascular endothelial cells stimulated with sphingosine 1-phosphate - Possible involvement in cell motility enhancement in cooperation with Rho-mediated pathways", J BIOL CHEM, 276(7), 2001, pp. 5274-5280

Abstract

Since blood platelets release sphingosine 1-phosphate (Sph-1-P) upon activation, it is important to examine the effects of this bioactive lipid on vascular endothelial cell functions from the viewpoint of platelet-endothelial cell interactions. In the present study, we examined Sph-1-P-stimulated signaling pathways related to human umbilical vein endothelial cell (HUVEC) motility, with a special emphasis on the cytoskeletal docking protein Crk-associated substrate (Cas). Sph-1-P stimulated tyrosine phosphorylation of Gas, which was inhibited by the Gi inactivator pertussis toxin but not by the Rho inactivator C3 exoenzyme or the Rho kinase inhibitor Y-27632. Fyn constitutively associated with and phosphorylated Gas, suggesting that Gas tyrosine phosphorylation may be catalyzed by Fyn. Furthermore, upon HUVEC stimulation with Sph-1-P, Crk, through its SH2 domain, interacted with tyrosine-phosphorylated Gas, and the Cas-Crk complex translocated to the cell periphery (membrane ruffles), through mediation of Gi (Fyn) but not Rho. In contrast, tyrosine phosphorylation of focal adhesion kinase, and formation of stress fibers and focal adhesion were mediated by Rho but not G(i) (Fyn). Finally, Sph-1-P-enhanced HUVEC motility, assessed by a phagokinetic assay using gold sol-coated plates and a Boyden's chamber assay, was markedly inhibited not only by pertussis toxin (or the Fyn kinase inhibitor PP2) but alsoby C3 exoenzyme (or Y-27632). In HUVECs stimulated with Sph-1-P, these data suggest the following: (i) cytoskeletal signalings may be separable into G(i)-mediated signaling pathways (involving Gas) and Rho-mediated ones (involving FAK), and (ii) coordinated signalings from both pathways are required for Sph-1-P-enhanced HUVEC motility. Since HUVECs reportedly express the Sph-1-P receptors EDG-1 (coupled with G(i)) and EDG-3 (coupled with G(13) and G(q)) and the EDG-3 antagonist suramin was found to block specifically Rho-mediated responses, it is likely that Gas-related responses following G(i) activation originate from EDG-1, whereas Rho-related responses originatefrom EDG-3.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 08:56:58