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Titolo:
Rac recruits high-affinity integrin alpha v beta 3 to lamellipodia in endothelial cell migration
Autore:
Kiosses, WB; Shattil, SJ; Pampori, N; Schwartz, MA;
Indirizzi:
Dept Vasc Biol, La Jolla, CA 92037 USA Dept Vasc Biol La Jolla CA USA 92037 pt Vasc Biol, La Jolla, CA 92037 USA Dept Expt Med, La Jolla, CA 92037 USA Dept Expt Med La Jolla CA USA 92037Dept Expt Med, La Jolla, CA 92037 USA
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 3, volume: 3, anno: 2001,
pagine: 316 - 320
SICI:
1465-7392(200103)3:3<316:RRHIAV>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADHESION RECEPTOR; RHO-GTPASES; ALPHA(V)BETA(3); 3-KINASE; LIGAND; IIIA; CYTOSKELETON; VITRONECTIN; INHIBITION; FIBRINOGEN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Kiosses, WB Dept Vasc Biol, 10550 N torrey Pines Rd, La Jolla, CA 92037 USA Dept Vasc Biol 10550 N torrey Pines Rd La Jolla CA USA 92037 A
Citazione:
W.B. Kiosses et al., "Rac recruits high-affinity integrin alpha v beta 3 to lamellipodia in endothelial cell migration", NAT CELL BI, 3(3), 2001, pp. 316-320

Abstract

Integrin alphav beta3 has an important role in the proliferation, survival, invasion and migration of vascular endothelial cells(1,2). Like other integrins, alphav beta3 can exist in different functional states with respect to ligand binding. These changes involve both affinity modulation, by whichconformational changes in the integrin heterodimer govern affinity for individual extracellular matrix proteins, and avidity modulation, by which changes in lateral mobility and integrin clustering affect the binding of cells to multivalent matrices. Here we have used an engineered monoclonal antibody Fab (antigen-binding fragment) named WOW-1, which binds to activated integrins alphav beta3 and alphav beta5 from several species(3), to investigate the role of alphav beta3 activation in endothelial cell behaviour. Because WOW-1 is monovalent, it is insensitive to changes in integrin clusteringand therefore reports only changes in affinity. WOW-1 contains an RGD tract in its variable region and binds only to unoccupied, high-affinity integrins. By using WOW-1, we have identified the selective recruitment of high-affinity integrins as a mechanism by which lamel-lipodia promote formation of new adhesions at the leading edge in cell migration.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 13:21:37