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Titolo:
CHANGING LIGAND SPECIFICITIES OF ALPHA-V-BETA-1 AND ALPHA-V-BETA-3 INTEGRINS BY SWAPPING A SHORT DIVERSE SEQUENCE OF THE BETA-SUBUNIT
Autore:
TAKAGI J; KAMATA T; MEREDITH J; PUZONMCLAUGHLIN W; TAKADA Y;
Indirizzi:
SCRIPPS CLIN & RES INST,DEPT VASC BIOL,VB-1,10550 N TORREY PINES RD LA JOLLA CA 92037 SCRIPPS CLIN & RES INST,DEPT VASC BIOL LA JOLLA CA 92037
Titolo Testata:
The Journal of biological chemistry
fascicolo: 32, volume: 272, anno: 1997,
pagine: 19794 - 19800
SICI:
0021-9258(1997)272:32<19794:CLSOAA>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL ATTACHMENT; POINT MUTATION; GPIIB-IIIA; BINDING; ADHESION; ALPHA; FIBRONECTIN; EXPRESSION; DOMAIN; SITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
J. Takagi et al., "CHANGING LIGAND SPECIFICITIES OF ALPHA-V-BETA-1 AND ALPHA-V-BETA-3 INTEGRINS BY SWAPPING A SHORT DIVERSE SEQUENCE OF THE BETA-SUBUNIT", The Journal of biological chemistry, 272(32), 1997, pp. 19794-19800

Abstract

Integrins mediate signal transduction through interaction with multiple cellular or extracellular matrix ligands. Integrin alpha v beta 3 recognizes fibrinogen, von Willebrand factor, and vitronectin, while alpha v beta 1 does not. We studied the mechanisms for defining ligand specificity of these integrins by swapping the highly diverse sequencesin the I domain-like structure of the beta 1 and beta 3 subunits. When the sequence CTSEQNC (residues 187-193) of beta 1 is replaced with the corresponding CYD-MKTTC sequence of beta 3, the ligand specificity of alpha v beta 1 is altered. The mutant (alpha v beta 1-3-1), like alpha v beta 3, recognizes fibrinogen, von Willebrand factor, and vitronectin (a gain-of-function effect). The alpha v beta 1-3-1 mutant is recruited to focal contacts on fibrinogen and vitronectin, suggesting that the mutant transduces intracellular signals on adhesion. The reciprocal beta 3-1-3 mutation blocks binding of alpha v beta 3 to these multiple ligands and to LM609, a function-blocking anti-alpha v beta 3 antibody. These results suggest that the highly divergent sequence is a key determinant of integrin ligand specificity. Also, the data supporta recent hypothetical model of the I domain of beta, in which the sequence is located in the ligand binding site.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 05:08:43