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Titolo:
REGULATION OF BETA(1)-INTEGRIN FUNCTION IN CULTURED HUMAN VASCULAR SMOOTH-MUSCLE CELLS
Autore:
SEKI J; KOYAMA N; KOVACH NL; YEDNOCK T; CLOWES AW; HARLAN JM;
Indirizzi:
FUJISAWA PHARMACEUT CO LTD,NEW DRUG RES LABS,DEPT PHARMACOL,YODOGAWA KU,2-1-6 KASHIMA OSAKA 532 JAPAN HARBORVIEW MED CTR,DIV HEMATOL SEATTLE WA 00000 UNIV WASHINGTON,SCH MED,DEPT SURG SEATTLE WA 98195 ATHENA NEUROSCI INC S SAN FRANCISCO CA 94080
Titolo Testata:
Circulation research
fascicolo: 4, volume: 78, anno: 1996,
pagine: 596 - 605
SICI:
0009-7330(1996)78:4<596:ROBFIC>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-FACTOR RECEPTOR; EXTRACELLULAR-MATRIX; MONOCLONAL-ANTIBODY; ENDOTHELIAL-CELLS; ADHESION MOLECULE-1; INTEGRIN RECEPTOR; FOCAL ADHESIONS; FIBRONECTIN; MIGRATION; EXPRESSION;
Keywords:
ADHESION; MIGRATION; MONOCLONAL ANTIBODY; EXTRACELLULAR MATRIX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
67
Recensione:
Indirizzi per estratti:
Citazione:
J. Seki et al., "REGULATION OF BETA(1)-INTEGRIN FUNCTION IN CULTURED HUMAN VASCULAR SMOOTH-MUSCLE CELLS", Circulation research, 78(4), 1996, pp. 596-605

Abstract

Avidity modulation and function of beta(1)-integrin receptors in cultured human vascular smooth muscle cells (SMCs) were investigated usingmonoclonal antibody (mAb) 8A2, which binds to the beta(1) subunit of integrin heterodimers and induces a high avidity state. The adhesion of SMCs to extra cellular matrix proteins, but not to poly-L-lysine, was enhanced by pretreatment with mAb 8A2. A qualitative alteration of beta(1) integrin was assessed with mAb 15/7, which binds to an activation-dependent epitope on the beta(1) subunit. Binding of mAb 15/7 was enhanced by mAb 8A2 in a dose-dependent manner. Arg-Gly-Asp peptide andsoluble fibronectin also enhanced expression of the 15/7 epitope, suggesting that the 15/7 epitope is closely related to the ligand-occupied state of beta(1) integrin. Platelet-derived growth factor (PDGF)-AA and -BB increased SMC adhesion to type I collagen but did not augment mAb 15/7 binding, suggesting that PDGFs increase binding avidity bf a postreceptor mechanism. In addition mAb 8A2 inhibited PDGF-BB-induced SMC migration through Matri-gel-coated filters. These results suggest that avidity modulation of beta(1) integrin may play an important rolein the Function of SMCs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:35:31