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Titolo:
ADHESION TO FIBRONECTIN PRIMES EOSINOPHILS VIA ALPHA(4) BETA(1) (VLA-4)/
Autore:
ANWAR ARE; WALSH GM; CROMWELL O; KAY AB; WARDLAW AJ;
Indirizzi:
NATL HEART & LUNG INST,DEPT ALLERGY & CLIN IMMUNOL,DOVEHOUSE ST LONDON SW3 6LY ENGLAND NATL HEART & LUNG INST,DEPT ALLERGY & CLIN IMMUNOL LONDON SW3 6LY ENGLAND
Titolo Testata:
Immunology
fascicolo: 2, volume: 82, anno: 1994,
pagine: 222 - 228
SICI:
0019-2805(1994)82:2<222:ATFPEV>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
VASCULAR ENDOTHELIAL-CELLS; HUMAN NEUTROPHIL ADHERENCE; PLASMA FIBRONECTIN; INTEGRIN RECEPTOR; IDENTIFICATION; FAMILY; ATTACHMENT; DISTINCT; BINDING; HETERODIMERS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
A.R.E. Anwar et al., "ADHESION TO FIBRONECTIN PRIMES EOSINOPHILS VIA ALPHA(4) BETA(1) (VLA-4)/", Immunology, 82(2), 1994, pp. 222-228

Abstract

Human peripheral blood eosinophils adhered specifically to microtitreplates coated with plasma fibronectin (Fn) in a dose- and time-dependent fashion. Adhesion was optimal at 60 min at a concentration of 100 mu g/ml. Adherence to Fn was up-regulated by platelet-activating factor (PAF; optimum concentration of 10(-6) M) and was significantly inhibited by a polyclonal anti-Fn antibody (P < 0.05). The following evidence suggested that eosinophil adhesion to Fn was mediated by alpha(4) beta(1): (1) eosinophil adherence to Fn was not inhibited by an Arg-Gly-Asp-Ser (RGDS) synthetic peptide; (2) there was a dose-dependent adherence of eosinophils to microtitre plates coated with the 40,000 MW proteolytic fragment of Fn that contains the CS-1 alpha(4) beta(1) binding region, whereas adherence to the 120,000 MW chymotryptic fragment of Fn, which contains the RGD-dependent binding site, was weak and onlyobserved at high concentrations (> 250 mu g/ml); (3) significant inhibition of eosinophil adherence to Fn was achieved by monoclonal antibodies (mAb) against the alpha chain of VLA-4 but not by a mAb against CD45 or a mouse myeloma antibody as negative controls. After adhesion to Fn, eosinophils were investigated for their capacity to release leukotriene C-4 in response to stimulation with a suboptimal concentrationof calcium ionophore (2 x 10(-6) M). Significant enhancement of release was detected with Fn-coated plates but not with the control bovine serum albumin (BSA) (P < 0 .01). Furthermore, this enhancement was significantly inhibited by the alpha(4) beta(1) mAb HP2/1 (P < 0.05) but not by an anti-CD45 mAb. From these studies we conclude that (1) alpha(4) beta(1) (VLA-4) integrin is a major receptor for Fn on human eosinophils and (2) adhesion to Fn may prime eosinophils for mediator release during allergic inflammation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:52:33