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Titolo:
Soluble fibronectin interaction with cell surface and extracellular matrixis mediated by carbohydrate-to-carbohydrate interaction
Autore:
Zheng, MZ; Hakomori, S;
Indirizzi:
Pacific NW Res Inst, Seattle, WA 98122 USA Pacific NW Res Inst Seattle WAUSA 98122 Res Inst, Seattle, WA 98122 USA Univ Washington, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 iv Washington, Seattle, WA 98195 USA Albany Med Coll, Dept Physiol & Cell Biol, Albany, NY 12208 USA Albany MedColl Albany NY USA 12208 iol & Cell Biol, Albany, NY 12208 USA
Titolo Testata:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
fascicolo: 1, volume: 374, anno: 2000,
pagine: 93 - 99
SICI:
0003-9861(20000201)374:1<93:SFIWCS>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPHA-5-BETA-1 INTEGRIN RECEPTOR; REACTIVE PROTEINS GLYCOSIDASES; MASS-SPECTROMETRY; ADHESION; RECOGNITION; BINDING; DOMAIN; GLYCOSYLATION; ASSOCIATION; COLLAGEN;
Keywords:
fibronectin; soluble-form fibronectin; glycosphingolipid; carbohydrate-to-carbohydrate interaction; disialyl-I; Gg3; integrin-independent process;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Hakomori, S Pacific NW Res Inst, 720 Broadway, Seattle, WA 98122 USA Pacific NW Res Inst 720 Broadway Seattle WA USA 98122 8122 USA
Citazione:
M.Z. Zheng e S. Hakomori, "Soluble fibronectin interaction with cell surface and extracellular matrixis mediated by carbohydrate-to-carbohydrate interaction", ARCH BIOCH, 374(1), 2000, pp. 93-99

Abstract

Cell adhesion and spreading on solid phase fibronectin (FN), coated on plate or presented in extracellular matrix, are mediated by integrin receptorsalpha 5 beta 1, alpha 4 beta 1, etc., although binding of ''soluble-form F'' to cell surface varies extensively depending on glycosylation status of FN per se. Deposition or incorporation at the cell surface or pericellular matrix of soluble-form FN from body fluids or synthesized de novo takes place through a yet-unknown (perhaps integrin-independent) mechanism. Here we present evidence that the mechanism involves carbohydrate-to-carbohydrate interaction. Binding or incorporation of soluble-form placental or hepatoma FN to cell surface or pericellular matrix is highly dependent on the specific glycosylation status of FN per se and combination with glycosylation status of the cell surface, and is greatly promoted by a certain type of coexisting (shedded) glycosphingolipid, A few lines of study indicate that the process is mediated by interaction of FN carbohydrate with cell surface carbohydrate. The great enhancement of the binding process by glycosphingolipidis based on dual interaction of glycosphingolipid carbohydrate with FN carbohydrate and with cell surface carbohydrate. Here we present an example ofpromotion of binding of soluble-form FN from placenta or from hepatoma cells, having a specific carbohydrate epitope termed ''disialyl-I,'' to K562 or VA13 cell surface in the presence of glycosphingolipid Gg3, which interacts specifically with disialyl-I. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 13:28:10