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Titolo:
Glycosylation effect on membrane domain (GEM) involved in cell adhesion and motility: A preliminary note on functional alpha 3, alpha 5-CD82 glycosylation complex in ldlD 14 cells
Autore:
Ono, M; Handa, K; Withers, DA; Hakomori, SI;
Indirizzi:
Pacific NW Res Inst, Seattle, WA 98122 USA Pacific NW Res Inst Seattle WAUSA 98122 Res Inst, Seattle, WA 98122 USA Univ Washington, Dept Pathobiol, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 ept Pathobiol, Seattle, WA 98195 USA Univ Washington, Dept Microbiol, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 ept Microbiol, Seattle, WA 98195 USA
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 3, volume: 279, anno: 2000,
pagine: 744 - 750
SICI:
0006-291X(200012)279:3<744:GEOMD(>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPHA-5-BETA-1 INTEGRIN RECEPTOR; METASTASIS SUPPRESSOR GENE; MELANOMA B16 CELLS; PROTEINS; SURFACE; ASSOCIATION; FIBRONECTIN; FAMILY; CD81; CD9;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Ono, M Jichi Med Sch, Dept Surg, Minamimaki, Tochigiken 3290498, Japan Jichi Med Sch Minamimaki Tochigiken Japan 3290498 n 3290498, Japan
Citazione:
M. Ono et al., "Glycosylation effect on membrane domain (GEM) involved in cell adhesion and motility: A preliminary note on functional alpha 3, alpha 5-CD82 glycosylation complex in ldlD 14 cells", BIOC BIOP R, 279(3), 2000, pp. 744-750

Abstract

Laminin (LN)- or fibronectin (FN)-dependent adhesion in Krieger's ldlD 14 (D14) cells is enhanced significantly in the presence vs absence, of galactose (Gal), whereas LN- or FN-induced haptotactic cell motility is barely affected unless cells express CD82 by its gene transfection (cells termed D14/CD82), The effect of CD82 on LN- or FN-induced motility is based on its ability to associate with alpha3 or alpha5 integrin to form a complex associated with a low-density lipid membrane domain (termed GEM or GSD), Complex formation is greatly affected by N-glycosylation of both integrin and CD82, as well as by concurrent GM3 ganglioside synthesis. The effect of glycosylation on alpha5-CD82 complex was also studied in D14 cells expressing mutantCD82, defective in all three N-glycosylation sites. LN-induced motility was greatly inhibited, whereas FN-induced motility was enhanced, with complete N-glycosylation in D14/CD82 cells in Gal-added medium, whereby alpha5-CD82 complex formation did not occur or occurred at a minimal level, Both LN- and FN-induced motility were inhibited when N-glycosylation was impaired, or N-glycosylation of CD82 was deleted, whereby alpha5-CD82 complex formation occurred strongly. Thus, glycosylation profoundly affects interaction of integrin with CD82, leading to significant inhibition or promotion of cell motility, (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:24:12