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Titolo:
Sialidase treatment exposes the beta 1-integrin active ligand binding siteon HL60 cells and increases binding to fibronectin
Autore:
Pretzlaff, RK; Xue, VW; Rowin, ME;
Indirizzi:
Childrens Med Ctr, Div Crit Care Med, Dayton, OH 45404 USA Childrens Med Ctr Dayton OH USA 45404 Crit Care Med, Dayton, OH 45404 USA Childrens Hosp, Med Ctr, Div Crit Care Med, Cincinnati, OH 45229 USA Childrens Hosp Cincinnati OH USA 45229 Care Med, Cincinnati, OH 45229 USA
Titolo Testata:
CELL ADHESION AND COMMUNICATION
fascicolo: 6, volume: 7, anno: 2000,
pagine: 491 - 500
SICI:
1061-5385(2000)7:6<491:STETB1>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
O-LINKED OLIGOSACCHARIDES; ALTERED GLYCOSYLATION; HUMAN-NEUTROPHILS; HL-60 CELLS; ADHESION MOLECULES; INTEGRIN RECEPTOR; BETA-1 INTEGRINS; REPERFUSION; ACTIVATION; ACID;
Keywords:
beta 1-integrin; extracellular matrix; glycosidase; neutrophil; sialidase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Pretzlaff, RK Childrens Med Ctr, Div Crit Care Med, 1 Childrens Plaza, Dayton, OH 45404 USA Childrens Med Ctr 1 Childrens Plaza Dayton OH USA 45404 USA
Citazione:
R.K. Pretzlaff et al., "Sialidase treatment exposes the beta 1-integrin active ligand binding siteon HL60 cells and increases binding to fibronectin", CELL AD COM, 7(6), 2000, pp. 491-500

Abstract

The migration of neutrophils from the circulation to areas of inflammationis the result of the sequential activation of multiple cellular adhesion molecules. beta 1-Integrins are cell surface glycoproteins and the class of adhesion molecules responsible for binding to the extracellular matrix. Thegoal of this study was to determine the contribution of glycosylation, specifically the presence of sialic acid, to beta 1-integrin adhesion in a neutrophil model. beta 1-Integrins on differentiated HL60 cells were remodeledby treatment with the exoglycosidases, sialidase and beta-galactosidase. beta 1-Integrin activity was determined by measuring adherence to the extracellular matrix protein fibronectin. The expression of beta 1-integrins, beta 2-integrins and activated beta 1-integrins was determined by flow cytometry, Remodeling of beta 1 -integrins by treatment with sialidase increased adhesion by greater than 100%. Flow cytometric analysis of remodeled beta 1-integrins demonstrated an increased expression of the activated beta 1-integrin, but only minor increases in the expression of total beta 1- and beta 2-integrins. We postulate that glycosidase treatment increases adhesion andexpression of activated beta 1-integrins by exposure of the normally hidden ligand-binding site, The glycosylation of beta 1-integrins on neutrophilsmay act to hide the ligand-binding site in unstimulated cells thereby contributing to the affinity modulation observed in neutrophil beta 1-integrin function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 14:24:13