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Titolo:
THE ALPHA-V-BETA-5 INTEGRIN FUNCTIONS AS AN ENDOCYTIC RECEPTOR FOR VITRONECTIN
Autore:
MEMMO LM; MCKEOWNLONGO P;
Indirizzi:
ALBANY MED COLL,CELL & MOL BIOL PROGRAM,47 NEW SCOTLAND AVE ALBANY NY12208 ALBANY MED COLL,CELL & MOL BIOL PROGRAM ALBANY NY 12208 ALBANY MED COLL,DEPT PHYSIOL & CELL BIOL ALBANY NY 12208
Titolo Testata:
Journal of Cell Science
, volume: 111, anno: 1998,
parte:, 4
pagine: 425 - 433
SICI:
0021-9533(1998)111:<425:TAIFAA>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR INHIBITOR; SOMATOMEDIN-B DOMAIN; MEDIATED ENDOCYTOSIS; ALPHA(V)BETA(5) INTEGRIN; PHOSPHATIDYLINOSITOL 3-KINASE; ADHESIVE PROTEIN; TYROSINE KINASE; CELL-MIGRATION; HT-1080 CELLS; IN-VIVO;
Keywords:
VITRONECTIN; ALPHA(V)BETA(5) INTEGRIN; ENDOCYTOSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
L.M. Memmo e P. Mckeownlongo, "THE ALPHA-V-BETA-5 INTEGRIN FUNCTIONS AS AN ENDOCYTIC RECEPTOR FOR VITRONECTIN", Journal of Cell Science, 111, 1998, pp. 425-433

Abstract

Endocytosis and degradation of vitronectin by human skin fibroblasts are regulated by the beta(5) integrin. To determine whether the beta(5) integrin is directly mediating the internalization of vitronectin, both vitronectin and the beta(5) integrin were localized by indirect immunofluorescence during the endocytic process. This analysis showed that both vitronectin and beta(5) were found in intracellular vesicles within 5 minutes of the addition of exogenous vitronectin to fibroblastcell layers, By 15 minutes, approximately 20% of the vitronectin-containing vesicles stained positively for beta(5). In contrast, the beta(3) integrin was not found in any intracellular vesicles. Within 30 minutes, more than 50% of vitronectin-containing vesicles also stained for lamp-1, indicating that internalized vitronectin traveled to lysosomes. Inhibition of clathrin assembly by either potassium depletion or hypertonic buffer inhibited vitronectin internalization, suggesting that vitronectin internalization occurred through coated pits. Confocal analysis confirmed the colocalization of vitronectin and alpha(v) beta(5) in intracellular compartments and further demonstrated that the highest colocalization of the two proteins occurred within 1.8 mu m from the ventral surface of the cell, suggesting endocytosis occurred at the substrate level, Pretreatment of cells with the PI-3 kinase inhibitor, wortmannin, resulted in a marked increase in the coincidence of vitronectin and beta(5) staining within vesicles and prevented the accumulation of vitronectin within lysosomes. This suggests that following internalization, vitronectin and the alpha(v) beta(5) integrin are segregated to different cellular compartments. This study provides the first evidence that the alpha(v) beta(5) vitronectin receptor directly mediates the internalization of vitronectin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 19:17:35