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Titolo:
BASIC FIBROBLAST GROWTH-FACTOR (FGF-2) INTERNALIZATION THROUGH THE HEPARAN-SULFATE PROTEOGLYCANS-MEDIATED PATHWAY - AN ULTRASTRUCTURAL APPROACH
Autore:
GLEIZES PE; NOAILLACDEPEYRE J; AMALRIC F; GAS N;
Indirizzi:
LAB BIOL MOLEC EUCARYOTE,CNRS,UPR 9006,118 ROUTE NARBONNE F-31062 TOULOUSE FRANCE LAB BIOL MOLEC EUCARYOTE,CNRS,UPR 9006 F-31062 TOULOUSE FRANCE
Titolo Testata:
European journal of cell biology
fascicolo: 1, volume: 66, anno: 1995,
pagine: 47 - 59
SICI:
0171-9335(1995)66:1<47:BFG(IT>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR PRODUCTION; EXTRACELLULAR-MATRIX; ENDOTHELIAL-CELLS; GLYCOSYL-PHOSPHATIDYLINOSITOL; VASCULAR ENDOTHELIUM; A431 CELLS; RECEPTOR; BINDING; ENDOCYTOSIS; RELEASE;
Keywords:
BASIC FIBROBLAST GROWTH FACTOR; HEPARAN SULFATE PROTEOGLYCANS; ENDOCYTOSIS; ELECTRON MICROSCOPY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
63
Recensione:
Indirizzi per estratti:
Citazione:
P.E. Gleizes et al., "BASIC FIBROBLAST GROWTH-FACTOR (FGF-2) INTERNALIZATION THROUGH THE HEPARAN-SULFATE PROTEOGLYCANS-MEDIATED PATHWAY - AN ULTRASTRUCTURAL APPROACH", European journal of cell biology, 66(1), 1995, pp. 47-59

Abstract

Biochemical studies have shown that basic fibroblast growth factor (bFGF or FGF-2) is internalized by two pathways, after binding to eitherFGF tyrosine kinase receptors or to heparan sulfate proteoglycans (HSPG). To get insights on the HSPG-mediated pathway, we have examined byelectron microscopy the intracellular route of bFGF-HRP, a monovalentconjugate of bFGF and horseradish peroxidase which was found to bind to HSPG only and was detectable by electron microscopy. bFGF-HRP association to adult bovine aortic endothelial (ABAE) cells or baby hamsterkidney (BHK) cells was inhibited by a high molar excess of native bFGF, a 2 M NaCl wash at neutral pH, heparin and heparan sulfate, but notby chondroitin 4-sulfate or chondroitin 6-sulfate. bFGF-HRP was not able to displace [I-125]bFGF from its high-affinity binding sites, and the dissociation constant of its binding to ABAE cells was estimated at 3 nM. Timecourse experiments were performed to follow bFGF-HRP endocytosis in ABAE cells. bFGF-HRP was found to enter the cell after binding to the plasma membrane or extracellular matrix. On the cell surface, the probe accumulated in noncoated flask-shaped invaginations and incaveolae rather than in clathrin-coated pits. Immediately after endocytosis, bFGF-HRP was detected in pleiomorphic tubulovesicular and tubulovesicular early endosomes. Multivesicular bodies contained diaminobenzidine (DAB) precipitate after 5 to 15 min, but lysosomes were not labeled before 1 h, indicating a delayed transfer from late endosomes tolysosomes. Labeling was never detected in the nucleus, even after intensification of the DAB reaction product by silver-gold enhancement. Similar endocytic pathways and intracellular locations were observed inother endothelial and non-endothelial cell types. These results suggest that bFGF associated to HSPG can enter the cell via several pathways and follows mainly a degradative route.

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Documento generato il 05/12/20 alle ore 19:48:58