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Titolo:
HEPARAN-SULFATE PROTEOGLYCANS AS TRANSDUCERS OF FGF-2 SIGNALING
Autore:
QUARTO N; AMALRIC F;
Indirizzi:
CNRS,BIOL MOLEC EUCARYOTE LAB,118 ROUTE NARBONNE F-31062 TOULOUSE FRANCE CNRS,BIOL MOLEC EUCARYOTE LAB F-31062 TOULOUSE FRANCE
Titolo Testata:
Journal of Cell Science
, volume: 107, anno: 1994,
parte:, 11
pagine: 3201 - 3212
SICI:
0021-9533(1994)107:<3201:HPATOF>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
FIBROBLAST GROWTH-FACTOR; SUBENDOTHELIAL EXTRACELLULAR-MATRIX; PLASMINOGEN-ACTIVATOR PRODUCTION; TYROSINE KINASE-ACTIVITY; FACTOR RECEPTOR; ANGIOGENIC PROTEIN; CELL-SURFACE; PROTEOLYTIC DEGRADATION; NUCLEOTIDE-SEQUENCE; LIPOPROTEIN-LIPASE;
Keywords:
HEPARAN SULFATE PROTEOGLYCANS; INTERNALIZATION; FGF-SIGNALING; UROKINASE-PLASMINOGEN ACTIVATOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
78
Recensione:
Indirizzi per estratti:
Citazione:
N. Quarto e F. Amalric, "HEPARAN-SULFATE PROTEOGLYCANS AS TRANSDUCERS OF FGF-2 SIGNALING", Journal of Cell Science, 107, 1994, pp. 3201-3212

Abstract

The fibroblast growth factor-2 (FGF-2) low-affinity binding sites, heparan sulfate proteoglycans (HSPGs), function as modulators of FGF-2 activity. It is noteworthy that HSPG binding protects FGF-2 from denaturation and proteolytic degradation, provides a matrix-bound or cell-surface reservoir of this factor for the cells and is required for the activation of FGF high-affinity receptors. In our study we investigatedthe biological meaning of FGF-2 internalization mediated through its low-affinity binding sites, HSPGs. Using as model system L6 myoblasts lacking endogenous FGF receptors (FGFRs), we demonstrated that these cells internalize FGF-2 efficiently through an HSPG-mediated pathway. FGF-2 internalization occurring through HSPGs was paralleled by an increase in the activity of urokinase plasminogen activator (u-PA). The u-PA-inducing activity of FGF-2 was strictly correlated to its internalization, as chlorate treatment, which causes a strong inhibition of FGF-2 internalization, abrogated the u-PA-inducing activity of FGF-2. In addition, expression of functional FGF high-affinity receptors (FGFR-1) did not enhance u-PA in L6 myoblasts upon FGF-2 stimulation. According to our results we propose that FGF-2 internalization mediated through HSPGs may transduce FGF-2 signalling such as u-PA-activity stimulation. Thus, HSPGs may act as direct transducers of FGF signalling and indeed, different FGF-signalling pathways must exist.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 14:41:14