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http://purl.uniprot.org/citations/11509569http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11509569http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11509569http://www.w3.org/2000/01/rdf-schema#comment"Fibroblast growth factor-binding protein (FGF-BP) 1 is a secreted protein that can bind fibroblast growth factors (FGFs) 1 and 2. These FGFs are typically stored on heparan sulfate proteoglycans in the extracellular matrix in an inactive form, and it has been proposed that FGF-BP1 functions as a chaperone molecule that can mobilize locally stored FGF and present the growth factor to its tyrosine kinase receptor. FGF-BP1 is up-regulated in squamous cell, colon, and breast cancers and can act as an angiogenic switch during malignant progression of epithelial cells. For the present studies, we focused on FGF-1 and -2 and investigated interactions with recombinant human FGF-BP1 protein as well as effects on signal transduction, cell proliferation, and angiogenesis. We show that recombinant FGF-BP1 specifically binds FGF-2 and that this binding is inhibited by FGF-1, heparan sulfate, and heparinoids. Furthermore, FGF-BP1 enhances FGF-1- and FGF-2-dependent proliferation of NIH-3T3 fibroblasts and FGF-2-induced extracellular signal-regulated kinase 2 phosphorylation. Finally, in the chicken chorioallantoic membrane angiogenesis assay, FGF-BP1 synergizes with exogenously added FGF-2. We conclude that FGF-BP1 binds directly to FGF-1 and FGF-2 and positively modulates the biological activities of these growth factors."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m104933200"xsd:string
http://purl.uniprot.org/citations/11509569http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m104933200"xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Tassi E."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Tassi E."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"McDonnell K."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"McDonnell K."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Aigner A."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Aigner A."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Karavanov A."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Karavanov A."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Wellstein A."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Wellstein A."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Al-Attar A."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Al-Attar A."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Swift M.R."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/author"Swift M.R."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/pages"40247-40253"xsd:string
http://purl.uniprot.org/citations/11509569http://purl.uniprot.org/core/pages"40247-40253"xsd:string