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and the Department of Biomedical Sciences and Biotechnology, School of Medicine, University of Brescia, Italy." } ], "person_or_org": { "family_name": "Giavazzi", "given_name": "Raffaella", "name": "Giavazzi, Raffaella", "type": "personal" } }, { "affiliations": [ { "name": "From the Tumor Angiogenesis Unit, Department of Oncology, Mario Negri Institute for Pharmacological Research, Bergamo, Italy; and the Department of Biomedical Sciences and Biotechnology, School of Medicine, University of Brescia, Italy." } ], "person_or_org": { "family_name": "Rusnati", "given_name": "Marco", "name": "Rusnati, Marco", "type": "personal" } }, { "affiliations": [ { "name": "From the Tumor Angiogenesis Unit, Department of Oncology, Mario Negri Institute for Pharmacological Research, Bergamo, Italy; and the Department of Biomedical Sciences and Biotechnology, School of Medicine, University of Brescia, Italy." } ], "person_or_org": { "family_name": "Presta", "given_name": "Marco", "name": "Presta, Marco", "type": "personal" } }, { "affiliations": [ { "name": "From the Tumor Angiogenesis Unit, Department of Oncology, Mario Negri Institute for Pharmacological Research, Bergamo, Italy; and the Department of Biomedical Sciences and Biotechnology, School of Medicine, University of Brescia, Italy." } ], "person_or_org": { "family_name": "Taraboletti", "given_name": "Giulia", "name": "Taraboletti, Giulia", "type": "personal" } } ], "description": "AbstractThe antiangiogenic factor thrombospondin 1 (TSP-1) binds with high affinity to several heparin-binding angiogenic factors, including fibroblast growth factor 2 (FGF-2), vascular endothelial growth factor (VEGF), and hepatocyte growth factor/scatter factor (HGF/SF). The aim of this study was to investigate whether TSP-1 affects FGF-2 association with the extracellular matrix (ECM) and its bioavailability. TSP-1 prevented the binding of free FGF-2 to endothelial cell ECM. It also promoted the mobilization of matrix-bound FGF-2, generating a TSP-1/FGF-2 complex. The region of TSP-1 responsible for these activities was located within the 140-kDa antiangiogenic and FGF-2 binding fragment, whereas the 25-kDa heparin-binding fragment was inactive. Matrix-released FGF-2/TSP-1 complex had a reduced ability to bind to and induce proliferation of endothelial cells. TSP-1 depleted the ECM laid by FGF-2-overproducing tumor cells of its FGF-2-dependent mitogenic activity for endothelial cells. Besides FGF-2, TSP-1 also inhibited VEGF and HGF/SF binding to the ECM and mobilized them from the ECM. Our study shows that TSP-1 acts as a scavenger for matrix-associated angiogenic factors, affecting their location, bioavailability, and function. 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