| http://purl.uniprot.org/citations/17879962 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17879962 | http://www.w3.org/2000/01/rdf-schema#comment | "Thrombospondin-1 (TSP-1) is an extracellular matrix protein that modulates focal adhesion in mammalian cells and exhibits dual roles in angiogenesis. In a previous work, we showed that a recombinant 18 kDa protein encompassing the N-terminal residues 1-174 of human TSP-1 (TSP18) induced tubulogenesis of human umbilical vein endothelial cells and protected them from apoptosis. Our results indicated that these effects were possibly mediated by syndecan-4 proteoglycan, since binding of TSP18 to endothelial extracts was inhibited by anti-syndecan-4 antibody. Syndecan-4 is a heparan-sulfate proteoglycan that regulates cell-matrix interactions and is the only member of its family present in focal adhesions. In this report, we demonstrate that a monoclonal antibody against syndecan-4 blocks TSP18-induced tubulogenesis. Furthermore, through 2D adhesion and 3D angiogenic assays, we demonstrate that two sequences, TSP Hep I and II, retain the major pro-angiogenic activity of TSP18. These TSP-1 motifs also compete with the fibronectin Hep II domain for binding to syndecan-4 on endothelial cell surface, indicating that they may exert their effects by interfering with the recognition of fibronectin by syndecan-4. Additionally, TSP18 and its derived peptides activate the PKC-dependent Akt-PKB signaling pathway. Blockage of PKC activation prevented HUVEC spreading when seeded on TSP18 fragment, and on TSP Hep I and TSP Hep II peptides, but not on gelatin-coated substrates. Our results identify syndecan-4 as a novel receptor for the N-terminus of TSP-1 and suggest that TSP-1 N-terminal pro-angiogenic activity is linked to its capacity of interfering with syndecan-4 functions in the course of cell adhesion."xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.org/dc/terms/identifier | "doi:10.1002/jcp.21281"xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/author | "Juliano L."xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/author | "Nader H.B."xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/author | "Woods A."xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/author | "Legrand C."xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/author | "Morandi V."xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/author | "Nunes S.S."xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/author | "Outeiro-Bernstein M.A."xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/author | "Vardiero F."xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/name | "J Cell Physiol"xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/pages | "828-837"xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/title | "Syndecan-4 contributes to endothelial tubulogenesis through interactions with two motifs inside the pro-angiogenic N-terminal domain of thrombospondin-1."xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://purl.uniprot.org/core/volume | "214"xsd:string |
| http://purl.uniprot.org/citations/17879962 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17879962 |
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