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http://purl.uniprot.org/citations/17158881http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17158881http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17158881http://www.w3.org/2000/01/rdf-schema#comment"Human fibrillin-1, the major structural protein of connective tissue 10-12 nm microfibrils, contains multiple calcium binding epidermal growth factor-like domains interspersed with transforming growth factor beta-binding protein-like (TB) domains. TB4 contains a flexible RGD loop that mediates cell adhesion via alphaVbeta3 and alpha5beta1 integrins. This study identifies integrin alphaVbeta6 as a novel cellular receptor for fibrillin-1 with a K(d) of approximately 0.45 mum. Analyses of this interaction by surface plasmon resonance and immunocytochemistry reveal different module requirements for alphaVbeta6 activation compared with those of alphaVbeta3, suggesting that a covalent linkage of an N-terminal calcium binding epidermal growth factor-like domain to TB4 can modulate alphaV integrin binding specificity. Furthermore, our data suggest alpha5beta1 is a low affinity fibrillin-1 receptor (K(d) > 1 mum), thus providing a molecular explanation for the different alpha5beta1 distribution patterns seen when human keratinocytes and fibroblasts are plated on recombinant fibrillin fragments versus those derived from the physiological ligand fibronectin. Non-focal contact distribution of alpha5beta1 suggests that its engagement by fibrillin-1 may elicit a lesser degree and/or different type of intracellular signaling compared with that seen with a high affinity ligand."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m607008200"xsd:string
http://purl.uniprot.org/citations/17158881http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m607008200"xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Abrescia N.G."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Abrescia N.G."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Stuart D.I."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Stuart D.I."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Takagi J."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Takagi J."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Handford P.A."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Handford P.A."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"van der Merwe P.A."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"van der Merwe P.A."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Choulier L."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Choulier L."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Jovanovic J."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Jovanovic J."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Mardon H.J."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/author"Mardon H.J."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17158881http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string