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rdf:type |
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lifeskim:mentions |
umls-concept:C0010435,
umls-concept:C0016055,
umls-concept:C0331858,
umls-concept:C0442805,
umls-concept:C1145667,
umls-concept:C1420801,
umls-concept:C1514562,
umls-concept:C1704640,
umls-concept:C1706515,
umls-concept:C1706853,
umls-concept:C1879748,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
3
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pubmed:dateCreated |
2008-3-17
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pubmed:abstractText |
Human plasma fibronectin binds with high affinity to the inflammation-induced secreted protein TSG-6. Fibronectin binds to the CUB_C domain of TSG-6 but not to its Link module. TSG-6 can thus act as a bridging molecule to facilitate fibronectin association with the TSG-6 Link module ligand thrombospondin-1. Fibronectin binding to TSG-6 is divalent cation-independent and is conserved in cellular fibronectins. Based on competition binding studies using recombinant and proteolytic fragments of fibronectin, TSG-6 binding localizes to type III repeats 9-14 of fibronectin. This region of fibronectin contains the Arg-Gly-Asp sequence recognized by alpha5beta1 integrin, but deletion of that sequence does not prevent TSG-6 binding, and TSG-6 does not inhibit cell adhesion on fibronectin substrates mediated by this integrin. This region of fibronectin is also involved in fibronectin matrix assembly, and addition of TSG-6 enhances exogenous and endogenous fibronectin matrix assembly by human fibroblasts. Therefore, TSG-6 is a high affinity ligand that can mediate fibronectin interactions with other matrix components and modulate some interactions of fibronectin with cells.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-10490955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-10508649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-10727214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-11358957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-11854277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-11980922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-12668637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-12692188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-12959984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-1527055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-15457471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-15615773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-15718240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-15840581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-16006654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-16061370,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-16709183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-17046999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-1730767,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-1755828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-2071570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-3920218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-6254391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-8071326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-8424687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-8510165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-8739346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-8812829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-9126602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18042364-9708918
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0945-053X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
201-10
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18042364-Cations,
pubmed-meshheading:18042364-Cell Adhesion Molecules,
pubmed-meshheading:18042364-Dose-Response Relationship, Drug,
pubmed-meshheading:18042364-Extracellular Matrix,
pubmed-meshheading:18042364-Fibroblasts,
pubmed-meshheading:18042364-Fibronectins,
pubmed-meshheading:18042364-Gene Deletion,
pubmed-meshheading:18042364-Humans,
pubmed-meshheading:18042364-Integrin alpha5beta1,
pubmed-meshheading:18042364-Kinetics,
pubmed-meshheading:18042364-Ligands,
pubmed-meshheading:18042364-Models, Biological,
pubmed-meshheading:18042364-Protein Structure, Tertiary,
pubmed-meshheading:18042364-Recombinant Proteins,
pubmed-meshheading:18042364-Thrombospondin 1
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pubmed:year |
2008
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pubmed:articleTitle |
TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly.
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pubmed:affiliation |
Laboratory of Pathology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, United States.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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