Source:http://linkedlifedata.com/resource/pubmed/id/10956668
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
47
|
| pubmed:dateCreated |
2001-1-8
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| pubmed:abstractText |
Full-length and truncated forms of rat thrombospondin-4 (TSP-4) were expressed recombinantly in a mammalian cell line and purified to homogeneity. Biochemical analysis revealed a limited proteolytic processing, which detaches the N-terminal heparin-binding domain from the rest of the molecule and confirmed the importance of the heptad-repeat domain for pentamerization. In electron microscopy the uncleaved TSP-4 was seen as a large central particle to which five smaller globules are attached by elongated linker regions. Binding of TSP-4 to collagens and to non-collagenous proteins could be detected in enzyme-linked immunosorbent assay-style ligand binding assays, by surface plasmon resonance spectroscopy, and in rotary shadowing electron microscopy. Although the binding of TSP-4 to solid-phase collagens was enhanced by Zn(2+), that to non-collagenous proteins was not. The interactions of TSP-4 with both classes of proteins are mediated by C-terminal domains of the TSP-4 subunits but do not require an oligomeric structure. Major binding sites for TSP-4 are located in or close to the N- and C-terminal telopeptides in collagen I, but additional sites are detected in more central regions of the molecule.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombospondins,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc,
http://linkedlifedata.com/resource/pubmed/chemical/thrombospondin 4
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
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| pubmed:volume |
275
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
37110-7
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10956668-Amino Acid Sequence,
pubmed-meshheading:10956668-Animals,
pubmed-meshheading:10956668-Biosensing Techniques,
pubmed-meshheading:10956668-Cell Adhesion Molecules,
pubmed-meshheading:10956668-Cell Line,
pubmed-meshheading:10956668-Cloning, Molecular,
pubmed-meshheading:10956668-Collagen,
pubmed-meshheading:10956668-DNA, Complementary,
pubmed-meshheading:10956668-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10956668-Extracellular Matrix Proteins,
pubmed-meshheading:10956668-Humans,
pubmed-meshheading:10956668-Microscopy, Electron,
pubmed-meshheading:10956668-Molecular Sequence Data,
pubmed-meshheading:10956668-Rats,
pubmed-meshheading:10956668-Skin,
pubmed-meshheading:10956668-Structure-Activity Relationship,
pubmed-meshheading:10956668-Thrombospondins,
pubmed-meshheading:10956668-Zinc
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| pubmed:year |
2000
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| pubmed:articleTitle |
Thrombospondin-4 binds specifically to both collagenous and non-collagenous extracellular matrix proteins via its C-terminal domains.
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| pubmed:affiliation |
Institute for Biochemistry, Medical Faculty, University of Cologne, Joseph-Stelzmann-Strasse 52, Cologne D-50931, Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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