Source:http://linkedlifedata.com/resource/pubmed/id/18669635
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
40
|
| pubmed:dateCreated |
2008-9-29
|
| pubmed:abstractText |
Fibrillin-1 N- and C-terminal heparin binding sites have been characterized. An unprocessed monomeric N-terminal fragment (PF1) induced a very high heparin binding response, indicating heparin-mediated multimerization. Using PF1 deletion and short fragments, a heparin binding site was localized within the domain encoded by exon 7 after the first hybrid domain. Rodent embryonic fibroblasts adhered to PF1 and deletion fragments, and, when cells were plated on fibrillin-1 or fibronectin Arg-Gly-Asp cell-binding fragments, cells showed heparin-dependent spreading and focal contact formation in response to soluble PF1. Within domains encoded by exons 59-62 near the fibrillin-1 C terminus are novel conformation-dependent high affinity heparin and tropoelastin binding sites. Heparin disrupted tropoelastin binding but did not disrupt N- and C-terminal fibrillin-1 interactions. Thus, fibrillin-1 N-terminal interactions with heparin/heparan sulfate directly influence cell behavior, whereas C-terminal interactions with heparin/heparan sulfate regulate elastin deposition. These data highlight how heparin/heparan sulfate controls fibrillin-1 interactions.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Heparitin Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tropoelastin,
http://linkedlifedata.com/resource/pubmed/chemical/fibrillin
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
3
|
| pubmed:volume |
283
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
27017-27
|
| pubmed:meshHeading |
pubmed-meshheading:18669635-Amino Acid Sequence,
pubmed-meshheading:18669635-Animals,
pubmed-meshheading:18669635-Binding Sites,
pubmed-meshheading:18669635-CHO Cells,
pubmed-meshheading:18669635-Cricetinae,
pubmed-meshheading:18669635-Cricetulus,
pubmed-meshheading:18669635-Embryo, Mammalian,
pubmed-meshheading:18669635-Exons,
pubmed-meshheading:18669635-Fibroblasts,
pubmed-meshheading:18669635-Heparin,
pubmed-meshheading:18669635-Heparitin Sulfate,
pubmed-meshheading:18669635-Humans,
pubmed-meshheading:18669635-Mice,
pubmed-meshheading:18669635-Microfilament Proteins,
pubmed-meshheading:18669635-Peptide Mapping,
pubmed-meshheading:18669635-Protein Binding,
pubmed-meshheading:18669635-Protein Structure, Tertiary,
pubmed-meshheading:18669635-Rats,
pubmed-meshheading:18669635-Sequence Deletion,
pubmed-meshheading:18669635-Tropoelastin
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| pubmed:year |
2008
|
| pubmed:articleTitle |
Heparan sulfate regulates fibrillin-1 N- and C-terminal interactions.
|
| pubmed:affiliation |
Wellcome Trust Centre for Cell Matrix Research, Faculty of Life Sciences, University of Manchester, United Kingdom.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|