Fibrillin-1 interactions with heparin. Implications for microfibril and elastic fiber assembly.
Authors
Cain, Stuart ABaldock, Clair
Gallagher, John T
Morgan, Amanda
Bax, Daniel V
Weiss, Anthony S
Shuttleworth, C Adrian
Kielty, Cay M
Affiliation
Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom.Issue Date
2005-08-26
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Show full item recordAbstract
Fibrillin-1 assembly into microfibrils and elastic fiber formation involves interactions with glycosaminoglycans. We have used BIAcore technology to investigate fibrillin-1 interactions with heparin and with heparin saccharides that are analogous to S-domains of heparan sulfate. We have identified four high affinity heparin-binding sites on fibrillin-1, localized three of these sites, and defined their binding kinetics. Heparin binding to the fibrillin-1 N terminus has particularly rapid kinetics. Hyaluronan and chondroitin sulfate did not interact significantly with fibrillin-1. Heparin saccharides with more than 12 monosaccharide units bound strongly to all four fibrillin-1 sites. Heparin did not inhibit fibrillin-1 N- and C-terminal interactions or RGD-dependent cell attachment, but heparin and MAGP-1 competed for binding to the fibrillin-1 N terminus, and heparin and tropoelastin competed for binding to a central fibrillin-1 sequence. By regulating these key interactions, heparin can profoundly influence microfibril and elastic fiber assembly.Citation
Fibrillin-1 interactions with heparin. Implications for microfibril and elastic fiber assembly. 2005, 280 (34):30526-37 J. Biol. Chem.Journal
The Journal of Biological ChemistryDOI
10.1074/jbc.M501390200PubMed ID
15980072Type
ArticleLanguage
enISSN
0021-9258ae974a485f413a2113503eed53cd6c53
10.1074/jbc.M501390200
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