Fibrillin-1 interactions with heparin. Implications for microfibril and elastic fiber assembly.

作者: Stuart A. Cain , Clair Baldock , John Gallagher , Amanda Morgan , Daniel V. Bax

DOI: 10.1074/JBC.M501390200

关键词:

摘要: Fibrillin-1 assembly into microfibrils and elastic fiber formation involves interactions with glycosaminoglycans. We have used BIAcore technology to investigate fibrillin-1 heparin saccharides that are analogous S-domains of heparan sulfate. identified four high affinity heparin-binding sites on fibrillin-1, localized three these sites, defined their binding kinetics. Heparin the N terminus has particularly rapid Hyaluronan chondroitin sulfate did not interact significantly fibrillin-1. more than 12 monosaccharide units bound strongly all sites. inhibit N- C-terminal or RGD-dependent cell attachment, but MAGP-1 competed for terminus, tropoelastin a central sequence. By regulating key interactions, can profoundly influence microfibril assembly.

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