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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Publication : The Journal of biological chemistry

Heparan sulfate regulates fibrillin-1 N- and C-terminal interactions

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 31 Jul 2008

Cain SA, Baldwin AK, Mahalingam Y, Raynal B, Jowitt TA, Shuttleworth CA, Couchman JR, Kielty CM

Link to Pubmed [PMID] – 18669635

J. Biol. Chem. 2008 Oct;283(40):27017-27

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.

https://www.ncbi.nlm.nih.gov/pubmed/18669635