@article{811d62e0a1a711dd95e9000ea68e967b,
title = "Heparan sulfate regulates fibrillin-1 N- and C-terminal interactions.",
abstract = "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.",
author = "Cain, {Stuart A} and Baldwin, {Andrew K} and Yashithra Mahalingam and Bertrand Raynal and Jowitt, {Thomas A} and Shuttleworth, {C Adrian} and Couchman, {John R} and Kielty, {Cay M}",
year = "2008",
doi = "10.1074/jbc.M803373200",
language = "English",
volume = "283",
pages = "27017--27",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "40",
}