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Common binding sites for beta-amyloid fibrils and fibroblast growth factor-2 in heparan sulfate from human cerebral cortex

AutorLindahl, Birgitta; Westling, Camilla; Giménez-Gallego, Guillermo ; Lindahl, Ulf; Salmivirta, Markku
Palabras claveAlzheimers-disease
A-beta
Basic fgf
Peptides
Proteoglycans
Aggregation
Inhibition
Perlecan
Plaques
Amylin
Fecha de publicación22-oct-1999
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJ Biol Chem 274(43):30631-5 (1999)
ResumenHeparan sulfate found in the cerebral plaques of Alzheimer's disease binds to beta-amyloid (Abeta) fibrils. This interaction has been proposed to enhance fibril deposition and mediate Abeta-induced glia activation and neurotoxicity. On the other hand, heparan sulfate augments signaling of fibroblast growth factor-2 (FGF-2), a neuroprotective factor that antagonizes the neurotoxic effects of Abeta. We defined structures in heparan sulfate from human cerebral cortex that bind Abeta fibrils. The minimal binding site is found in N-sulfated hexasaccharide domains and contains critical 2-O-sulfated iduronic acid residues. By contrast, binding of Abeta monomers requires, in addition, 6-O-sulfate groups on glucosamine residues. The binding specificity of fibrillar Abeta is shared by FGF-2, and we here show that cerebral heparan sulfate domains selected for binding to Abeta-(1-40) fibrils bind also to FGF-2. These data suggest that neurotoxic and neuroprotective signals may converge by competing for the same binding sites on the heparan sulfate chain.
Descripción6 p.-4 fig.-1 tab.
Versión del editorhttps://doi.org/10.1074/jbc.274.43.30631
URIhttp://hdl.handle.net/10261/169530
DOI10.1074/jbc.274.43.30631
ISSN0021-9258
E-ISSN1083-351X
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