title: Laminin inhibits amyloid-beta-peptide fibrillation.
abstract: Laminin, an important extracellular matrix component is induced by brain injury and colocalizes with amyloid-beta-peptide (A beta) deposits in Alzheimer brains. We report here that laminin inhibits amyloid fibril formation as determined by thioflavin T fluorescence spectroscopy and electron microscopic examination. The inhibition of amyloid formation by laminin was concentration dependent and was observed at a laminin concentration of 300 nM, corresponding to a laminin/A beta protein molar ratio of 1:800. The potential effect of laminin, may prove important to inhibit A beta fibrillogenesis in vivo, specifically at the level of cerebral blood vessels.
authors.affiliation: Departamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago, Chile.
authors.forename: F C
authors.initials: FC
authors.lastname: Bronfman
authors.forename: J
authors.initials: J
authors.lastname: Garrido
authors.forename: A
authors.initials: A
authors.lastname: Alvarez
authors.forename: C
authors.initials: C
authors.lastname: Morgan
authors.forename: N C
authors.initials: NC
authors.lastname: Inestrosa
mesh_terms: D016229:Amyloid beta-Peptides / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D007797:Laminin / Q000494:pharmacology*; D008854:Microscopy, Electron; D016874:Neurofibrillary Tangles / Q000737:chemistry
chemical_list: D016229:Amyloid beta-Peptides; D007797:Laminin