Laminin inhibits amyloid-beta-peptide fibrillation.
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.
Bronfman
F C
FC
Departamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago, Chile.
Garrido
J
J
Alvarez
A
A
Morgan
C
C
Inestrosa
N C
NC
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
D016229:Amyloid beta-Peptides; D007797:Laminin