Meyer-Luehmann, MelanieCoomaraswamy, JanakyBolmont, TristanKaeser, StephanSchaefer, ClaudiaKilger, EllenNeuenschwander, AntonAbramowski, DorotheeFrey, PeterJaton, Anneliese L.Vigouret, Jean-MariePaganetti, PaoloWalsh, Dominic M.Mathews, Paul M.Ghiso, JorgeStaufenbiel, MatthiasWalker, Lary C.Jucker, Mathias2010-03-162010-03-162010-03-16200610.1126/science.1131864https://infoscience.epfl.ch/handle/20.500.14299/48156Protein aggregation is an established pathogenic mechanism in Alzheimer's disease, but little is known about the initiation of this process in vivo. Intracerebral injection of dilute, amyloid-beta (A beta)-containing brain extracts from humans with Alzheimer's disease or beta-amyloid precursor protein (APP) transgenic mice induced cerebral beta-amyloidosis and associated pathology in APP transgenic mice in a time- and concentration-dependent manner. The seeding activity of brain extracts was reduced or abolished by A beta immunodepletion, protein denaturation, or by A beta immunization of the host. The phenotype of the exogenously induced amyloidosis depended on both the host and the source of the agent, suggesting the existence of polymorphic A beta strains with varying biological activities reminiscent of prion strains.Disease-Like PathologyAlzheimers-DiseaseTransgenic MiceLong-TermIn-VivoProteinDepositionOligomersMouseConformationtext::journal::journal article::research article