Protein 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-ß (Aß)–containing brain extracts from humans with Alzheimer's disease or ß-amyloid precursor protein (APP) transgenic mice induced cerebral ß-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 Aß immunodepletion, protein denaturation, or by Aß 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 Aß strains with varying biological activities reminiscent of prion strains.
Source:
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host. Melanie Meyer-Luehmann et al. Science 22 September 2006: Vol. 313. no. 5794, pp. 1781 - 178
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Exogenous Induction of Alzheimers disease
September 26, 2006Postado por Admin às 5:43 AM
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