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Cold Spring Harb Perspect Med. 2018 May 1;8(5). pii: a023507. doi: 10.1101/cshperspect.a023507.

β-Amyloid Prions and the Pathobiology of Alzheimer's Disease.

Author information

1
Tanz Centre for Research in Neurodegenerative Diseases and Department of Biochemistry, University of Toronto, Toronto, Ontario M5T 2S8, Canada.
2
Institute for Neurodegenerative Diseases, Departments of Neurology and of Biochemistry and Biophysics, Weill Institute for Neurosciences, University of California, San Francisco, San Francisco, California 94143.

Abstract

Alzheimer's disease (AD) is the most common neurodegenerative disease in humans and will pose a considerable challenge to healthcare systems in the coming years. Aggregation of the β-amyloid (Aβ) peptide within the brain is thought to be an initiating event in AD pathogenesis. Many recent studies in transgenic mice have provided evidence that Aβ aggregates become self-propagating during disease, leading to a cascade of protein aggregation in the brain, which may underlie the progressive nature of AD. The ability to self-propagate and the existence of distinct "strains" reveals that Aβ aggregates exhibit many properties indistinguishable from those of prions composed of PrPSc proteins. Here, we review the evidence that Aβ can become a prion during disease and discuss how Aβ prions may be important for understanding the pathobiology of AD.

PMID:
28193770
PMCID:
PMC5554751
[Available on 2019-05-01]
DOI:
10.1101/cshperspect.a023507
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