Journal
ACTA NEUROPATHOLOGICA
Volume 142, Issue 1, Pages 17-39Publisher
SPRINGER
DOI: 10.1007/s00401-020-02201-2
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Funding
- Swedish Research Institute
- Wenner-Gren Foundations
- Canadian Institutes of Health Research
- Alzheimer Society Canada
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Alzheimer's disease shares considerable clinical and pathological variability with human prion diseases. A beta peptide can assemble into a spectrum of aggregate strains similar to prion protein, exhibiting key hallmarks of prion strains and potentially driving phenotypic heterogeneity in Alzheimer's disease.
Reminiscent of the human prion diseases, there is considerable clinical and pathological variability in Alzheimer's disease, the most common human neurodegenerative condition. As in prion disorders, protein misfolding and aggregation is a hallmark feature of Alzheimer's disease, where the initiating event is thought to be the self-assembly of A beta peptide into aggregates that deposit in the central nervous system. Emerging evidence suggests that A beta, similar to the prion protein, can polymerize into a conformationally diverse spectrum of aggregate strains both in vitro and within the brain. Moreover, certain types of A beta aggregates exhibit key hallmarks of prion strains including divergent biochemical attributes and the ability to induce distinct pathological phenotypes when intracerebrally injected into mouse models. In this review, we discuss the evidence demonstrating that A beta can assemble into distinct strains of aggregates and how such strains may be primary drivers of the phenotypic heterogeneity in Alzheimer's disease.
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