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Prion. 2017 Jul 4;11(4):215-225. doi: 10.1080/19336896.2017.1334029. Epub 2017 Jun 28.

Aβ seeds and prions: How close the fit?

Author information

1
a Department of Cellular Neurology , Hertie Institute for Clinical Brain Research, University of Tübingen , Tübingen , Germany.
2
b German Center for Neurodegenerative Diseases (DZNE) , Tübingen , Germany.
3
c Graduate Training Center of Neuroscience, University of Tübingen , Tübingen , Germany.
4
d Department of Neurology and Yerkes National Primate Research Center , Emory University , Atlanta , GA , USA.

Abstract

The prion paradigm is increasingly invoked to explain the molecular pathogenesis of neurodegenerative diseases involving the misfolding and aggregation of proteins other than the prion protein (PrP). Extensive evidence from in vitro and in vivo studies indicates that misfolded and aggregated Aβ peptide, which is the probable molecular trigger for Alzheimer's disease, manifests all of the key characteristics of canonical mammalian prions. These features include a β-sheet rich architecture, tendency to polymerize into amyloid, templated corruption of like protein molecules, ability to form structurally and functionally variant strains, systematic spread by neuronal transport, and resistance to inactivation by heat and formaldehyde. In addition to Aβ, a growing body of research supports the view that the prion-like molecular transformation of specific proteins drives the onset and course of a remarkable variety of clinicopathologically diverse diseases. As such, the expanded prion paradigm could conceptually unify fundamental and translational investigations of these disorders.

KEYWORDS:

Abeta; Alzheimer; aging; amyloid; dementia; neurodegeneration; prion; proteopathy; seeding; tau

PMID:
28657440
PMCID:
PMC5553305
DOI:
10.1080/19336896.2017.1334029
[Indexed for MEDLINE]
Free PMC Article

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