One or more β-amyloid(s)? New insights into the prion-like nature of Alzheimer's disease

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Misfolding and aggregation of proteins play a central role in the pathogenesis of several neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's and Lewy Body diseases, Frontotemporal Lobar Degeneration and prion diseases. Increasing evidence supports the view that Aβ and tau, which are the two main molecular players in AD, share with the prion protein several “prion-like” features that can be relevant for disease pathogenesis. These features essentially include structural/conformational/biochemical variations, resistance to degradation by endogenous proteases, seeding ability, attitude to form neurotoxic assemblies, spreading and propagation of toxic aggregates, transmissibility of tau- and Aβ-related pathology to animal models. Following this view, part of the recent scientific literature has generated a new reading frame for AD pathophysiology, based on the application of the prion paradigm to the amyloid cascade hypothesis in an attempt to definitely explain the key events causing the disease and inducing its occurrence under different clinical phenotypes.

Original languageEnglish
Title of host publicationProgress in Molecular Biology and Translational Science
EditorsGiuseppe Legname
PublisherElsevier B.V.
Pages213-237
Number of pages25
ISBN (Print)9780128200025
DOIs
Publication statusPublished - 2020

Publication series

NameProgress in Molecular Biology and Translational Science
Volume175
ISSN (Print)1877-1173
ISSN (Electronic)1878-0814

Keywords

  • Alzheimer's disease
  • Amyloid
  • Misfolding
  • Oligomers
  • Phenotypes
  • Prion
  • Prion-like
  • PrP
  • Tau

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology

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