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Alzheimer disease: a tale of two prions

Justin M Nussbaum1, Matthew E Seward, George S Bloom

  • 1Department of Biology, University of Virginia, Charlottesville, VA, USA.

Prion
|September 12, 2012
PubMed

Insights

Alzheimer disease pathogenesis may involve prion-like mechanisms where amyloid-beta (Aβ) and tau proteins misfold and spread. Misfolded Aβ might directly trigger tau misfolding, challenging traditional views of Alzheimer disease progression.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Alzheimer disease (AD) pathogenesis traditionally involves separate amyloid-beta (Aβ) and tau protein aggregation.
  • Recent findings reveal functional interactions between Aβ and tau in AD pathology.
  • The spread of misfolded Aβ and tau resembles prion protein (PrP) propagation.

Purpose of the Study:

  • To review evidence for prion-like properties of Aβ and tau in Alzheimer disease.
  • To explore the hypothesis that misfolded Aβ induces tau misfolding in vivo.

Main Methods:

  • Literature review of studies on Aβ and tau aggregation and propagation.
  • Analysis of in vitro and in vivo evidence for Aβ-tau interactions.
  • Comparison of Aβ and tau misfolding with prion protein pathogenesis.

Main Results:

  • Evidence supports prion-like characteristics for both Aβ and tau individually.
  • Misfolded Aβ has demonstrated the ability to induce tau misfolding in vitro.
  • Functional interactions between Aβ and tau are increasingly recognized in AD.

Conclusions:

  • The traditional parallel model of AD pathogenesis is challenged by Aβ-tau interactions.
  • Aβ and tau may propagate in a prion-like manner.
  • Misfolded Aβ may act as a template to initiate tau misfolding in Alzheimer disease.
Keywords:
Alzheimer diseaseamyloid plaqueamyloid-βneurodegenerationneurofibrillary tanglepriontau

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