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Biol Psychiatry. 2018 Feb 15;83(4):358-368. doi: 10.1016/j.biopsych.2017.11.020. Epub 2017 Nov 21.

Prion Protein as a Toxic Acceptor of Amyloid-β Oligomers.

Author information

1
Medical Research Council Prion Unit, Institute of Prion Diseases, University College London (UCL), London, United Kingdom.
2
Medical Research Council Prion Unit, Institute of Prion Diseases, University College London (UCL), London, United Kingdom; Elkington and Fife LLP, Kent, United Kingdom. Electronic address: a.nicoll@ucl.ac.uk.
3
Medical Research Council Prion Unit, Institute of Prion Diseases, University College London (UCL), London, United Kingdom. Electronic address: jc@prion.ucl.ac.uk.

Abstract

The initial report that cellular prion protein (PrPC) mediates toxicity of amyloid-β species linked to Alzheimer's disease was initially treated with scepticism, but growing evidence supports this claim. That there is a high-affinity interaction is now clear, and its molecular basis is being unraveled, while recent studies have identified possible downstream toxic mechanisms. Determination of the clinical significance of such interactions between PrPC and disease-associated amyloid-β species will require experimental medicine studies in humans. Trials of compounds that inhibit PrP-dependent amyloid-β toxicity are commencing in humans, and although it is clear that only a fraction of Alzheimer's disease toxicity could be governed by PrPC, a partial, but still therapeutically useful, role in human disease may soon be testable.

KEYWORDS:

Alzheimer’s disease; Amyloid; Neurodegeneration; Oligomers; Prion; Therapeutics

PMID:
29331212
DOI:
10.1016/j.biopsych.2017.11.020
[Indexed for MEDLINE]

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