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Updated: Feb 15, 2026

Assaying β-amyloid Toxicity using a Transgenic C. elegans Model
Published on: October 9, 2010
Prion Protein as a Toxic Acceptor of Amyloid-β Oligomers
Silvia A Purro1, Andrew J Nicoll2, John Collinge1
1Medical Research Council Prion Unit, Institute of Prion Diseases, University College London (UCL), London, United Kingdom.
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.
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