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JBC News Podcast: Prion-mediated toxicity of Aβ oligomers: JBC’s best Neurobiology article of 2013

Conversation between Associate Editor Paul Fraser and corresponding author Nigel Hooper



JBC Best of 2013 logoFeb. 24, 2014 — In this, the second in our four-part podcast series on the best articles of 2013 in The Journal of Biological Chemistry, we hear a conversation between Associate Editor Paul Fraser, a professor in the Department of Medical Biophysics at the University of Toronto, and Nigel Hooper from the Faculty of Biological Sciences at the University of Leeds in the United Kingdom. Dr. Hooper is the author of JBC’s Best Article of 2013 in the category of Neurobiology. It is titled, Prion Protein-mediated Toxicity of Amyloid-β Oligomers Requires Lipid Rafts and the Transmembrane LRP1, and it was published in March. The paper focuses attention on how remodeling amyloid-β oligomers and disrupting the prion LRP1 raft interaction can provide therapeutic targets for Alzheimer disease. Drs. Fraser and Hooper talk about the progression of this work and where the research may lead.

ARTICLE CAPSULE


Prion Protein-mediated Toxicity of Amyloid-β Oligomers Requires Lipid Rafts and the Transmembrane LRP1

Background: Prion protein (PrPC) is a receptor for amyloid-β oligomers (AβOs).

Results: AβO binding to PrPC and cytotoxicity require transmembrane LRP1 and are reduced by cholesterol depletion and AβO remodeling.

Conclusion: Cellular binding and toxicity of AβOs are dependent on PrPC being localized in a raft-based complex.

Significance: Remodeling AβOs and disrupting the prion-LRP1-raft interaction provide therapeutic targets for Alzheimer disease.


Click here to read a transcript of this podcast interview.