The prion protein or PrP is present in most of our cells. Although it is highly conserved between species, little is known about its role. In the neurons of sick people, prion proteins adopt a bad conformation, become resistant to degradation and aggregate together: these are known as 'scrapie' prion proteins, PrPsc. The protein deposits multiply and accumulate inside and outside neurons, causing them to malfunction and eventually degenerate. The propagation of prions is based on their ability to interact with the normal form of the prion protein, changing its conformation and converting it into the pathological form.
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Research at the Paris Brain Institute


Most neurodegenerative diseases, from Alzheimer’s to Parkinson’s to amyotrophic lateral sclerosis, share common features with prion diseases. Studying the mechanisms by which prion proteins propagate provides valuable information about these diseases. Marie-Claude Potier and Stéphane Haïk’s “Alzheimer’s disease, prion diseases” team is particularly interested in the propagation of lesions typical of Alzheimer’s disease, amyloid plaques, which appear to behave in a similar way to pathological prion proteins. Understanding these ‘prion-like’ mechanisms could benefit both diseases.


For more information: https://institutducerveau-icm.org/en/actualite/prion-diseases-a-model-for-neurodegenerative-disorders/