Prion protein or PrP is present in most of our cells. Although highly conserved between species, its role is poorly known. In the neurons of sick people, prion proteins take on a wrong conformation, become resistant to degradation, and aggregate with each other, called scrapie prion proteins, PrPsc. Protein deposits multiply and then accumulate inside and outside the 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, change its conformation and convert it into a pathological form.
At Paris Brain Institute
Most neurodegenerative diseases, from Alzheimer’s to Parkinson’s to amyotrophic lateral sclerosis, share characteristics with prion diseases. The study of prion protein propagation mechanisms provides valuable insights into these diseases. The team of Marie-Claude Potier and Stéphane Haïk, “Alzheimer’s Disease, Prion Diseases” is particularly interested in the spread of the typical Alzheimer’s disease lesions, amyloid plaques, which appear to behave similarly to pathological prion proteins. Understanding these prion-like mechanisms could benefit both pathologies.
