title: Taking advantage of physiological proteolytic processing of the prion protein for a therapeutic perspective in prion and Alzheimer diseases.
abstract: Prion and Alzheimer diseases are fatal neurodegenerative diseases caused by misfolding and aggregation of the cellular prion protein (PrP(C)) and the β-amyloid peptide, respectively. Soluble oligomeric species rather than large aggregates are now believed to be neurotoxic. PrP(C) undergoes three proteolytic cleavages as part of its natural life cycle, α-cleavage, β-cleavage, and ectodomain shedding. Recent evidences demonstrate that the resulting secreted PrP(C) molecules might represent natural inhibitors against soluble toxic species. In this mini-review, we summarize recent observations suggesting the potential benefit of using PrP(C)-derived molecules as therapeutic agents in prion and Alzheimer diseases.
authors: Maxime
authors: M
authors: Béland
authors: Xavier
authors: X
authors: Roucou
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism* / Q000628:therapy; D006801:Humans; D018621:PrPC Proteins / Q000378:metabolism*; D017096:Prion Diseases / Q000378:metabolism* / Q000628:therapy; D059748:Proteolysis
chemical_list: D018621:PrPC Proteins