Río Fernández, José Antonio delFerrer, Isidro (Ferrer Abizanda)Gavín Marín, Rosalina2019-10-082019-12-012018-06-010301-0082https://hdl.handle.net/2445/141852Several studies have indicated that certain misfolded amyloids composed of tau, β-amyloid or α-synuclein can be transferred from cell to cell, suggesting the contribution of mechanisms reminiscent of those by which infective prions spread through the brain. This process of a 'prion-like' spreading between cells is also relevant as a novel putative therapeutic target that could block the spreading of proteinaceous aggregates throughout the brain which may underlie the progressive nature of neurodegenerative diseases. The relevance of β-amyloid oligomers and cellular prion protein (PrPC) binding has been a focus of interest in Alzheimer's disease (AD). At the molecular level, β-amyloid/PrPC interaction takes place in two differently charged clusters of PrPC. In addition to β-amyloid, participation of PrPC in α-synuclein binding and brain spreading also appears to be relevant in α-synucleopathies. This review summarizes current knowledge about PrPC as a putative receptor for amyloid proteins and the physiological consequences of these interactions.16 p.application/pdfengcc-by-nc-nd (c) Elsevier Ltd, 2018http://creativecommons.org/licenses/by-nc-nd/3.0/esAmiloïdosiPèptidsMetabolismeAlfa-sinucleïnaProteïnesAmyloidosisPeptidesMetabolismAlpha-synucleinProteinsinfo:eu-repo/semantics/article6798232019-10-08info:eu-repo/semantics/openAccess29530723