Urrea Zazurca, LauraSegura Feliu, MiriamMasuda-Suzukake, MasamiHervera Abad, ArnauPedraz López, LucasGarcía Aznar, José ManuelVila, MiquelSamitier i Martí, JosepTorrents Serra, EduardFerrer, Isidro (Ferrer Abizanda)Gavín Marín, RosalinaHagesawa, MasatoRío Fernández, José Antonio del2020-12-152020-12-152018-03-01https://hdl.handle.net/2445/172791The cellular prion protein, encoded by the gene Prnp, has been reported to be a receptor of beta-amyloid. Their interaction is mandatory for neurotoxic effects of beta-amyloid oligomers. In this study, we aimed to explore whether the cellular prion protein participates in the spreading of alpha-synuclein. Results demonstrate that Prnp expression is not mandatory for alpha-synuclein spreading. However, although the pathological spreading of alpha-synuclein can take place in the absence of Prnp, alpha-synuclein expanded faster in PrPC-overexpressing mice. In addition, alpha-synuclein binds strongly on PrPC-expressing cells, suggesting a role in modulating the effect of alpha-synuclein fibrils.application/pdfengcc by (c) Urrea Zazurca et al., 2018http://creativecommons.org/licenses/by/3.0/es/Alfa-sinucleïnaPrionsAlpha-synucleinPrionsinfo:eu-repo/semantics/article2020-12-04info:eu-repo/semantics/openAccess28229331