Involvement of Cellular Prion Protein in alpha-Synuclein Transport in Neurons

The 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-synu...

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Detalles Bibliográficos
Autores: Urrea Zazurca, Laura, Segura Feliu, Miriam, Masuda-Suzukake, Masami, Hervera Abad, Arnau, Pedraz López, Lucas, García Aznar, José Manuel, Vila, Miquel, Samitier i Martí, Josep, Torrents Serra, Eduard, Ferrer, Isidro (Ferrer Abizanda), Gavín Marín, Rosalina, Hagesawa, Masato, Río Fernández, José Antonio del
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2018
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/172791
Acceso en línea:https://hdl.handle.net/2445/172791
Access Level:acceso abierto
Palabra clave:Alfa-sinucleïna
Prions
Alpha-synuclein
Descripción
Sumario:The 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.

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