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

Laura Urrea, Miriam Segura-Feliu, Masami Masuda-Suzukake, Arnau Hervera, Lucas Pedraz, José Manuel García Aznar, Miquel Vila, Josep Samitier, Eduard Torrents, Isidro Ferrer, Rosalina Gavín, Masato Hagesawa, José Antonio del Río

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42 Citations (Scopus)


© 2017, The Author(s). The cellular prion protein, encoded by the gene Prnp, has been reported to be a receptor of β-amyloid. Their interaction is mandatory for neurotoxic effects of β-amyloid oligomers. In this study, we aimed to explore whether the cellular prion protein participates in the spreading of α-synuclein. Results demonstrate that Prnp expression is not mandatory for α-synuclein spreading. However, although the pathological spreading of α-synuclein can take place in the absence of Prnp, α-synuclein expanded faster in PrPC-overexpressing mice. In addition, α-synuclein binds strongly on PrPC-expressing cells, suggesting a role in modulating the effect of α-synuclein fibrils.
Original languageEnglish
Pages (from-to)1847-1860
JournalMolecular Neurobiology
Issue number3
Publication statusPublished - 1 Mar 2018


  • Amyloid spreading
  • Microfluidic devices
  • Prnp
  • Synuclein


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