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Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons
by
Gavín, Rosalina
, Vila, Miquel
, García Aznar, José Manuel
, del Río, José Antonio
, Urrea, Laura
, Hagesawa, Masato
, Segura-Feliu, Miriam
, Ferrer, Isidro
, Samitier, Josep
, Torrents, Eduard
, Masuda-Suzukake, Masami
, Hervera, Arnau
, Pedraz, Lucas
in
Alzheimer's disease
/ Axonal transport
/ Fibrils
/ Neurotoxicity
/ Prion protein
/ Protein transport
/ Proteins
/ Rodents
/ Spreading
/ Synuclein
/ β-Amyloid
2018
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Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons
by
Gavín, Rosalina
, Vila, Miquel
, García Aznar, José Manuel
, del Río, José Antonio
, Urrea, Laura
, Hagesawa, Masato
, Segura-Feliu, Miriam
, Ferrer, Isidro
, Samitier, Josep
, Torrents, Eduard
, Masuda-Suzukake, Masami
, Hervera, Arnau
, Pedraz, Lucas
in
Alzheimer's disease
/ Axonal transport
/ Fibrils
/ Neurotoxicity
/ Prion protein
/ Protein transport
/ Proteins
/ Rodents
/ Spreading
/ Synuclein
/ β-Amyloid
2018
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Do you wish to request the book?
Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons
by
Gavín, Rosalina
, Vila, Miquel
, García Aznar, José Manuel
, del Río, José Antonio
, Urrea, Laura
, Hagesawa, Masato
, Segura-Feliu, Miriam
, Ferrer, Isidro
, Samitier, Josep
, Torrents, Eduard
, Masuda-Suzukake, Masami
, Hervera, Arnau
, Pedraz, Lucas
in
Alzheimer's disease
/ Axonal transport
/ Fibrils
/ Neurotoxicity
/ Prion protein
/ Protein transport
/ Proteins
/ Rodents
/ Spreading
/ Synuclein
/ β-Amyloid
2018
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Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons
Journal Article
Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons
2018
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Overview
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.
Publisher
Springer Nature B.V
Subject
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