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

doi:10.1007/s12035-017-0451-4

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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Abstract

© 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 language	English
Pages (from-to)	1847-1860
Journal	Molecular Neurobiology
Volume	55
Issue number	3
DOIs	https://doi.org/10.1007/s12035-017-0451-4
Publication status	Published - 1 Mar 2018

Keywords

Amyloid spreading
Microfluidic devices
Prnp
Synuclein

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10.1007/s12035-017-0451-4

https://ddd.uab.cat/record/188578

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title = "Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons",

abstract = "{\textcopyright} 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.",

keywords = "Amyloid spreading, Microfluidic devices, Prnp, Synuclein",

author = "Laura Urrea and Miriam Segura-Feliu and Masami Masuda-Suzukake and Arnau Hervera and Lucas Pedraz and {Garc{\'i}a Aznar}, {Jos{\'e} Manuel} and Miquel Vila and Josep Samitier and Eduard Torrents and Isidro Ferrer and Rosalina Gav{\'i}n and Masato Hagesawa and {del R{\'i}o}, {Jos{\'e} Antonio}",

year = "2018",

month = mar,

day = "1",

doi = "10.1007/s12035-017-0451-4",

language = "English",

volume = "55",

pages = "1847--1860",

journal = "Molecular Neurobiology",

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TY - JOUR

T1 - Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons

AU - Urrea, Laura

AU - Segura-Feliu, Miriam

AU - Masuda-Suzukake, Masami

AU - Hervera, Arnau

AU - Pedraz, Lucas

AU - García Aznar, José Manuel

AU - Vila, Miquel

AU - Samitier, Josep

AU - Torrents, Eduard

AU - Ferrer, Isidro

AU - Gavín, Rosalina

AU - Hagesawa, Masato

AU - del Río, José Antonio

PY - 2018/3/1

Y1 - 2018/3/1

N2 - © 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.

AB - © 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.

KW - Amyloid spreading

KW - Microfluidic devices

KW - Prnp

KW - Synuclein

U2 - 10.1007/s12035-017-0451-4

DO - 10.1007/s12035-017-0451-4

M3 - Article

SN - 0893-7648

VL - 55

SP - 1847

EP - 1860

JO - Molecular Neurobiology

JF - Molecular Neurobiology

IS - 3

ER -

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

Abstract

Keywords

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