期刊
MOLECULAR NEUROBIOLOGY
卷 55, 期 3, 页码 1847-1860出版社
SPRINGER
DOI: 10.1007/s12035-017-0451-4
关键词
Synuclein; Amyloid spreading; Prnp; Microfluidic devices
资金
- Spanish Ministry of Economy and Competitiveness [BFU2015-67777-R]
- Spanish prion network [AGL2015-71764-REDT]
- Generalitat de Catalunya [SGR2014-1218, 2015-FI-B-00817]
- CIBERNED [PI2014/02-4, PRY-14-114, PRY2016-02]
- La Caixa Obra Social Foundation
- La Marato de TV3
- European Research Council (ERC) [ERC-2012-StG 306751]
- MINECO [DPI2015-64221-C2-1-R]
- Fondo de Investigacion Sanitaria-Instituto de Salud Carlos III
- MINECO/FEDER [BIO2015-63557-R, TEC2015-72718-EXP]
- Seventh Framework Programme of the European Commission [278486, 228685-2]
- Instituto de Salud Carlos III-Fondos FEDER
- Instituto de Salud Carlos III [PI10/01171]
- Botin Foundation
- CIBERNED
- Marato TV3 foundation
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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