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Mol Neurobiol
; 55(3): 1847-1860, 2018 03.
Article
in English
| MEDLINE
| ID: mdl-28229331
ABSTRACT
The cellular prion protein, encoded by the gene Prnp, has been reported to be a receptor of ß-amyloid. Their interaction is mandatory for neurotoxic effects of ß-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.
Subject(s)
Neurons/metabolism , PrPC Proteins/genetics , PrPC Proteins/metabolism , alpha-Synuclein/genetics , alpha-Synuclein/metabolism , Animals , Cells, Cultured , HEK293 Cells , Humans , Male , Mice , Mice, 129 Strain , Mice, Inbred C57BL , Mice, Transgenic , Prion Proteins/genetics , Prion Proteins/metabolism , Protein Transport/physiology
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