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 PrP-overexpressing mice. In addition, α-synuclein binds strongly on PrP-expressing cells, suggesting a role in modulating the effect of α-synuclein fibrils.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5840251 | PMC |
http://dx.doi.org/10.1007/s12035-017-0451-4 | DOI Listing |
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