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

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 a-synuclein. Results demonstrate that Prnp expression is not mandatory for a-synuclein spreading. However, although the pathological spreading of a-synuclein can take place in the absence of Prnp, a-synuclein expanded faster in PrPC-overexpressing mice. In addition, a-synuclein binds strongly on PrPC-expressing cells, suggesting a role in modulating the effect of a-synuclein fibrils

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

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