We first determined the endocytic route of PrPC in L929 cells.
Several studies report the importance of expression of PrPC in prion pathology30, 31.
Our data illustrate the role of PrPC in facilitating the internalization of α-Syn amyloids.
However, there are no reports of role of PrPC in synucleinopathies.
We have previously reported the inducible stable expression of a human PrPC in murine 3T3 cells.
In this study we provide new insights of how the expression of PrPC in neurons may facilitate the accumulation and spreading of α-Syn aggregates.
Shyng, S. L., Lehmann, S., Moulder, K. L. & Harris, D. A. Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells.
Here, we show the role of the cellular prion protein (PrPC) in mediating the uptake and the spread of recombinant α-Syn amyloids.
Prnp −/− mice neither propagate prions nor develop scrapie suggesting the central role of PrPC in the development of prion diseases23, 24.
However, the role of PrPC in mediating PrPSc formation and its spread in the presence of α-Syn amyloids has never been described.
C1 and N1 fragment formation is a result of increased α-cleavage processing of PrPC in the presence of α-Syn amyloids.
