In prion diseases, the cellular prion protein (PrP(C)), abundant in neurons, is converted posttranslationally into an amyloid-forming scrapie prion protein (PrP(Sc)), which accumulates in white matter tracts and nerve terminals. The trafficking of PrP(C) in neurons was investigated in vivo by injecting [35S]methionine into the L4 and L5 dorsal root ganglia and the entorhinal cortices of adult rats and by tracing the movement of radiolabeled PrP(C). In both paradigms, labeled 33-35-kDa PrP(C) was transported, within 4 h, to distal axons and nerve terminals cofractionating with proteins in the fast component. Future studies using these methods may allow us to determine whether PrP(C) is converted into PrP(Sc) during axonal transport and whether PrP(Sc) is transported in animals with prion diseases.
|Original language||English (US)|
|Number of pages||4|
|Journal||Journal of Biological Chemistry|
|State||Published - May 20 1994|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology