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| Home > Publications Database > Cellular prion protein mediates toxic signaling of amyloid beta. |
| Journal Article | DZNE-2020-02832 |
; ;
2012
Karger
Basel
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Please use a persistent id in citations: doi:10.1159/000332596
Abstract: Prion diseases in humans and animals comprise a group of invariably fatal neurodegenerative diseases characterized by the formation of a pathogenic protein conformer designated PrP(Sc) and infectious particles denoted prions. The cellular prion protein (PrP(C)) has a central role in the pathogenesis of prion disease. First, it is the precursor of PrP(Sc) and infectious prions and second, its expression on neuronal cells is required to mediate toxic effects of prions. To specifically study the role of PrP(C) as a mediator of toxic signaling, we have developed novel cell culture models, including primary neurons prepared from PrP-deficient mice. Using these approaches we have been able to show that PrP(C) can interact with and mediate toxic signaling of various β-sheet-rich conformers of different origins, including amyloid β, suggesting a pathophysiological role of the prion protein beyond prion diseases.
Keyword(s): Amyloid beta-Peptides: metabolism (MeSH) ; Amyloid beta-Peptides: toxicity (MeSH) ; Animals (MeSH) ; Humans (MeSH) ; Mice (MeSH) ; Mice, Transgenic (MeSH) ; Prions: genetics (MeSH) ; Prions: metabolism (MeSH) ; Protein Conformation (MeSH) ; Signal Transduction: drug effects (MeSH) ; Signal Transduction: physiology (MeSH) ; Amyloid beta-Peptides ; Prions
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