TY  - JOUR
AU  - Resenberger, Ulrike K
AU  - Winklhofer, Konstanze F
AU  - Tatzelt, Jörg
TI  - Cellular prion protein mediates toxic signaling of amyloid beta.
JO  - Neurodegenerative diseases
VL  - 10
IS  - 1-4
SN  - 1660-2862
CY  - Basel
PB  - Karger
M1  - DZNE-2020-02832
SP  - 298-300
PY  - 2012
AB  - 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.
KW  - Amyloid beta-Peptides: metabolism
KW  - Amyloid beta-Peptides: toxicity
KW  - Animals
KW  - Humans
KW  - Mice
KW  - Mice, Transgenic
KW  - Prions: genetics
KW  - Prions: metabolism
KW  - Protein Conformation
KW  - Signal Transduction: drug effects
KW  - Signal Transduction: physiology
KW  - Amyloid beta-Peptides (NLM Chemicals)
KW  - Prions (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:22156337
DO  - DOI:10.1159/000332596
UR  - https://pub.dzne.de/record/136510
ER  -