TY  - JOUR
AU  - Resenberger, Ulrike K
AU  - Winklhofer, Konstanze F
AU  - Tatzelt, Jörg
TI  - Neuroprotective and neurotoxic signaling by the prion protein.
JO  - Topics in current chemistry
VL  - 305
SN  - 0340-1022
CY  - Heidelberg
PB  - Springer
M1  - DZNE-2020-02777
SN  - 978-3-642-24066-9 (print)
T2  - Topics in Current Chemistry
SP  - 101-119
PY  - 2011
AB  - Prion diseases in humans and animals are characterized by progressive neurodegeneration and the formation of infectious particles called prions. Both features are intimately linked to a conformational transition of the cellular prion protein (PrP(C)) into aberrantly folded conformers with neurotoxic and self-replicating activities. Interestingly, there is increasing evidence that the infectious and neurotoxic properties of PrP conformers are not necessarily coupled. Transgenic mouse models revealed that some PrP mutants interfere with neuronal function in the absence of infectious prions. Vice versa, propagation of prions can occur without causing neurotoxicity. Consequently, it appears plausible that two partially independent pathways exist, one pathway leading to the propagation of infectious prions and another one that mediates neurotoxic signaling. In this review we will summarize current knowledge of neurotoxic PrP conformers and discuss the role of PrP(C) as a mediator of both stress-protective and neurotoxic signaling cascades.
KW  - Animals
KW  - Humans
KW  - Mice
KW  - Models, Biological
KW  - Mutation
KW  - Neurodegenerative Diseases: metabolism
KW  - Neurons: metabolism
KW  - Neurons: pathology
KW  - Neurotoxicity Syndromes: metabolism
KW  - Prion Diseases: metabolism
KW  - Prion Diseases: pathology
KW  - Prions: metabolism
KW  - Protein Conformation
KW  - Protein Denaturation
KW  - Protein Folding
KW  - Protein Structure, Tertiary
KW  - Signal Transduction
KW  - Prions (NLM Chemicals)
LB  - PUB:(DE-HGF)3 ; PUB:(DE-HGF)16
C6  - pmid:21598098
DO  - DOI:10.1007/128_2011_160
UR  - https://pub.dzne.de/record/136455
ER  -