Abstract
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 (PrPC) 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 PrPC as a mediator of both stress-protective and neurotoxic signaling cascades.
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Work of the authors was supported by grants from the Deutsche Forschungsgemeinschaft (SFB 596), the Max Planck Society, and the BMBF (BioDisc, DIP5.1).
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Resenberger, U.K., Winklhofer, K.F., Tatzelt, J. (2011). Neuroprotective and Neurotoxic Signaling by the Prion Protein. In: Tatzelt, J. (eds) Prion Proteins. Topics in Current Chemistry, vol 305. Springer, Berlin, Heidelberg. https://doi.org/10.1007/128_2011_160
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