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000145359 1001_ $$0P:(DE-2719)9000396$$aTatzelt, Jörg$$b0$$udzne
000145359 1112_ $$aInternational Prion Congress—Prion 2012$$cAmsterdam$$d2012-05-09 - 2012-05-12$$wThe Netherlands
000145359 245__ $$aOR-28: The cellular prion protein mediatesneurotoxic signaling of scrapie prions and Aβ
000145359 260__ $$c2012
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000145359 520__ $$aNeuronal dysfunction in different neurodegenerative diseases,such as Alzheimer disease, Parkinson disease, polyglutaminediseases or prion diseases is causally linked to aberrant proteinfolding. Our goal is to reach an understanding of how neurotoxicconformers are formed within the context of neuronal cells and interfere with neuronal integrity. We have previously establisheda cell culture model to shown that PrPSc-induced cell death isdependent on the expression of GPI-anchored PrPC and to identify domains of PrPC required for this activity.1 Employing celllines and primary neurons prepared from wild-type or PrP0/0mice we recently showed that PrPC can interact with and mediate toxic signaling of various β-sheet-rich conformers of different origins, including Aβ, suggesting a pathophysiological role ofthe prion protein beyond prion diseases. Notably, the N-terminaldomain of PrPC mediated binding to the β-conformers, and asecreted version of the isolated N-terminal domain interferedwith toxic signaling via PrPC.2 The mechanisms underlyingthe toxic activity of β-sheet-rich conformers are far from beingunderstood, but it is conceivable that different upstream eventsconverge at similar neurotoxic signaling pathways. We thereforestarted to define components downstream of PrPC involved intoxic signaling. Interestingly, Aβ-, PrPSc- and β-peptide-inducedtoxicity was significantly reduced by pharmacological blockage ofNMDA receptor activity. In addition, we observed that PrPSc caninduce mitochondrial alterations in neurons, such as perinuclearclustering of mitochondria.
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000145359 773__ $$0PERI:(DE-600)2267671-5$$nSupplement 1$$p15$$tPrion$$v6$$x1933-6896$$y2012
000145359 8564_ $$uhttps://www.tandfonline.com/doi/abs/10.4161/pri.20605
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