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@INPROCEEDINGS{Tatzelt:145359,
      author       = {Tatzelt, Jörg},
      title        = {{OR}-28: {T}he cellular prion protein mediatesneurotoxic
                      signaling of scrapie prions and {A}β},
      journal      = {Prion},
      volume       = {6},
      number       = {Supplement 1},
      issn         = {1933-6896},
      reportid     = {DZNE-2020-00715},
      pages        = {15},
      year         = {2012},
      abstract     = {Neuronal 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.},
      month         = {May},
      date          = {2012-05-09},
      organization  = {International Prion Congress—Prion
                       2012, Amsterdam (The Netherlands), 9
                       May 2012 - 12 May 2012},
      cin          = {Ext AG Tatzelt},
      ddc          = {570},
      cid          = {I:(DE-2719)5000053},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)1 / PUB:(DE-HGF)16},
      url          = {https://pub.dzne.de/record/145359},
}