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@PHDTHESIS{Breid:144786,
      author       = {Breid, Sara},
      title        = {{T}ransmission of pathogenic alpha-synuclein to mice},
      school       = {Rheinische Friedrich-Wilhelms-Universität Bonn},
      type         = {Dissertation},
      address      = {Bonn},
      reportid     = {DZNE-2020-00229},
      pages        = {111 pages},
      year         = {2017},
      note         = {Dissertation, Rheinische Friedrich-Wilhelms-Universität
                      Bonn, 2017},
      abstract     = {α-Synuclein is a soluble, cellular protein that in a
                      number of neurodegenerative diseases, including Parkinson's
                      disease, multiple system atrophy, and Lewy body dementia
                      aggregates into pathological protein deposits. Principles
                      how misfolded and aggregated α-synuclein is transmitted
                      within the central nervous system (CNS) causing neurologic
                      disease were found to be similar to those of prions.
                      Misfolded α-synuclein can be transmitted between cells and
                      act as a seed, recruiting native, unfolded α-synuclein to
                      form insoluble aggregates. The mechanisms and the routes
                      through which pathogenic proteins enter the CNS causing
                      progressive disease are still not completely understood. The
                      work in this thesis confirms previous findings indicating
                      that α-synuclein fibrils intracerebrally injected into
                      wild-type mice for α-synuclein can induce neuropathology in
                      interconnected brain regions as similarly observed in
                      sporadic Parkinson's disease. In contrast, α-synuclein
                      fibrils injected into the tongue muscle of wild-type mice
                      for α-synuclein did not neuroinvade the CNS causing
                      α-synuclein pathology. Moreover, the present study is the
                      first to show, that α-synuclein fibrils peripherally
                      injected into the tongue and the peritoneum of mice
                      overexpressing human α-synuclein, can neuroinvade the CNS,
                      cause widespread α-synuclein pathology and induce
                      neurologic symptoms. The induction of neuropathology was
                      accompanied by neuroinflammation as monitored by astrocytic
                      gliosis and microgliosis. In addition, the study presented
                      here indicates that exposure of mice overexpressing human
                      α-synuclein with pathogenic α-synuclein aerosols was not
                      sufficient for α-synuclein prionoids to enter the brain via
                      the olfactory epithelium and induce neuropathology. In
                      summary, these findings corroborate the prionoid character
                      of misfolded α-synuclein using similar routes like prions
                      to neuroinvade brain and spinal cord and induce neurologic
                      disease.},
      cin          = {AG Tamgüney},
      cid          = {I:(DE-2719)1013022},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)11},
      urn          = {urn:nbn:de:hbz:5n-47847},
      url          = {https://pub.dzne.de/record/144786},
}