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@ARTICLE{Klinkenberg:256448,
      author       = {Klinkenberg, Michael and Helwig, Michael and Pinto-Costa,
                      Rita and Rollar, Angela and Rusconi, Raffaella and Di Monte,
                      Donato A and Ulusoy, Ayse},
      title        = {{I}nterneuronal {I}n {V}ivo {T}ransfer of {S}ynaptic
                      {P}roteins.},
      journal      = {Cells},
      volume       = {12},
      number       = {4},
      issn         = {2073-4409},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {DZNE-2023-00310},
      pages        = {569},
      year         = {2023},
      note         = {CC BY},
      abstract     = {Neuron-to-neuron transfer of pathogenic α-synuclein
                      species is a mechanism of likely relevance to Parkinson's
                      disease development. Experimentally, interneuronal
                      α-synuclein spreading from the low brainstem toward higher
                      brain regions can be reproduced by the administration of AAV
                      vectors encoding for α-synuclein into the mouse vagus
                      nerve. The aim of this study was to determine whether
                      α-synuclein's spreading ability is shared by other
                      proteins. Given α-synuclein synaptic localization,
                      experiments involved intravagal injections of AAVs encoding
                      for other synaptic proteins, β-synuclein, VAMP2, or SNAP25.
                      Administration of AAV-VAMP2 or AAV-SNAP25 caused robust
                      transduction of either of the proteins in the dorsal medulla
                      oblongata but was not followed by interneuronal VAMP2 or
                      SNAP25 transfer and caudo-rostral spreading. In contrast,
                      AAV-mediated β-synuclein overexpression triggered its
                      spreading to more frontal brain regions. The aggregate
                      formation was investigated as a potential mechanism involved
                      in protein spreading, and consistent with this hypothesis,
                      results showed that overexpression of β-synuclein, but not
                      VAMP2 or SNAP25, in the dorsal medulla oblongata was
                      associated with pronounced protein aggregation. Data
                      indicate that interneuronal protein transfer is not a mere
                      consequence of increased expression or synaptic
                      localization. It is rather promoted by structural/functional
                      characteristics of synuclein proteins that likely include
                      their tendency to form aggregate species.},
      keywords     = {Mice / Animals / alpha-Synuclein: metabolism /
                      beta-Synuclein: metabolism / Parkinson Disease: metabolism /
                      Brain: metabolism / Brain Stem: pathology /
                      Vesicle-Associated Membrane Protein 2: metabolism /
                      Parkinson’s disease (Other) / Parkinson’s disease
                      (Other) / animal models (Other) / oligomerization (Other) /
                      protein spreading (Other) / vagus nerve (Other) /
                      alpha-Synuclein (NLM Chemicals) / beta-Synuclein (NLM
                      Chemicals) / Vesicle-Associated Membrane Protein 2 (NLM
                      Chemicals)},
      cin          = {AG Di Monte},
      ddc          = {570},
      cid          = {I:(DE-2719)1013008},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36831238},
      pmc          = {pmc:PMC9954582},
      doi          = {10.3390/cells12040569},
      url          = {https://pub.dzne.de/record/256448},
}