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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},
}