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@ARTICLE{Ulusoy:138081,
author = {Ulusoy, Ayse and Musgrove, Ruth E and Rusconi, Raffaella
and Klinkenberg, Michael and Helwig, Michael and Schneider,
Anja and Di Monte, Donato A},
title = {{N}euron-to-neuron α-synuclein propagation in vivo is
independent of neuronal injury.},
journal = {Acta Neuropathologica Communications},
volume = {3},
number = {1},
issn = {2051-5960},
address = {London},
publisher = {Biomed Central},
reportid = {DZNE-2020-04403},
pages = {13},
year = {2015},
abstract = {Interneuronal propagation of α-synuclein has been
demonstrated in a variety of experimental models and may be
involved in disease progression during the course of human
synucleinopathies. The aim of this study was to assess the
role that neuronal injury or, vice versa, cell integrity
could have in facilitating interneuronal α-synuclein
transfer and consequent protein spreading in an in vivo
animal model.Viral vectors carrying the DNA for human
α-synuclein were injected into the rat vagus nerve to
trigger protein overexpression in the medulla oblongata and
consequent spreading of human α-synuclein toward pons,
midbrain and forebrain. Two vector preparations sharing the
same viral construct were manufactured using identical
procedures with the exception of methods for their
purification. They were also injected at concentrations that
induced comparable levels of α-synuclein
transduction/overexpression in the medulla oblongata.
α-Synuclein load was associated with damage (at 6 weeks
post injection) and death (at 12 weeks) of medullary neurons
after treatment with only one of the two vector
preparations. Of note, neuronal injury and degeneration was
accompanied by a substantial reduction of caudo-rostral
propagation of human α-synuclein.Interneuronal α-synuclein
transfer, which underlies protein spreading from the medulla
oblongata to more rostral brain regions in this rat model,
is not a mere consequence of passive release from damaged or
dead neurons. Neuronal injury and degeneration did not
exacerbate α-synuclein propagation. In fact, data suggest
that cell-to-cell passage of α-synuclein may be
particularly efficient between intact, relatively healthy
neurons.},
keywords = {Animals / Brain: metabolism / Disease Models, Animal /
Female / Gene Transfer Techniques / Humans / Medulla
Oblongata: metabolism / Nerve Degeneration: metabolism /
Nerve Degeneration: pathology / Neural Pathways: metabolism
/ Neural Pathways: pathology / Neurons: metabolism /
Neurons: pathology / Parkinson Disease: metabolism / Rats /
Rats, Sprague-Dawley / alpha-Synuclein: metabolism / SNCA
protein, human (NLM Chemicals) / alpha-Synuclein (NLM
Chemicals)},
cin = {AG Di Monte / AG Schneider Göttingen},
ddc = {610},
cid = {I:(DE-2719)1013008 / I:(DE-2719)1440011},
pnm = {342 - Disease Mechanisms and Model Systems (POF3-342) / 344
- Clinical and Health Care Research (POF3-344)},
pid = {G:(DE-HGF)POF3-342 / G:(DE-HGF)POF3-344},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:25853980},
pmc = {pmc:PMC4369863},
doi = {10.1186/s40478-015-0198-y},
url = {https://pub.dzne.de/record/138081},
}