% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{PintoCosta:169044,
author = {Pinto-Costa, Rita and Harbachova, Eugenia and La Vitola,
Pietro and Di Monte, Donato Antonio},
title = {{O}verexpression-{I}nduced α-{S}ynuclein {B}rain
{S}preading.},
journal = {Neurotherapeutics},
volume = {20},
number = {1},
issn = {1933-7213},
address = {New York, NY},
publisher = {Springer},
reportid = {DZNE-2022-01766},
pages = {83-96},
year = {2023},
abstract = {Interneuronal transfer of pathological α-synuclein species
is thought to play an important role in the progressive
advancement of Lewy pathology and increasing severity of
clinical manifestations in Parkinson's and other diseases
commonly referred to as synucleinopathies.
Pathophysiological conditions and mechanisms triggering this
trans-synaptic spreading bear therefore significant
pathogenetic implications but have yet to be fully
elucidated. In vivo experimental models support the
conclusion that increased expression of intraneuronal
α-synuclein can itself induce protein spreading throughout
the brain as well as from the brain to peripheral tissues.
For example, overexpression of α-synuclein targeted to the
rodent dorsal medulla oblongata results in its transfer and
accumulation into recipient axons innervating this brain
region; through these axons, α-synuclein can then travel
caudo-rostrally and reach other brain sites in the pons,
midbrain, and forebrain. When protein overexpression is
induced in the rodent midbrain, long-distance α-synuclein
spreading can be followed over time; spreading-induced
α-synuclein accumulation affects lower brain regions,
including the dorsal motor nucleus of the vagus, proceeds
through efferent axons of the vagus nerve, and is ultimately
detected within vagal motor nerve endings in the gastric
wall. As discussed in this review, animal models featuring
α-synuclein overexpression not only support a relationship
between α-synuclein burden and protein spreading but have
also provided important clues on conditions/mechanisms
capable of promoting interneuronal α-synuclein transfer.
Intriguing findings include the relationship between
neuronal activity and protein spreading and the role of
oxidant stress in trans-synaptic α-synuclein mobility.},
subtyp = {Review Article},
keywords = {Animals / alpha-Synuclein: metabolism / Brain: metabolism /
Neurons: metabolism / Parkinson Disease: metabolism /
Stomach: innervation / Stomach: metabolism / Synaptic
Transmission: physiology / Synucleinopathies: metabolism /
Vagus Nerve: metabolism / Vagus Nerve: physiology /
alpha-Synuclein (NLM Chemicals) / Animal models (Other) /
Gut-brain axis (Other) / Neuronal activity (Other) /
Oxidative stress (Other) / Parkinson (Other) / Vagus nerve
(Other)},
cin = {AG Di Monte},
ddc = {610},
cid = {I:(DE-2719)1013008},
pnm = {352 - Disease Mechanisms (POF4-352)},
pid = {G:(DE-HGF)POF4-352},
typ = {PUB:(DE-HGF)16},
pmc = {pmc:PMC10119350},
pubmed = {pmid:36512255},
doi = {10.1007/s13311-022-01332-6},
url = {https://pub.dzne.de/record/169044},
}