% 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{Paiva:140217,
author = {Paiva, Isabel and Jain, Gaurav and Lázaro, Diana F and
Jerčić, Kristina Gotovac and Hentrich, Thomas and
Kerimoglu, Cemil and Pinho, Raquel and Szegő, Èva M and
Burkhardt, Susanne and Capece, Vincenzo and Halder, Rashi
and Islam, Rezaul and Xylaki, Mary and Caldi Gomes, Lucas A
and Roser, Anna-Elisa and Lingor, Paul and Schulze-Hentrich,
Julia M and Borovečki, Fran and Fischer, André and
Outeiro, Tiago F},
title = {{A}lpha-synuclein deregulates the expression of {COL}4{A}2
and impairs {ER}-{G}olgi function.},
journal = {Neurobiology of disease},
volume = {119},
issn = {0969-9961},
address = {Orlando, Fla.},
publisher = {Academic Press},
reportid = {DZNE-2020-06539},
pages = {121-135},
year = {2018},
abstract = {Alpha-synuclein (aSyn) is the major protein component of
Lewy bodies and Lewy neurites, the typical pathological
hallmarks in Parkinson's disease (PD) and Dementia with Lewy
bodies. aSyn is capable of inducing transcriptional
deregulation, but the precise effect of specific aSyn
mutants associated with familial forms of PD, remains
unclear. Here, we used transgenic mice overexpressing human
wild-type (WT) or A30P aSyn to compare the transcriptional
profiles of the two animal models. We found that A30P aSyn
promotes strong transcriptional deregulation and increases
DNA binding. Interestingly, COL4A2, a major component of
basement membranes, was found to be upregulated in both A30P
aSyn transgenic mice and in dopaminergic neurons expressing
A30P aSyn, suggesting a crucial role for collagen related
genes in aSyn-induced toxicity. Finally, we observed that
A30P aSyn alters Golgi morphology and increases the
susceptibility to endoplasmic reticulum (ER) stress in
dopaminergic cells. In total, our findings provide novel
insight into the putative role of aSyn on transcription and
on the molecular mechanisms involved, thereby opening novel
avenues for future therapeutic interventions in PD and other
synucleinopathies.},
keywords = {Animals / Cells, Cultured / Collagen Type IV: biosynthesis
/ Collagen Type IV: genetics / Endoplasmic Reticulum:
physiology / Gene Expression / Golgi Apparatus: physiology /
Humans / Mice / Mice, Inbred C57BL / Mice, Transgenic /
Peptide Fragments: biosynthesis / Peptide Fragments:
genetics / alpha-Synuclein: biosynthesis / alpha-Synuclein:
genetics / Col4a2 protein, mouse (NLM Chemicals) / Collagen
Type IV (NLM Chemicals) / Peptide Fragments (NLM Chemicals)
/ Snca protein, mouse (NLM Chemicals) / alpha-Synuclein (NLM
Chemicals)},
cin = {AG Fischer / AG Bonn 2},
ddc = {570},
cid = {I:(DE-2719)1410002 / I:(DE-2719)1440012},
pnm = {342 - Disease Mechanisms and Model Systems (POF3-342)},
pid = {G:(DE-HGF)POF3-342},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:30092270},
doi = {10.1016/j.nbd.2018.08.001},
url = {https://pub.dzne.de/record/140217},
}