Home > Publications Database > Alpha-synuclein deregulates the expression of COL4A2 and impairs ER-Golgi function. > print

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024 7 _ |a 10.1016/j.nbd.2018.08.001
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024 7 _ |a pmid:30092270
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024 7 _ |a 0969-9961
|2 ISSN
024 7 _ |a 1095-953X
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024 7 _ |a altmetric:46641495
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037 _ _ |a DZNE-2020-06539
041 _ _ |a English
082 _ _ |a 570
100 1 _ |a Paiva, Isabel
|b 0
245 _ _ |a Alpha-synuclein deregulates the expression of COL4A2 and impairs ER-Golgi function.
260 _ _ |a Orlando, Fla.
|c 2018
|b Academic Press
264 _ 1 |3 print
|2 Crossref
|b Elsevier BV
|c 2018-11-01
336 7 _ |a article
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336 7 _ |a ARTICLE
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336 7 _ |a Journal Article
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520 _ _ |a 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.
536 _ _ |a 342 - Disease Mechanisms and Model Systems (POF3-342)
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542 _ _ |i 2018-11-01
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|u https://www.elsevier.com/tdm/userlicense/1.0/
588 _ _ |a Dataset connected to CrossRef, PubMed,
650 _ 7 |a Col4a2 protein, mouse
|2 NLM Chemicals
650 _ 7 |a Collagen Type IV
|2 NLM Chemicals
650 _ 7 |a Peptide Fragments
|2 NLM Chemicals
650 _ 7 |a Snca protein, mouse
|2 NLM Chemicals
650 _ 7 |a alpha-Synuclein
|2 NLM Chemicals
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Cells, Cultured
|2 MeSH
650 _ 2 |a Collagen Type IV: biosynthesis
|2 MeSH
650 _ 2 |a Collagen Type IV: genetics
|2 MeSH
650 _ 2 |a Endoplasmic Reticulum: physiology
|2 MeSH
650 _ 2 |a Gene Expression
|2 MeSH
650 _ 2 |a Golgi Apparatus: physiology
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Mice
|2 MeSH
650 _ 2 |a Mice, Inbred C57BL
|2 MeSH
650 _ 2 |a Mice, Transgenic
|2 MeSH
650 _ 2 |a Peptide Fragments: biosynthesis
|2 MeSH
650 _ 2 |a Peptide Fragments: genetics
|2 MeSH
650 _ 2 |a alpha-Synuclein: biosynthesis
|2 MeSH
650 _ 2 |a alpha-Synuclein: genetics
|2 MeSH
700 1 _ |a Jain, Gaurav
|0 P:(DE-2719)2811223
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700 1 _ |a Lázaro, Diana F
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700 1 _ |a Jerčić, Kristina Gotovac
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700 1 _ |a Hentrich, Thomas
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700 1 _ |a Kerimoglu, Cemil
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700 1 _ |a Pinho, Raquel
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700 1 _ |a Szegő, Èva M
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700 1 _ |a Burkhardt, Susanne
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700 1 _ |a Capece, Vincenzo
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700 1 _ |a Halder, Rashi
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700 1 _ |a Xylaki, Mary
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700 1 _ |a Caldi Gomes, Lucas A
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700 1 _ |a Roser, Anna-Elisa
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700 1 _ |a Lingor, Paul
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700 1 _ |a Schulze-Hentrich, Julia M
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700 1 _ |a Borovečki, Fran
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700 1 _ |a Fischer, André
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700 1 _ |a Outeiro, Tiago F
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773 1 8 |a 10.1016/j.nbd.2018.08.001
|b : Elsevier BV, 2018-11-01
|p 121-135
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|t Neurobiology of Disease
|v 119
|y 2018
|x 0969-9961
773 _ _ |a 10.1016/j.nbd.2018.08.001
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