Evidence map›Paper›PMID 29064068›Full record

ArticleNeurotoxicity research2018

Dexamethasone Inhibits Copper-Induced Alpha-Synuclein Aggregation by a Metallothionein-Dependent Mechanism.

Fleur A McLeary, Alexandre N Rcom-H'cheo-Gauthier, Jessica Kinder, Michael Goulding, Tien K Khoo, George D Mellick, Roger S Chung, Dean L Pountney

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Article in Neurotoxicity research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 17 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Fleur A McLearyMenzies Health Institute Queensland, Griffith University, Gold Coast, QLD, 4222, Australia.
Alexandre N Rcom-H'cheo-GauthierMenzies Health Institute Queensland, Griffith University, Gold Coast, QLD, 4222, Australia.
Jessica KinderMenzies Health Institute Queensland, Griffith University, Gold Coast, QLD, 4222, Australia.
Michael GouldingMenzies Health Institute Queensland, Griffith University, Gold Coast, QLD, 4222, Australia.
Tien K KhooMenzies Health Institute Queensland, Griffith University, Gold Coast, QLD, 4222, Australia.
George D MellickGriffith Institute for Drug Discovery, Griffith University, Nathan, QLD, 4111, Australia.
Roger S ChungDepartment of Biomedical Sciences, Faculty of Medicine & Health Sciences, Macquarie University, Sydney, NSW, Australia.
Dean L PountneyMenzies Health Institute Queensland, Griffith University, Gold Coast, QLD, 4222, Australia. d.pountney@griffith.edu.au.
Griffith University · AUMacquarie University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intracellular aggregates of α-synuclein are the pathological hallmark of Parkinson's disease (PD) and dementia with Lewy bodies (DLB), being linked to neurotoxicity. Multiple triggers of α-synuclein aggregation have been implicated, including raised copper. The potential protective role of the endogenous copper-/zinc-binding proteins, metallothioneins (MT), has been explored in relation to copper-induced α-synuclein aggregation. Up-regulated endogenous expression of MT was induced in SHSY-5Y cells by the synthetic glucocorticoid analogue, dexamethasone. After treatment to induce endogenous MT expression, immunofluorescence confocal microscopy was used to quantify protein aggregates in cells with/without copper treatment. MT induction resulted in significant (p < 0.01), dose-dependent up-regulation of MT expression and significant reduction in Cu-dependent α-synuclein intracellular aggregates (p < 0.01) that could be suppressed by MT-specific siRNA. Ubiquitous (MT-2) and brain-specific (MT-3) isoforms were investigated by transient transfection of the GFP-fusion proteins, observing equivalent α-synuclein aggregate suppression by each. These studies indicate MT induction could have potential in PD/DLB neuroprotective therapy by suppressing α-synuclein aggregation.

Indexed as

alpha-SynucleinBrainCell Line, TumorCopperDexamethasoneHumansLewy Body DiseaseMetallothioneinParkinson Diseasealpha-SynucleinCopperDexamethasoneMetallothioneinAlpha-synucleinCopperDementia with Lewy bodiesMetallothioneinNeurodegenerationNeuroprotectionOxidative stressParkinson’s disease

Identifiers

PMID29064068
OpenAlexW2765749217

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.