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

    Author(s)
    McLeary, Fleur A
    Rcom-H'cheo-Gauthier, Alexandre N
    Kinder, Jessica
    Goulding, Michael
    Khoo, Tien K
    Mellick, George D
    Chung, Roger S
    Pountney, Dean L
    Griffith University Author(s)
    Mellick, George
    Pountney, Dean L.
    Khoo, Tien Kheng
    Year published
    2018
    Metadata
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    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 ...
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    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.
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    Journal Title
    Neurotoxicity Research
    Volume
    33
    Issue
    2
    DOI
    https://doi.org/10.1007/s12640-017-9825-7
    Note
    This publication has been entered into Griffith Research Online as an Advanced Online Version.
    Subject
    Biochemistry and cell biology
    Clinical sciences
    Clinical sciences not elsewhere classified
    Neurosciences
    Publication URI
    http://hdl.handle.net/10072/372384
    Collection
    • Journal articles

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