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- W2561002833 abstract "Aggregation of the pre-synaptic protein, α-synuclein (α-syn), is the key etiological factor in Parkinson's disease (PD) and other alpha-synucleinopathies, such as multiple system atrophy (MSA) and Dementia with Lewy bodies (DLB). Various triggers for pathological α-syn aggregation have been elucidated, including post-translational modifications, oxidative stress, and binding of metal ions, such as calcium. Raised neuronal calcium levels in PD may occur due to mitochondrial dysfunction and/or may relate to calcium channel dysregulation or the reduced expression of the neuronal calcium buffering protein, calbindin-D28k. Recent results on human tissue and a mouse oxidative stress model show that neuronal calbindin-D28k expression excludes α-syn inclusion bodies. Previously, cell culture model studies have shown that transient increases of intracellular free Ca(II), such as by opening of the voltage-gated plasma calcium channels, could induce cytoplasmic aggregates of α-syn. Raised intracellular free calcium and oxidative stress also act cooperatively to promote α-syn aggregation. The association between raised neuronal calcium, α-syn aggregation, oxidative stress, and neurotoxicity is reviewed in the context of neurodegenerative α-syn disease and potential mechanism-based therapies." @default.
- W2561002833 created "2017-01-06" @default.
- W2561002833 creator A5000305786 @default.
- W2561002833 creator A5010893750 @default.
- W2561002833 creator A5030829136 @default.
- W2561002833 creator A5089732655 @default.
- W2561002833 date "2016-12-20" @default.
- W2561002833 modified "2023-10-17" @default.
- W2561002833 title "Calcium: Alpha-Synuclein Interactions in Alpha-Synucleinopathies" @default.
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