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• W2017040646 abstract "Several neurodegenerative diseases are typified by intraneuronal α-synuclein deposits, synaptic dysfunction, and dementia. While even modest α-synuclein elevations can be pathologic, the precise cascade of events induced by excessive α-synuclein and eventually culminating in synaptotoxicity is unclear. To elucidate this, we developed a quantitative model system to evaluate evolving α-synuclein-induced pathologic events with high spatial and temporal resolution, using cultured neurons from brains of transgenic mice overexpressing fluorescent-human-α-synuclein. Transgenic α-synuclein was pathologically altered over time and overexpressing neurons showed striking neurotransmitter release deficits and enlarged synaptic vesicles; a phenotype reminiscent of previous animal models lacking critical presynaptic proteins. Indeed, several endogenous presynaptic proteins involved in exocytosis and endocytosis were undetectable in a subset of transgenic boutons (“vacant synapses”) with diminished levels in the remainder, suggesting that such diminutions were triggering the overall synaptic pathology. Similar synaptic protein alterations were also retrospectively seen in human pathologic brains, highlighting potential relevance to human disease. Collectively the data suggest a previously unknown cascade of events where pathologic α-synuclein leads to a loss of a number of critical presynaptic proteins, thereby inducing functional synaptic deficits." @default.
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• W2017040646 date "2010-06-16" @default.
• W2017040646 modified "2023-10-16" @default.
• W2017040646 title "A Pathologic Cascade Leading to Synaptic Dysfunction in -Synuclein-Induced Neurodegeneration" @default.
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• W2017040646 doi "https://doi.org/10.1523/jneurosci.1091-10.2010" @default.
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