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• W2049404795 abstract "Earlier investigations have demonstrated that tubulin co-localizes with alpha-synuclein in Lewy bodies and influences the formation of alpha-synuclein aggregation. However, it is not clear whether aggregated alpha-synuclein has any effects on the function of tubulin, i.e. tubulin polymerization, a critical mechanism by which neurons maintain their morphology and execute functions. In this study, we evaluated the effects of aggregated alpha-synuclein on tubulin polymerization in dopaminergic neurons (MES cells), along with mitochondrial function, cell morphology, and viability. The results indicate that MES cells exposed to extracellular oligomeric alpha-synuclein exhibited decreased tubulin polymerization and mitochondrial function as well as morphological alternation long before cell death. Further investigation showed that internalization of oligomeric alpha-synuclein by neurons appeared to be critical in the process, although direct interaction between tubulin and intracellular oligomeric alpha-synuclein was not necessary. Finally, we demonstrated that neurotoxicity induced by oligomeric alpha-synuclein was largely prevented by overexpressing the neuroprotective protein, DJ-1." @default.
• W2049404795 created "2016-06-24" @default.
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• W2049404795 date "2007-05-01" @default.
• W2049404795 modified "2023-10-14" @default.
• W2049404795 title "Oligomeric α-synuclein inhibits tubulin polymerization" @default.
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• W2049404795 doi "https://doi.org/10.1016/j.bbrc.2007.02.163" @default.
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