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• W1989855060 abstract "Parkinson's disease is a movement disorder that results from a loss of dopaminergic neurons in the substantia nigra. The disease is characterized by mitochondrial dysfunction, oxidative stress, and the presence of Lewy body inclusions enriched with aggregated forms of alpha-synuclein, a presynaptic protein. Although alpha-synuclein is modified at various sites in Lewy bodies, it is unclear how sequence-specific posttranslational modifications modulate the aggregation of the protein in oxidatively stressed neurons. To begin to address this problem, we developed an affinity pull-down/mass spectrometry method to characterize the primary structure of histidine-tagged alpha-synuclein isolated from catecholaminergic neurons. Using this method, we mapped posttranslational modifications of alpha-synuclein from untreated neurons and neurons exposed to rotenone, an inhibitor of mitochondrial complex I. Various posttranslational modifications suggestive of oxidative damage or repair were identified in a region comprising a 20-residue stretch in the C-terminal part of the protein. The results indicate that alpha-synuclein is subject to discrete posttranslational modifications in neurons with impaired mitochondrial function. Our affinity pull-down/mass spectrometry method is a useful tool to examine how specific modifications of alpha-synuclein contribute to neurologic disorders such as Parkinson's disease." @default.
• W1989855060 created "2016-06-24" @default.
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• W1989855060 date "2006-02-22" @default.
• W1989855060 modified "2023-09-26" @default.
• W1989855060 title "Identification of Rotenone-Induced Modifications in α-Synuclein Using Affinity Pull-Down and Tandem Mass Spectrometry" @default.
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• W1989855060 doi "https://doi.org/10.1021/ac051978n" @default.
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• W1989855060 hasPublicationYear "2006" @default.
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