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• W1583390147 abstract "Mitochondrial dysfunction involving electron transport components is implicated in the pathogenesis of several neurodegenerative disorders and is a critical event in excitotoxicity. Excitatory amino acidl-β-<i>N</i>-oxalylamino-l-alanine (l-BOAA), causes progressive corticospinal neurodegeneration in humans. In mice, l-BOAA triggers glutathione loss and protein thiol oxidation that disrupts mitochondrial complex I selectively in motor cortex and lumbosacral cord, the regions affected in humans. We examined the factors regulating postinjury recovery of complex I in CNS regions after a single dose of l-BOAA. The expression of thioltransferase (glutaredoxin), a protein disulfide oxidoreductase regulated through AP1 transcription factor was upregulated within 30 min ofl-BOAA administration, providing the first evidence for functional regulation of thioltransferase during restoration of mitochondrial function. Regeneration of complex I activity in motor cortex was concurrent with increase in thioltransferase protein and activity, 1 hr after the excitotoxic insult. Pretreatment with α-lipoic acid, a thiol delivery agent that protects motor neurons from l-BOAA-mediated toxicity prevented the upregulation of thioltransferase and AP1 activation, presumably by maintaining thiol homeostasis. Downregulation of thioltransferase using antisense oligonucleotides prevented the recovery of complex I in motor cortex and exacerbated the mitochondrial dysfunction in lumbosacral cord, providing support for the critical role for thioltransferase in maintenance of mitochondrial function in the CNS." @default.
• W1583390147 created "2016-06-24" @default.
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• W1583390147 date "2002-10-01" @default.
• W1583390147 modified "2023-10-17" @default.
• W1583390147 title "Thioltransferase (Glutaredoxin) Mediates Recovery of Motor Neurons from Excitotoxic Mitochondrial Injury" @default.
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• W1583390147 doi "https://doi.org/10.1523/jneurosci.22-19-08402.2002" @default.
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