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- W1145544071 abstract "Aims: To examine the role of the enzyme methionine sulfoxide reductase A-1 (MSRA-1) in amyloid-β peptide (Aβ)-peptide aggregation and toxicity in vivo, using a Caenorhabditis elegans model of the human amyloidogenic disease inclusion body myositis. Results: MSRA-1 specifically reduces oxidized methionines in proteins. Therefore, a deletion of the msra-1 gene was introduced into transgenic C. elegans worms that express the Aβ-peptide in muscle cells to prevent the reduction of oxidized methionines in proteins. In a constitutive transgenic Aβ strain that lacks MSRA-1, the number of amyloid aggregates decreases while the number of oligomeric Aβ species increases. These results correlate with enhanced synaptic dysfunction and mislocalization of the nicotinic acetylcholine receptor ACR-16 at the neuromuscular junction (NMJ). Innovation: This approach aims at modulating the oxidation of Aβ in vivo indirectly by dismantling the methionine sulfoxide repair system. The evidence presented here shows that the absence of MSRA-1 influences Aβ aggregation and aggravates locomotor behavior and NMJ dysfunction. The results suggest that therapies which boost the activity of the Msr system could have a beneficial effect in managing amyloidogenic pathologies. Conclusion: The absence of MSRA-1 modulates Aβ-peptide aggregation and increments its deleterious effects in vivo. Antioxid. Redox Signal. 22, 48–62." @default.
- W1145544071 created "2016-06-24" @default.
- W1145544071 creator A5002325739 @default.
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- W1145544071 creator A5091641475 @default.
- W1145544071 date "2015-01-01" @default.
- W1145544071 modified "2023-09-25" @default.
- W1145544071 title "The Protein Oxidation Repair Enzyme Methionine Sulfoxide Reductase A Modulates Aβ Aggregation and Toxicity <i>In Vivo</i>" @default.
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- W1145544071 doi "https://doi.org/10.1089/ars.2013.5803" @default.
- W1145544071 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4270145" @default.
- W1145544071 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24988428" @default.
- W1145544071 hasPublicationYear "2015" @default.
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