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- W2023279699 abstract "Oxidative stress, protein misfolding, protein complex formation, and detergent insolubility are biochemical features of Alzheimer's disease (AD). We tested the cause-and-effect relationships among these using MC65 human neuroblastoma cells that exhibit toxicity upon conditional expression of carboxy-terminal fragments (CTFs) of the human amyloid precursor protein (APP). Treatments with three different antioxidants (alpha-tocopherol, N-acetyl cysteine, and alpha-lipoic acid) or three different compounds (glycerol, trimethylamine-N-oxide, and 4-phenylbutyric acid) that have been described to have a chemical chaperone function in promoting protein folding all had a protective effect on MC65 cells and decreased markers of oxidative damage and accumulation of high molecular weight amyloid (A) beta-immunoreactive (IR) species. However, chaperones partially reduced detergent insolubility of the remaining Abeta-IR species, while antioxidants did not. These results suggest that protein misfolding associated with overexpression of APP CTFs promotes oxidative stress and cytotoxicity and contributes to formation of detergent-insoluble species that appear unrelated to cytotoxicity." @default.
- W2023279699 created "2016-06-24" @default.
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- W2023279699 date "2007-02-01" @default.
- W2023279699 modified "2023-09-26" @default.
- W2023279699 title "Effects of chemical chaperones on oxidative stress and detergent-insoluble species formation following conditional expression of amyloid precursor protein carboxy-terminal fragment" @default.
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- W2023279699 doi "https://doi.org/10.1016/j.nbd.2006.10.003" @default.
- W2023279699 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17141508" @default.
- W2023279699 hasPublicationYear "2007" @default.
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