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• W2045181512 startingPage "129" @default.
• W2045181512 abstract "Prion diseases are characterized by neuronal cell death, glial proliferation and deposition of prion peptide aggregates. An abnormal misfolded isoform of the prion protein (PrP) is considered to be responsible for this neurodegeneration. The PrP 106-126, a synthetic peptide obtained from the amyloidogenic region of the PrP, constitutes a model system to study prion-induced neurodegeneration as it retains the ability to trigger cell death in neuronal cultures. In the present study, we show that the addition of this prion peptide to cultured neurons increases the activity of glycogen synthase kinase 3 (GSK-3), which is accompanied by the enhanced phosphorylation of some microtubule-associated proteins including tau and microtubule-associated protein 2. Prion peptide-treated neurons become progressively atrophic, and die ultimately. Both lithium and insulin, which inhibit GSK-3 activity, significantly decrease prion peptide-induced cell death both in primary neuronal cultures and in neuroblastoma cells. Finally, the overexpression of a dominant-negative mutant of GSK-3 in transfected neuroblastoma cells efficiently prevents prion peptide-induced cell death. These results are consistent with the view that the activation of GSK-3 is a crucial mediator of prion peptide-induced neurodegeneration." @default.
• W2045181512 created "2016-06-24" @default.
• W2045181512 creator A5024568847 @default.
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• W2045181512 date "2003-05-15" @default.
• W2045181512 modified "2023-10-18" @default.
• W2045181512 title "Prion peptide induces neuronal cell death through a pathway involving glycogen synthase kinase 3" @default.
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• W2045181512 doi "https://doi.org/10.1042/bj20021596" @default.
• W2045181512 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1223368" @default.
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• W2045181512 hasPublicationYear "2003" @default.
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