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• W2158204493 abstract "Alzheimer's disease (AD) is a disorder of two pathologies: amyloid plaques, the core of which is a peptide derived from the amyloid precursor protein (APP), and neurofibrillary tangles composed of highly phosphorylated tau. Protein kinase C (PKC) is known to increase non-amyloidogenic alpha-secretase cleavage of APP, producing secreted APP (sAPPalpha), and glycogen synthase kinase (GSK)-3beta is known to increase tau phosphorylation. Both PKC and GSK-3beta are components of the wnt signaling cascade. Here we demonstrate that overexpression of another member of this pathway, dishevelled (dvl-1), increases sAPPalpha production. The dishevelled action on APP is mediated via both c-jun terminal kinase (JNK) and protein kinase C (PKC)/mitogen-activated protein (MAP) kinase but not via p38 MAP kinase. These data position dvl-1 upstream of both PKC and JNK, thereby explaining the previously observed dual signaling action of dvl-1. Furthermore, we show that human dvl-1 and wnt-1 also reduce the phosphorylation of tau by GSK-3beta. Therefore, both APP metabolism and tau phosphorylation are potentially linked through wnt signaling." @default.
• W2158204493 created "2016-06-24" @default.
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• W2158204493 date "2001-07-15" @default.
• W2158204493 modified "2023-10-02" @default.
• W2158204493 title "Dishevelled Regulates the Metabolism of Amyloid Precursor Protein via Protein Kinase C/Mitogen-Activated Protein Kinase and c-Jun Terminal Kinase" @default.
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• W2158204493 doi "https://doi.org/10.1523/jneurosci.21-14-04987.2001" @default.
• W2158204493 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6762860" @default.
• W2158204493 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11438574" @default.

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