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- W3008609042 abstract "Alzheimer's disease (AD) is a progressive neurodegenerative disorder associated with synaptic dysfunction, pathological accumulation of β-amyloid peptide 1-42 (Aβ1-42 ), and neuronal loss. The self-association of Aβ1-42 monomers (Aβ-M) into soluble oligomers seems to be crucial for the development of neurotoxicity. Previous publications have shown that Aβ oligomers and dimers might play key roles in inducing AD. The role of Aβ-M was rarely investigated and still unclear in AD. To understand the effects of Aβ-M on neurons and other cell types in the brain could be the key to understand its function. In our study, we found that Aβ-M expression slowly induced cell apoptosis within 48 hours after transfection, β2 adrenergic receptor (β2AR) interacted with Aβ-M in the pull-down and the yeast two-hybrid assays, and Aβ-M played a major role in inducing phosphorylation of Tau at Ser-214, c-Jun N-terminal kinase (JNK) at Thr-183/Tyr-185, p70 ribosomal protein S6 kinase (p70S6K) at Thr-389. We also discovered that β2AR, G protein-coupled receptor kinase 2 (GRK2), and protein kinase A (PKA) mediated the phosphorylation of Tau and JNK. Aβ-M induced phosphorylation of Tau at Ser-214 through both β2AR-cAMP/PKA-JNK and β2AR-GRK signaling pathways. Mitogen-activated protein kinase kinase (MEK) mediated the phosphorylation of p70S6K induced by Aβ-M." @default.
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- W3008609042 date "2020-02-17" @default.
- W3008609042 modified "2023-10-17" @default.
- W3008609042 title "Aβ monomer induces phosphorylation of Tau at Ser‐214 through β2AR‐PKA‐JNK signaling pathway" @default.
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- W3008609042 doi "https://doi.org/10.1096/fj.201902230rr" @default.
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