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• W2019489051 abstract "Abstract One of pathological hallmarks of Alzheimer's disease (AD) is neurofibrillary tangles (NFTs) consisting of abnormally hyperphosphorylated tau. The molecular mechanisms underlying the regulation of tau hyperphosphorylation remain largely unclear. The phosphoinositide 3‐kinase (PI3K)/Akt pathway has been implicated in the pathogenesis of AD, however, potential functions and role of tumor suppressor phosphatase and tensin homologue deleted on chromosome 10 (PTEN) in AD pathogenesis have not been fully explored. Here, we report that okadaic acid (OA)‐induced tau phosphorylation is accompanied by PTEN induction, knockdown of PTEN reduces the tau hyperphosphorylation by OA in SH‐SY5Y cells and increases cell proliferation and survival. The effect of PTEN suppression on tau dephosphorylation appeared to be mediated by inhibition of glycogen synthase kinase 3 while enhancing the Akt activity. Reduction of tau phosphorylation was also observed in the OA‐induced parental SH‐SY5Y cells co‐treated with bisperoxovanadate (bpv), a potent PTEN inhibitor. Our studies provide evidence for an effect of PTEN on the phosphorylation of tau in AD pathogenesis and give some insight into the mechanisms through which suppression of PTEN expression may contribute towards the amelioration of tauopathy, implying that pharmacological intervention of PTEN may be a new therapeutic approach for the treatment of AD." @default.
• W2019489051 created "2016-06-24" @default.
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• W2019489051 date "2012-08-13" @default.
• W2019489051 modified "2023-09-25" @default.
• W2019489051 title "Effects of PTEN inhibition on regulation of tau phosphorylation in an okadaic acid‐induced neurodegeneration model" @default.
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• W2019489051 doi "https://doi.org/10.1016/j.ijdevneu.2012.08.003" @default.
• W2019489051 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22906543" @default.
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