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P4–031: The effect of okadaic acid–induced tau hyperphosphorylation on Pin1 expression in primary cortical neurons
Author(s) -
Metin Derya,
GezenAk Duygu,
Dursun Erdinc,
Atasoy Irem Lutfiye,
Yilmazer Selma,
Ozturk Melek
Publication year - 2013
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2013.05.1419
Subject(s) - okadaic acid , pin1 , hyperphosphorylation , phosphorylation , dephosphorylation , tau protein , chemistry , peptidylprolyl isomerase , protein phosphatase 2 , phosphatase , senile plaques , tauopathy , neurodegeneration , microbiology and biotechnology , alzheimer's disease , biology , biochemistry , medicine , isomerase , enzyme , disease
phosphotase 2A (PP2A) was induced by 25nM Okadaic acid (OKA) treatment in primary cortical neuron cultures of Sprague Dawley rat embryos (E16). OKA dependent hyperphosphorylation of tau protein was determined with Western blotting using anti-tau antibodies; T231, S262, Tau-46 and Tau-1 in the 8th hours of treatment. BDNF levels were determined by ELISA in the 8 and 24 hours of treatment. Results: Our results showed that okadaic acid treatment increased the level of tau phosphorylation at T231, S262 sites and decreased the level of non phosphorylated tau. BDNF release of OKA treated cortical neurons was not different than either controls or vehicle group in the 8 hours of treatment but decreased on the 24 th hours of treatment compared to untreated control and vehicle treated groups (p<0.01, p<0.01, respectively). Conclusions: Twenty four hours of treatment in our study showed that tau hyperphosphorylation significantly decreases the BDNF release. Our results might indicate the decrease in the BDNF release in AD might depend on disrupted microtubule structure.