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P1‐081: Tau decreases the phosphorylation of erk1/2 through recruiting and promoting the phosphatase activity of PP2A
Author(s) -
Tuo Qing-Zhang,
Sun Xu-Ying,
Liuyang Zhen-Yu,
Wang Jian-Zhi,
Liu Rong
Publication year - 2015
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.2015.06.278
Subject(s) - dephosphorylation , phosphorylation , mapk/erk pathway , protein phosphatase 2 , phosphatase , kinase , dusp6 , serine , threonine , immunoprecipitation , chemistry , microbiology and biotechnology , signal transduction , protein kinase a , biology , biochemistry , gene
latency and increased number of errors in the step down passive avoid test. We found that CNGA2 knockout induced memory deficits with activation of several memory-related protein kinases in the hippocampal extracts, including extracellular-signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and protein kinase B (AKT), reduction of synapsinI, NR2A/B, and PSD95, decreased spine numbers and mushroom-type spines. We also found that tau hyperphosphorylation at S-396, S-262, T-205, T-231 sites in the CNGA2 (-/Y) animal model. These findings indicated the AD like memory impairment and pathological changes in CNGA2 (-/Y) mice. Conclusions: Using CNGA2 (-/Y) mice as the olfactory dysfunction model, our study indicated the underlying correlation of olfactory dysfunction and AD like pathological changes.