The cytoplasmic domain of Alzheimer's amyloid precursor protein is phosphorylated at Thr654, Ser655, and Thr668 in adult rat brain and cultured cells.

摘要: BACKGROUND: The cytoplasmic domain of the Alzheimer's disease amyloid precursor protein (APP) is phosphorylated in vitro at Thr654 and Ser655, both intact cells Thr668 (numbering for APP695 isoform). MATERIALS AND METHODS: We have developed phosphorylation state-specific antibodies to each sites, we used these analyze APP adult rat brain cultured cell lines. RESULTS: demonstrate that all three sites are brain. Phosphorylation Thr654, was also observed several In PC12 cells, Ser655 increased more than 10-fold by treatment with okadaic acid, a specific inhibitor phosphatases 1 2A, but not affected activators kinase C. HeLa regulated cycle-dependent manner near-stoichiometric being G2/M phase cycle. general, found be highest mature isoforms, whereas immature isoforms cells. CONCLUSIONS: results occurs under physiological conditions. further characterization using phosphorylation-specific may help elucidation biological function APP.