微管相关蛋白τ的异常磷酸化是阿尔茨海默病（ Ａ Ｄ） 神经原纤维退变的重要机制之一． 研究发现： 酪蛋白激酶１ （ Ｃ Ｋ１） ，ｃ Ａ Ｍ Ｐ 依赖性蛋白激酶（ Ｐ Ｋ Ａ） 和糖原合成酶激酶３ （ Ｇ Ｓ Ｋ３） 均可不同程度催化重组τ蛋白发生磷酸化， 从而不同程度抑制τ蛋白促微管组装的生物学功能． 如果先将τ蛋白与 Ｐ Ｋ Ａ 预温２ ｈ 后再和 Ｇ Ｓ Ｋ３温育， 则发现τ蛋白磷酸化程度比单纯用 Ｇ Ｓ Ｋ３ 处理显著增高， 生物学活性则显著降低， 电镜检测几乎看不见微管形成． 结果提示： Ｐ Ｋ Ａ 和 Ｇ Ｓ Ｋ３ 在τ蛋白的 Ａ Ｄ 样磷酸化及其功能抑制中具有正性协同作用 Aberrant phosphorylation of microtubule-associated protein τ is one of the important mechanisms of degeneration of Alzheimer’s disease (AD). The results showed that: Casein kinase 1 (C K-1), c A M P-dependent protein kinase (P K A) and glycogen synthase kinase-3 (G S K-3) Phosphorylation of protein occurs, which inhibits the biological function of tau protein-induced microtubule assembly to varying degrees. If tau protein and P K A pretreatment 2 h and then incubated with G S K  3, tau protein phosphorylation was found to be significantly higher than the treatment with G S K  3, biological activity was significantly reduced, Electron microscopy almost invisible microtubule formation. The results suggest that P K A and G S K3 have a positive synergistic effect on A D-like phosphorylation of tau protein and its function inhibition