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用蛋白磷酸酯酸PP-2A、-2B和-1型分别处理的Alzheimer病（AD）异常磷酸化tau蛋白可不同程度恢复其促微管聚集和组装功能。PP－2A的恢复作用比PP－2B和PP－1更强．PP－2A，PP－2B和PP－1使异常tau蛋白水解释放磷酸的量分别为其总量的57％，36％和30％。tau蛋白Ser－235位的磷酸化不是决定其功能的关键位点，而Thr－231的磷酸化可能与微管组装早期的成核聚集作用有关。该研究证明：体内蛋白磷酸酯酶PP－2A，PP－2B和PP－1可能参与tau蛋白异常磷酸化过程，保持这些磷酸酯酶的活性有可能抑制AD神经原纤维退化．
Abnormal phosphorylation of tau in Alzheimer’s disease (AD) treated with protein phosphates PP-2A, -2B and -1 respectively restored the function of promoting microtubule assembly and assembly to varying degrees. PP-2A recovery than PP-2B and PP-1 stronger. PP-2A, PP-2B and PP-1 to the abnormal tau proteolytic release of phosphate were the amount of 57%, 36% and 30% of their total. Phosphorylation of tau at Ser-235 is not the key determinant of its function, and phosphorylation of Thr-231 may be related to early nuclear assembly of microtubule assembly. This study demonstrated that in vivo protein phosphatases PP-2A, PP-2B and PP-1 may be involved in the aberrant phosphorylation of tau and that maintaining these phosphatase activity may inhibit AD neurofibrillary degeneration.