IN-SITU DEPHOSPHORYLATION OF TAU BY PROTEIN PHOSPHATASE-2A AND PHOSPHATASE-2B IN FETAL-RAT PRIMARY CULTURED NEURONS

被引：49
|
作者：
SAITO, T
ISHIGURO, K
UCHIDA, T
MIYAMOTO, E
KISHIMOTO, T
HISANAGA, S
机构：
[1] MITSUBISHI KASEI INST LIFE SCI,MACHIDA,TOKYO 194,JAPAN
[2] KUMAMOTO UNIV,SCH MED,DEPT PHARMACOL,KUMAMOTO 860,JAPAN
来源：
FEBS LETTERS | 1995年 / 376卷 / 03期
关键词：
PROTEIN PHOSPHATASE; TAU; MICROTUBULE-ASSOCIATED PROTEIN; PRIMARY CULTURED NEURON; CDK5;
D O I：
10.1016/0014-5793(95)01292-0
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Using antibodies recognizing the phosphorylation state of specific sites, phosphorylation states of tau were monitored in fetal rat primary cultured neurons. When cultured neurons were treated with okadaic acid (OA) or calyculin A (CalA) at concentrations sufficient to inhibit protein phosphatase 2A (PP2A), phosphorylation of Ser-199/Ser-202 (numbered according to the human tau 441) and Ser-235 increased. On the other hand, treatment with Ca2+ ionophore, A23187, induced dephosphorylation of Ser-199/Ser-202, Thr-205, Ser-396 and Ser-404, and this dephosphorylation was repressed by inhibitors of protein phosphatase 2B (PP2B), cyclosporin A and FK506. These results indicate that PP2A and PP2B are differentially involved in dephosphorylation of tau in neurons.
引用
收藏
页码：238 / 242
页数：5
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