Dephosphorylation of microtubule‐associated protein tau by protein phosphatase‐1 and ‐2C and its implication in Alzheimer disease

Damuni Zahi; Gong Cheng-Xin; Grundke-Iqbal Inge; Iqbal Khalid

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Dephosphorylation of microtubule‐associated protein tau by protein phosphatase‐1 and ‐2C and its implication in Alzheimer disease

机译：蛋白磷酸酶-1和-2C对微管相关蛋白tau的去磷酸化作用及其在阿尔茨海默病中的意义

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>Microtubule-associated protein tau is abnormally hyperphosphorylated and forms the major protein subunit of paired helical filaments (PHF) in Alzheimer disease brains. The abnormally phosphorylated sites Ser-199, Ser-202, Ser-396 and Ser-404 but not Ser-46 and Ser-235 of Alzheimer tau were found to be dephosphorylated by protein phosphatase-1 and this dephosphorylation was activated by Mn2+. In contrast, protein phosphatase-2C did not dephosphorylate any of these sites. Both protein phosphatase-1 and -2C had high activities towards [32P]tau phosphorylated by cAMPdependent protein kinase. These results suggest that both protein phosphatase-1 and -2C might be associated with normal phosphorylation state of tau, but only the former and not the latter phosphatase is involved in its abnormal phosphorylation in Alzheimer disease.

机译：>与微管相关的蛋白tau被异常地过度磷酸化，并形成阿尔茨海默病大脑中成对的螺旋丝（PHF）的主要蛋白亚基。发现Alzheimer tau的异常磷酸化位点Ser-199，Ser-202，Ser-396和Ser-404，而不是Ser-46和Ser-235被蛋白磷酸酶-1去磷酸化，并且该去磷酸化被Mn ^{2 + 。相反，蛋白磷酸酶2C不会使这些位点中的任何一个去磷酸化。磷酸酶-1和-2C对由cAMP依赖性蛋白激酶磷酸化的[ 32 P] tau具有较高的活性。这些结果表明蛋白磷酸酶-1和-2C可能与tau的正常磷酸化状态有关，但只有前者而不是后者的磷酸酶参与了阿尔茨海默病的异常磷酸化。}

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《FEBS Letters》 |1994年第1期|共页
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Damuni Zahi; Gong Cheng-Xin; Grundke-Iqbal Inge; Iqbal Khalid;
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1. 5′‐AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP‐activated protein kinase. Studies using bacterially expressed human protein phosphatase‐2Cα and native bovine protein phosphatase‐2Ac [J] . FEBS Letters . 1995,第3期

机译：5'-AMP抑制AMP激活的蛋白激酶的去磷酸化，并促进其磷酸化。使用细菌表达的人蛋白磷酸酶2Cα和天然牛蛋白磷酸酶2Ac进行研究
2. 5′‐AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP‐activated protein kinase. Studies using bacterially expressed human protein phosphatase‐2Cα and native bovine protein phosphatase‐2Ac [J] . FEBS Letters . 1995,第3期

机译：5'-AMP抑制AMP激活的蛋白激酶的去磷酸化，并促进其磷酸化。使用细菌表达的人蛋白磷酸酶2Cα和天然牛蛋白磷酸酶2Ac进行研究
3. p42 map kinase phosphorylation sites in microtubule‐associated protein tau are dephosphorylated by protein phosphatase 2A1 Implications for Alzheimer's disease [J] . Cohen E.Suzanne, Cohen Philip, Goedert Michel, FEBS Letters . 1992,第1期

机译：微管相关蛋白tau中的p42图激酶磷酸化位点被蛋白磷酸酶2A1去磷酸化对阿尔茨海默氏病的影响
4. Phosphorylation of microtubule-associated protein tau by mitogen-activated protein kinase in Alzheimer’s disease [C] . Tingting Li, Huahua Shi, Yan Zhao International Conference on Advanced Composite Materials and Manufacturing Engineering . 2018

机译：丝裂膜引起蛋白质促乳丝溶蛋白激酶在阿尔茨海默病中的磷酸化
5. Posttranslational modifications of tau protein in wildtype mice and a new model of neurofibrillary tangle formation: Implications for Alzheimer's disease. [D] . Andorfer, Cathy Ann. 2003

机译：野生型小鼠中tau蛋白的翻译后修饰和神经原纤维缠结形成的新模型：对阿尔茨海默氏病的影响。
6. Genetic background modifies neurodegeneration and neuroinflammation driven by misfolded human tau protein in rat model of tauopathy: implication for immunomodulatory approach to Alzheimers disease [O] . Zuzana Stozicka, Norbert Zilka, Petr Novak, 2010

机译：遗传背景改变了人tau蛋白错误折叠的人tau蛋白驱动的神经退行性变和神经炎症：对阿尔茨海默氏病免疫调节方法的意义
7. Dephosphorylation of microtubule-associated protein tau by protein phosphatase-1 and -2C and its implication in Alzheimer disease [O] . Gong Cheng-Xin, Grundke-Iqbal Inge, Damuni Zahi, 1994

机译：蛋白磷酸酶-1和-2C对微管相关蛋白tau的去磷酸化作用及其在阿尔茨海默病中的意义

Dephosphorylation of microtubule‐associated protein tau by protein phosphatase‐1 and ‐2C and its implication in Alzheimer disease

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