Analysis of phosphorylation of tau with antibodies specific for phosphorylation sites
Analysis of phosphorylation of tau with antibodies specific for phosphorylation sites
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DOI：
10.1016/0304-3940(95)12206-0
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发表时间：
1995-12-29
影响因子：
2.5
通讯作者：
Imahori, K
中科院分区：
文献类型：
--
作者：
Ishiguro, K;Sato, K;Imahori, K
之前，我们通过tau蛋白激酶（TPK） I/糖原合成酶激酶3 β (GSK-3 β)和TPKII/（细胞周期蛋白依赖性激酶5 (CDK5) + p23）确定了tau蛋白磷酸化的位点。我们利用化学合成的磷酸化肽作为抗原，制备了针对TPKI和TPKII磷酸化的tau蛋白位点的特异性抗体。每个抗体特异性地与每个磷酸化位点发生反应。使用这些抗体，证实TPKI和TPKII负责这些磷酸化位点，正如之前报道的那样，除了Ser404也被TPKI单独弱磷酸化外。我们还观察到tpkii -磷酸化能增强tpki -磷酸化。这些结果表明，这些抗体是研究TPKI和TPKII磷酸化tau蛋白的有用工具。
Previously, we determined sites of tau protein phosphorylation by tau protein kinase (TPK) I/glycogen synthase kinase 3 beta (GSK-3 beta) and TPKII/(cyclin-dependent kinase 5 (CDK5) + p23). We prepared antibodies specific for these sites of tau phosphorylated by TPKI and TPKII, using chemically synthesized phosphopeptides as antigens. Each antibody specifically reacts with each phosphorylation site. With these antibodies, it was confirmed that TPKI and TPKII are responsible for these phosphorylation sites, as reported previously, except that Ser404 is also weakly phosphorylated by TPKI alone. It was also observed that TPKII-phosphorylation enhances TPKI-phosphorylation. These results indicate that these antibodies are useful tools for investigation of the phosphorylation of tau by TPKI and TPKII.