Postmortem changes in the phosphorylation state of tau-protein in the rat brain
Postmortem changes in the phosphorylation state of tau-protein in the rat brain
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DOI：
10.1016/s0197-4580(98)00094-3
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发表时间：
1998-11-01
影响因子：
4.2
通讯作者：
Arendt, T
中科院分区：
文献类型：
--
作者：
Gärtner, U;Janke, C;Arendt, T
tau蛋白的磷酸化状态对神经元微管结构的调节至关重要。关于tau蛋白的功能性结论需要准确评估磷酸化位点。因此，在不同的固定和制备条件下，在大鼠脑中的tau蛋白的一些磷酸化表位的体内分布和死后保存进行了研究。与磷酸化独立的抗血清的TAN-蛋白的检测发现轴突和体树突：本地化，这是不受影响的死后间隔30分钟。12 E8，AT 8，和PHF-1的磷酸化抗原决定簇识别主要定位在体树突室。AT 8和PHF-1的结合位点在死后迅速去磷酸化，而Tau-1表位在体树突区域被暴露。位于轴突的磷酸化表位的AT 270和核表位的AT 100死后间隔30分钟后仍然可检测到。死后去磷酸化和抑制这一进程的PP 1和/或PP 2A进一步证明了蛋白质印迹。总之，tau蛋白的快速处理对于正确评估磷酸化异构体的研究至关重要。(C)1999 Elsevier Science Inc.
The phosphorylation state of tau-protein is crucial for the regulation of neuronal microtubule organization. Functional conclusions on tau-protein require an accurate assessment of phosphorylated sites. Therefore, the in vivo distribution and postmortem preservation of some phospho-epitopes on tau-protein were examined in the rat brain under different fixation and preparation conditions. Detection of tan-protein with a phosphorylation-independent antiserum revealed both axonal and somatodendritic: localizations, which were not influenced by a postmortem interval of 30 min. The phospho-epitopes recognized by 12E8, AT8, and PHF-1 were mainly localized in the somatodendritic compartment. The binding sites of AT8 and PHF-1 were rapidly dephosphorylated postmortem, whereas the Tau-l epitope was unmasked in the somatodendritic region. The axonally located phospho-epitope of AT270 and the nuclear epitope of AT100 were still detectable after a postmortem interval of 30 min. Postmortem dephosphorylation and inhibition of this process by PP1 and/or PP2A was further demonstrated on Western blot. In conclusion, rapid processing of tau-protein is essential for the correct assessment of investigations on phospho-isoforms. (C) 1999 Elsevier Science Inc.