Goedert M, Jakes R, Vanmechelen E
MRC Laboratory of Molecular Biology, Cambridge, UK.
Neurosci Lett. 1995 Apr 21;189(3):167-9. doi: 10.1016/0304-3940(95)11484-e.
Hyperphosphorylated microtubule-associated protein tau is the major component of the paired helical filament of Alzheimer's disease. Phosphorylation-dependent anti-tau antibodies are being used to identify specific amino acids that are phosphorylated in tau from normal brain and Alzheimer's disease brain. As such, monoclonal antibody AT8 is widely used. By a combination of site-directed mutagenesis of recombinant tau and in vitro phosphorylation, we show that AT8 requires tau protein to be phosphorylated at both serine 202 and threonine 205 (using the numbering of the longest human brain tau isoform.
过度磷酸化的微管相关蛋白tau是阿尔茨海默病双螺旋丝的主要成分。依赖磷酸化的抗tau抗体正被用于鉴定正常脑和阿尔茨海默病脑中tau蛋白发生磷酸化的特定氨基酸。因此，单克隆抗体AT8被广泛使用。通过重组tau的定点诱变和体外磷酸化相结合，我们发现AT8要求tau蛋白在丝氨酸202和苏氨酸205位点均发生磷酸化（使用最长的人类脑tau异构体的编号）。
