Shiurba R A, Ishiguro K, Takahashi M, Sato K, Spooner E T, Mercken M, Yoshida R, Wheelock T R, Yanagawa H, Imahori K, Nixon R A
Laboratories for Molecular Neuroscience, McLean Hospital, Harvard Medical School, Belmont, MA 02178, USA.
Brain Res. 1996 Oct 21;737(1-2):119-32. doi: 10.1016/0006-8993(96)00717-2.
One unique phosphorylation site consistently found in paired helical filament tau, serine 413, is modified by tau protein kinase I/glycogen synthase kinase-3 beta but no other known tau kinase. Here we present immunocytochemistry from Alzheimer's disease brains showing that focal subpopulations of hippocampal CA1 pyramidal neurons and neuritic plaques are strongly reactive for tau protein kinase I/glycogen synthase kinase-3 beta and tau phosphoserine 413 in early stages of pathology. Colocalization of these epitopes suggests that tau protein kinase I/glycogen synthase kinase-3 beta abnormally phosphorylates tau and is in a position to disrupt neuronal metabolism in anatomical areas vulnerable to Alzheimer's disease.
在成对螺旋丝tau中始终发现的一个独特磷酸化位点，即丝氨酸413，可被tau蛋白激酶I/糖原合酶激酶-3β修饰，但不被其他已知的tau激酶修饰。在此，我们展示了来自阿尔茨海默病大脑的免疫细胞化学结果，表明在病理早期，海马CA1锥体神经元和神经炎性斑块的局部亚群对tau蛋白激酶I/糖原合酶激酶-3β和tau磷酸丝氨酸413有强烈反应。这些表位的共定位表明，tau蛋白激酶I/糖原合酶激酶-3β异常磷酸化tau，并可能在易患阿尔茨海默病的解剖区域破坏神经元代谢。
