Maurage C A, Sergeant N, Ruchoux M M, Hauw J J, Delacourte A
INSERM U422, 1 Place de Verdun, 59045 Lille, France.
Neuroreport. 2001 Oct 29;12(15):3177-81. doi: 10.1097/00001756-200110290-00007.
The microtubule-associated tau proteins are abnormally aggregated in many tauopathies. Phosphorylation modulates the functions of tau. The serine 199 residue of tau is abnormally phosphorylated at early and late stages of Alzheimer's disease. The presence of the phosphorylated Ser199 was investigated in autopsy-derived and biopsy-derived brain tissue samples from non-demented individuals. A paradoxical expression was found in the hippocampus of the youngest ones, in granule cells of the dentate gyrus and in pyramidal cells of the Ammon's horn, which are particularly prone to neurodegeneration in several tauopathies. The rate of positive cells decreased with age. These data emphasize the importance of the phosphorylation of the Ser199 residue of tau in ageing and susceptibility to neurodegeneration.
微管相关的tau蛋白在许多tau蛋白病中异常聚集。磷酸化调节tau的功能。tau蛋白的丝氨酸199残基在阿尔茨海默病的早期和晚期异常磷酸化。在来自非痴呆个体的尸检和活检脑组织样本中研究了磷酸化Ser199的存在情况。在最年轻个体的海马体、齿状回颗粒细胞和海马角锥体细胞中发现了一种矛盾的表达，这些细胞在几种tau蛋白病中特别容易发生神经变性。阳性细胞率随年龄增长而降低。这些数据强调了tau蛋白丝氨酸199残基磷酸化在衰老和神经变性易感性中的重要性。
