Dupont-Wallois L, Sautière P E, Cocquerelle C, Bailleul B, Delacourte A, Caillet-Boudin M L
INSERM U156, Laboratoire de Neurosciences, Lille, France.
FEBS Lett. 1995 Jan 3;357(2):197-201. doi: 10.1016/0014-5793(94)01361-4.
Tau proteins are abnormally phosphorylated in Alzheimer's disease. Pathological Tau proteins named PHF-Tau 55, PHF-Tau 64, and PHF-Tau 69, are the main constituents of the paired helical filaments (PHF). When treating SKNSH-SY 5Y cells with okadaic acid (OA), Tau 55 protein was clearly induced whereas Tau 64 protein was only faintly induced. Here, we show that the absence of Tau 69 could be explained by the fact that adult isoforms containing N-terminal inserts are not detected. Phosphorylation is similar for untreated cellular Tau proteins and fetal Tau proteins, while OA cell treatment transformed fetal-type into Alzheimer-type phosphorylated proteins.
在阿尔茨海默病中，tau蛋白会发生异常磷酸化。病理性tau蛋白，即PHF-Tau 55、PHF-Tau 64和PHF-Tau 69，是双螺旋丝（PHF）的主要成分。用冈田酸（OA）处理SKNSH-SY 5Y细胞时，Tau 55蛋白明显被诱导，而Tau 64蛋白仅被微弱诱导。在此，我们表明Tau 69缺失的原因可能是未检测到含有N端插入片段的成人异构体。未处理的细胞tau蛋白和胎儿tau蛋白的磷酸化情况相似，而OA细胞处理可将胎儿型磷酸化蛋白转变为阿尔茨海默病型磷酸化蛋白。
