Sautière P E, Caillet-Boudin M L, Wattez A, Buée-Scherrer V, Delacourte A
INSERM U156, Laboratoire de Neurosciences, Lille, France.
C R Acad Sci III. 1993;316(5):533-5.
In Alzheimer's disease, Tau proteins are abnormally phosphorylated. In this paper, we describe a cellular model producing such pathological Tau proteins. After differentiation by NGF and treatment with okadaic acid (an inhibitor of phosphatases 1 and 2 A), neuroblastoma SKNSH-SY 5Y cells produced Tau proteins with an increased apparent molecular weight and a more acidic isoelectric point when compared to Tau proteins from control cells. These modified tau proteins bore Alzheimer-type epitopes detectable by antibodies specific to phosphorylated Alzheimer epitopes. This model is the first step toward a pharmacological approach of neuroprotection.
在阿尔茨海默病中， Tau 蛋白会发生异常磷酸化。在本文中，我们描述了一种产生此类病理性 Tau 蛋白的细胞模型。经神经生长因子分化并用冈田酸（一种蛋白磷酸酶 1 和 2A 的抑制剂）处理后，与对照细胞的 Tau 蛋白相比，神经母细胞瘤 SKNSH-SY 5Y 细胞产生的 Tau 蛋白表观分子量增加，等电点更偏酸性。这些修饰后的 Tau 蛋白带有可被磷酸化阿尔茨海默病表位特异性抗体检测到的阿尔茨海默病型表位。该模型是神经保护药理学方法的第一步。
