Caillet-Boudin M L, Delacourte A
INSERM U 422, Lille, France.
Neuroreport. 1996 Dec 20;8(1):307-10. doi: 10.1097/00001756-199612200-00061.
Hyperphosphorylation of the microtubule-associated tau proteins is one of the main pathological events that leads to neurofibrillary neurodegeneration in Alzheimer's disease. A similar tau phosphorylation pattern may be obtained in SY-5Y neuroblastoma cells after okadaic acid treatment. In this paper, we clearly demonstrate phosphorylation of Ser422 in tau proteins of treated cells as well as in Alzheimer brain homogenates. By contrast, Ser422 was not phosphorylated on native tau proteins from non-treated cells or rapidly processed biopsies. These results confirm that this cell model is still relevant to study neurofibrillary neurodegeneration of the Alzheimer type.
微管相关tau蛋白的过度磷酸化是导致阿尔茨海默病神经原纤维变性的主要病理事件之一。用冈田酸处理SY-5Y神经母细胞瘤细胞后，可能会获得类似的tau磷酸化模式。在本文中，我们清楚地证明了处理过的细胞以及阿尔茨海默病脑匀浆中tau蛋白的Ser422位点发生了磷酸化。相比之下，未处理细胞或快速处理的活检组织中的天然tau蛋白上的Ser422没有发生磷酸化。这些结果证实，该细胞模型在研究阿尔茨海默型神经原纤维变性方面仍然具有相关性。
