论文部分内容阅读
蛋白磷酸酯酶（PP）－2A和一1的缺陷参与Alzheimer病（AD）微管相关蛋白tau的异常磷酸化，继而导致神经细胞退化死亡。本研究采用不同剂量PP－2A和PP－1的抑制剂Okadaicacid（以下简称OA）与成神经瘤细胞株（SH－SYSY）共培养，实验结果显示：OA导致细胞代谢明显降低，突起消失，微管受损，死亡加速。OA的上述细胞毒性在PP－2A和PP－1均被抑制时显著增强。该研究进一步为PP－2A和PP－1与神经细胞活性的关系提供了实验依据，也为建立AD蛋自磷酸酯酶缺陷实验模型奠定了基础。
Defects in protein phosphatases (PP) -2A and -I are involved in the aberrant phosphorylation of the microtubule associated protein tau in Alzheimer’s disease (AD), which in turn leads to the degeneration of nerve cells. In this study, co-cultured Oknaicacid (hereinafter referred to as OA) and neuroblastoma cell line (SH-SYSY) with different doses of PP-2A and PP-1, the results showed that: OA caused cell metabolism was significantly reduced, Damaged tubes, accelerated death. The above cytotoxicity of OA was significantly enhanced when both PP-2A and PP-1 were inhibited. This study further provides the experimental evidence for the relationship between PP-2A and PP-1 and the activity of nerve cells, and lays the foundation for the establishment of an experimental model of AD egg phosphatase deficiency.