Abe K, Saito H
Department of Chemical Pharmacology, Faculty of Pharmaceutical Sciences, The University of Tokyo, 113-0033, Tokyo, Japan.
Neurosci Lett. 2000 Sep 29;292(1):1-4. doi: 10.1016/s0304-3940(00)01415-4.
It has recently been reported that Alzheimer's disease amyloid beta protein (Abeta) activates the mitogen-activated protein kinase (MAPK) cascade in certain types of cells. In the present study, we investigated whether this signal transduction cascade is involved in Abeta neurotoxicity by using cultured rat hippocampal and cortical neurons. Exposure of the cells to Abeta (1-20microM) resulted in a progressive cell death with no change in phosphorylation of p44/42 MAPK (ERK1/2). Furthermore, Abeta-induced neuronal death was not at all affected by U0126 and PD98059, inhibitors of the MAPK-activating enzyme MEK. These results suggest that the MEK/ERK signal transduction cascade is not crucial for Abeta neurotoxicity.
最近有报道称，阿尔茨海默病β淀粉样蛋白（Aβ）在某些类型的细胞中激活丝裂原活化蛋白激酶（MAPK）级联反应。在本研究中，我们通过使用培养的大鼠海马和皮质神经元来研究这种信号转导级联反应是否参与Aβ神经毒性。将细胞暴露于Aβ（1-20微摩尔）导致细胞逐渐死亡，而p44/42 MAPK（ERK1/2）的磷酸化没有变化。此外，Aβ诱导的神经元死亡完全不受MAPK激活酶MEK的抑制剂U0126和PD98059的影响。这些结果表明，MEK/ERK信号转导级联反应对于Aβ神经毒性并不关键。
