Sato K, Saito H, Matsuki N
Department of Chemical Pharmacology, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Brain Res. 1996 Nov 18;740(1-2):117-23. doi: 10.1016/s0006-8993(96)00846-3.
Many kinds of injuries induce 72 kDa heat-shock protein (HSP70) in the central nervous system. We investigated the role of HSP70 in promoting the survival of rat hippocampal neurons in primary culture. Heat-shock (42 degrees C for 30 min) significantly increased the number of surviving neurons independently of the initial density of plated cells, suggesting a direct effect on the neurons. Immunohistochemical detection revealed that HSP70 was expressed in virtually all cells six hours after the heat-shock and the immunostaining became stronger during the observation period of 72 h. HSP70 immunoreactivity was localized in the nucleus at 24 h after the heat-shock, but was diffused throughout the cytoplasm at 72 h. Addition of an antisense oligonucleotide to the medium significantly suppressed the neuroprotective effect of the heat-shock to control level, while a sense oligonucleotide had no effect. HSP70 immunoreactivity was completely abolished in the presence of the antisense oligonucleotide. These results indicate that HSP70 is essential for neuroprotection by heat-shock.
多种损伤可在中枢神经系统中诱导72 kDa热休克蛋白（HSP70）的产生。我们研究了HSP70在促进原代培养的大鼠海马神经元存活中的作用。热休克（42℃，30分钟）显著增加了存活神经元的数量，且与接种细胞的初始密度无关，这表明对神经元有直接作用。免疫组织化学检测显示，热休克6小时后，几乎所有细胞中都表达了HSP70，并且在72小时的观察期内免疫染色变得更强。热休克24小时后，HSP70免疫反应性定位于细胞核，但在72小时时扩散至整个细胞质。向培养基中添加反义寡核苷酸可将热休克的神经保护作用显著抑制至对照水平，而正义寡核苷酸则无作用。在存在反义寡核苷酸的情况下，HSP70免疫反应性完全消失。这些结果表明，HSP70对于热休克的神经保护作用至关重要。
