Ohnishi K, Matsumoto H, Takahashi A, Wang X, Ohnishi T
Department of Physiology, Nara Medical University, Japan.
Photochem Photobiol. 1996 Dec;64(6):949-52.
We demonstrated previously that human glioblastoma cell lines accumulated heat shock protein (hsp)72, not only after heat shock, but also after, gamma-ray or UV irradiation. In the present study, we investigated whether the binding activity of heat shock transcription factor (HSF) to the heat shock element (HSE) of the hsp72 gene promoter increased after UV irradiation of human glioblastoma A-172 cells. A gel mobility-shift assay showed that the activated HSF level increased markedly after UV irradiation. Furthermore, UV irradiation of nuclear extracts in vitro did not activate HSF, whereas in vitro heat shock treatment did. These results suggest that HSF activation can be induced by UV irradiation at normal physiological temperature and hsp72 accumulation results from an increased activated HSF level, i.e. a transcriptional up-regulation of hsp72. In addition, the mechanism responsible for UV-induced HSF activation may differ from the process that operates in heat-treated cells.
我们先前证明,人胶质母细胞瘤细胞系不仅在热休克后,而且在γ射线或紫外线照射后都会积累热休克蛋白(hsp)72。在本研究中,我们调查了人胶质母细胞瘤A-172细胞经紫外线照射后,热休克转录因子(HSF)与hsp72基因启动子的热休克元件(HSE)的结合活性是否增加。凝胶迁移率变动分析表明,紫外线照射后活化的HSF水平显著增加。此外,体外对核提取物进行紫外线照射不会激活HSF,而体外热休克处理则会激活。这些结果表明,在正常生理温度下,紫外线照射可诱导HSF活化,hsp72的积累是由于活化的HSF水平增加,即hsp72的转录上调所致。此外,紫外线诱导HSF活化的机制可能与热处理细胞中的机制不同。