Bruce J L, Price B D, Coleman C N, Calderwood S K
Joint Center for Radiation Therapy, Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
Cancer Res. 1993 Jan 1;53(1):12-5.
When cells are exposed to heat shock, heavy metals, amino acid analogues, and other stresses, the heat shock transcription factor (HSF) is activated. The HSF then binds to the promoter of the heat shock genes, stimulating transcription of the heat shock proteins. Here, we demonstrate that exposure of NIH-3T3 cells to oxidants (H2O2 or menadione) also causes activation of the HSF. This activation is not blocked by inhibitors of protein synthesis (cycloheximide) or by inhibitors of protein kinases (2-aminopurine or genistein). In addition, the oxidant activated HSF is located in the nucleus of the cells. However, oxidant activation of the HSF does not result in the accumulation of hsp70 mRNA or of heat shock proteins. This is in contrast to the accumulation of heat shock proteins seen after heat shock activation of the HSF. This suggests that oxidant induced activation of HSF binding may have a function different from that of heat induced activation of HSF binding.
当细胞暴露于热休克、重金属、氨基酸类似物及其他应激条件下时，热休克转录因子（HSF）会被激活。随后，HSF 与热休克基因的启动子结合，刺激热休克蛋白的转录。在此，我们证明将 NIH-3T3 细胞暴露于氧化剂（过氧化氢或甲萘醌）也会导致 HSF 的激活。这种激活不受蛋白质合成抑制剂（放线菌酮）或蛋白激酶抑制剂（2-氨基嘌呤或染料木黄酮）的阻断。此外，被氧化剂激活的 HSF 位于细胞核中。然而，HSF 的氧化剂激活并不会导致 hsp70 mRNA 或热休克蛋白的积累。这与热休克激活 HSF 后观察到的热休克蛋白积累形成对比。这表明氧化剂诱导的 HSF 结合激活可能具有与热诱导的 HSF 结合激活不同的功能。
