Mitogen-activated protein kinases (MAPKs) and heat shock proteins (HSPs) are ubiquitous proteins that are functional mediators in both normal and stressed states of the cell. In this study, we performed heat stress (37 °C) experiments on turbot kidney (TK) cells. Heat stress expression patterns of HSP90, as well as the expression and phosphorylation levels of extracellular-regulated signal kinases (ERKs) and the transcription factor HSF1 and c-Fos, were examined. The results show that heat stress activates ERK1/2 and HSF1, and induces HSP90 gene expression in TK cells. Inhibition of ERK activation attenuates heat stress-induced HSP90 gene expression. The double luciferase reporter gene experiment showed that HSF1 is an important transcription factor for heat-induced HSP90 gene expression. Likewise, c-Fos does not directly regulate the heat-induced expression of HSP90 in turbot kidney cells. To our knowledge, this is the first study to report a signaling pathway that regulates the heat shock response in turbot cells. Our results may facilitate an understanding of the underlying molecular mechanisms of the cellular stress response in marine fish.

丝裂原活化蛋白激酶 (MAPK) 和热休克蛋白 (HSP) 是普遍存在的蛋白质，它们是细胞正常和应激状态下的功能介质。在这项研究中，我们对大菱鲆肾 (TK) 细胞进行了热应激 (37 °C) 实验。检查了HSP90 的热应激表达模式，以及细胞外调节信号激酶 (ERK) 和转录因子HSF1和c-Fos的表达和磷酸化水平。结果表明，热应激激活 ERK1/2 和 HSF1，并诱导TK 细胞中的HSP90基因表达。抑制 ERK 激活减弱热应激诱导的HSP90基因表达。双荧光素酶报告基因实验表明HSF1是热诱导HSP90基因表达的重要转录因子。同样，c-Fos 不直接调节热诱导的菱鲆肾细胞中HSP90 的表达。据我们所知，这是第一项报告调节大菱鲆细胞热休克反应的信号通路的研究。我们的结果可能有助于理解海洋鱼类细胞应激反应的潜在分子机制。