Heat stress-inducedHSP90expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells
文献类型： 外文期刊
作者： Yang, Shuangshuang 1 ; Zhao, Tingting 1 ; Ma, Aijun 1 ; Huang, Zhihui 1 ; Yang, Jingkun 1 ; Yuan, Chenhao 1 ; Guo, Xia 1 ;
作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, 106 Nanjing Rd, Qingdao 266071, Peoples R China
2.Shandong Qilu Cell Therapy Engn Technol Co Ltd, Jinan 250000, Peoples R China
3.Shanghai Ocean Univ, Coll Fisheries & Life Sci, Shanghai 201306, Peoples R China
关键词： HSP90; HSF1; c-Fos; Heat shock response; Scophthalmus maximus
期刊名称：CELL STRESS & CHAPERONES （ 影响因子：3.667； 五年影响因子：3.717 ）
ISSN： 1355-8145
年卷期：
页码：
收录情况： SCI
摘要： 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 degrees C) experiments on turbot kidney (TK) cells. Heat stress expression patterns ofHSP90, as well as the expression and phosphorylation levels of extracellular-regulated signal kinases (ERKs) and the transcription factorHSF1andc-Fos, were examined. The results show that heat stress activates ERK1/2 and HSF1, and inducesHSP90gene expression in TK cells. Inhibition of ERK activation attenuates heat stress-inducedHSP90gene expression. The double luciferase reporter gene experiment showed that HSF1 is an important transcription factor for heat-inducedHSP90gene expression. Likewise, c-Fos does not directly regulate the heat-induced expression ofHSP90in 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.
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