Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot ( Scophthalmus maximus ) kidney c
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ORIGINAL PAPER
Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells Shuangshuang Yang 1,2 & Tingting Zhao 1,3 & Aijun Ma 1 & Zhihui Huang 1 & Jingkun Yang 1 & Chenhao Yuan 1 & Xiaoli Guo 1,3 & Chunyue Zhu 1,3 Received: 4 June 2020 / Revised: 15 September 2020 / Accepted: 16 September 2020 # Cell Stress Society International 2020
Abstract 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. Keywords HSP90 . HSF1 . c-Fos . Heat shock response . Scophthalmus maximus
Introduction Cellular stress response is a reaction to changes or fluctuations of extracellular conditions that damage the structure and function of macromolecules (Poljšak and Milisav 2012). This response entails the rapid synthesis of specific proteins involved in mitigating damage caused by various stressors, including elevated temperatures. Studies in both yeast and human systems show that stress can induce a novel protein-protein interaction network (Palotai Electronic supplementary material The online version of this article (https://doi.org/10.1007/s12192-020-01166-1) contains supplementary material, which is available to authorized users. * Aijun Ma [email protected] 1
Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, No.106 Nanjing Road, Qingdao 266071, China
2
Shandong Qilu Cell Therapy Engineering Technology Co., Ltd, Jinan 250000, China
3
College of Fisheries and Life Science, Shanghai Ocean University, Shanghai 201306, China
et al. 2008). Research on many species of fish and aquatic invertebrates has demonstrated that during a diverse array of stressesinduced HSP classes, the major molecular chaperones show significant changes at the mRNA and protein levels (Xie et al. 2015; Zhao et al. 2011). Four major HSP families of proteins, frequently referred to as HSP90, HSP70, HSP60, and the low molecular weight (LMW) HSPs, have been identified in many experi
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