Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells
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 H...
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ftpubmed:oai:pubmedcentral.nih.gov:7736437 2023-05-15T18:15:49+02:00 Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells Yang, Shuangshuang Zhao, Tingting Ma, Aijun Huang, Zhihui Yang, Jingkun Yuan, Chenhao Guo, Xiaoli Zhu, Chunyue 2020-10-06 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7736437/ http://www.ncbi.nlm.nih.gov/pubmed/33025381 https://doi.org/10.1007/s12192-020-01166-1 en eng Springer Netherlands http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7736437/ http://www.ncbi.nlm.nih.gov/pubmed/33025381 http://dx.doi.org/10.1007/s12192-020-01166-1 © Cell Stress Society International 2020 Cell Stress Chaperones Original Paper Text 2020 ftpubmed https://doi.org/10.1007/s12192-020-01166-1 2021-07-04T00:29:13Z 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s12192-020-01166-1) contains supplementary material, which is available to authorized users. Text Scophthalmus maximus Turbot PubMed Central (PMC) Cell Stress and Chaperones 26 1 173 185 |
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Original Paper |
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Original Paper Yang, Shuangshuang Zhao, Tingting Ma, Aijun Huang, Zhihui Yang, Jingkun Yuan, Chenhao Guo, Xiaoli Zhu, Chunyue Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells |
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Original Paper |
description |
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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s12192-020-01166-1) contains supplementary material, which is available to authorized users. |
format |
Text |
author |
Yang, Shuangshuang Zhao, Tingting Ma, Aijun Huang, Zhihui Yang, Jingkun Yuan, Chenhao Guo, Xiaoli Zhu, Chunyue |
author_facet |
Yang, Shuangshuang Zhao, Tingting Ma, Aijun Huang, Zhihui Yang, Jingkun Yuan, Chenhao Guo, Xiaoli Zhu, Chunyue |
author_sort |
Yang, Shuangshuang |
title |
Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells |
title_short |
Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells |
title_full |
Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells |
title_fullStr |
Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells |
title_full_unstemmed |
Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells |
title_sort |
heat stress-induced hsp90 expression is dependent on erk and hsf1 activation in turbot (scophthalmus maximus) kidney cells |
publisher |
Springer Netherlands |
publishDate |
2020 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7736437/ http://www.ncbi.nlm.nih.gov/pubmed/33025381 https://doi.org/10.1007/s12192-020-01166-1 |
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Scophthalmus maximus Turbot |
genre_facet |
Scophthalmus maximus Turbot |
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Cell Stress Chaperones |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7736437/ http://www.ncbi.nlm.nih.gov/pubmed/33025381 http://dx.doi.org/10.1007/s12192-020-01166-1 |
op_rights |
© Cell Stress Society International 2020 |
op_doi |
https://doi.org/10.1007/s12192-020-01166-1 |
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Cell Stress and Chaperones |
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