Alpha-Enolase Protects Hepatocyte Against Heat Stress Through Focal Adhesion Kinase-Mediated Phosphatidylinositol 3-Kinase/Akt Pathway
文献类型： 外文期刊
作者： Zeng, Tao 1 ; Cao, Yongqing 1 ; Gu, Tiantian 1 ; Chen, Li 1 ; Tian, Yong 1 ; Li, Guoqin 1 ; Shen, Junda 1 ; Tao, Zhenrong 1 ;
作者机构： 1.Zhejiang Acad Agr Sci, Inst Anim Husb & Vet Med, Hangzhou, Peoples R China
2.Minist Agr China, Key Lab Informat Traceabil Agr Prod, Hangzhou, Peoples R China
3.Yangzhou Univ, Jiangsu Key Lab Anim Genet Breeding & Mol Design, Yangzhou, Jiangsu, Peoples R China
关键词： ENO1; Hsp70; glycolysis; cell viability; FAK-PI3K/AKT
期刊名称：FRONTIERS IN GENETICS （ 影响因子：4.599； 五年影响因子：4.888 ）
ISSN：
年卷期： 2021 年 12 卷
页码：
收录情况： SCI
摘要： Accumulating pieces of evidence showed that alpha-enolase (ENO1) is a multifunctional protein that plays a crucial role in a variety of pathophysiological processes. In our previous study, differential expression of ENO1 was observed in different heat-tolerance duck breeds. Here, we examined in vitro expression level of ENO1 in hepatocytes against heat stress. The mechanisms of ENO1 on cell glycolysis, growth, and its potential regulatory pathways were also analyzed. The results showed that ENO1 expression in messenger RNA and protein levels were both greatly increased in heat-treated cells compared with non-treated cells. ENO1-overexpressed cells significantly elevated cell viability and glycolysis levels. It was further shown that stably upregulated ENO1 activated focal adhesion kinase-phosphatidylinositol 3-kinase/Akt and its downstream signals. In addition, the interaction between ENO1 and 70-kDa heat shock protein was detected using co-immunoprecipitation. Our research suggests that ENO1 may interact with 70-kDa heat shock protein to protect hepatocyte against heat stress through focal adhesion kinase-mediated phosphatidylinositol 3-kinase/Akt pathway.
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