Abstract
Accumulating pieces of evidence showed that α-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.
Highlights
Heat stress is defined as external factors acting on an animal to induce a body temperature increase that arouses a series of physiological responses (Dikmen and Hansen, 2009; Te Pas et al, 2019)
The results showed that ENO1 messenger RNA (mRNA) levels increased compared with the control group and reached the highest levels with treatment for 24 h (Figure 1B)
The ENO1 protein level presented the same trend with its mRNA level along with heat stress time changing (Figure 1C)
Summary
Heat stress is defined as external factors acting on an animal to induce a body temperature increase that arouses a series of physiological responses (Dikmen and Hansen, 2009; Te Pas et al, 2019). It is one of the most common and inevitable etiological phenomena in livestock and poultry breeds. Another study demonstrated that ENO1 interacts with constitutive 70-kDa heat shock protein (HSP70) and protects against oxidative stress in rat cardiomyocytes via enhancing glycolysis pathway and energy metabolism levels (Luo et al, 2011). We found that ENO1 and HSP70 showed a collaborative expression trend using proteomics analysis (Zeng et al, 2017)
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