Hsp70 expression induced by Co-Enzyme Q10 protected chicken myocardial cells from damage and apoptosis under in vitro heat stress

Abstract

The aim of this study was to investigate whether induction of Hsp70 expression by co-enzyme Q10 (Q10) treatment protects chicken primary myocardial cells (CPMCs) from damage and apoptosis in response to heat stress for 5 hours. Analysis of the expression and distribution of Hsp70 and the levels of the damage-related enzymes creatine kinase-MB (CK-MB) and lactate dehydrogenase (LDH), as well as pathological analysis showed that co-enzyme Q10 alleviated the damage caused to CPMCs during heat stress. Further, analysis of cell apoptosis and the expression of cleaved caspase-3 indicated that co-enzyme Q10 did have an anti-apoptotic role during heat stress. Western blot analysis showed that pretreatment with co-enzyme Q10 led to a significant increase in the expression of Hsp70 during heat stress. Immunostaining assays confirmed the results of western blot analysis and also showed that co-enzyme Q10 could accelerate the translocation of Hsp70 into the nucleus during heat stress, but this was not observed in the group that was treated with only co-enzyme Q10. These findings seem to indicate that co-enzyme Q10 protected CPMCs from heat stress via the induction of Hsp70. To investigate this, 200 μM quercetin, an Hsp70 inhibitor, was used to inhibit the expression of Hsp70 2 h before heat stress. Quercetin pre-treatment was observed to suppress the expression of Hsp70 as well the protective function of co-enzyme Q10 at 5 h of heat stress. This finding confirms that Q10 brought about its effects via Hsp70 expression, but the mechanism underlying this needs further investigation.

The Effect of High Temperature on Viability, Proliferation, Apoptosis and Anti-oxidant Status of Chicken Embryonic Fibroblast Cells

“…Several conditions, molecules, and organelles may be involved in apoptosis and ROS may play a key role in apoptosis (Wang et al, 2008). Our finding are in agreement with previous studies reporting that heat stress induced apoptosis in chicken myocardial cells (Xu et al, 2017), human umbilical vein endothelial cells (Li et al, 2015)hepatocytes and hepatocellular carcinoma cells (Thompson et al, 2014), and rat germ cells (Lizama et al, 2009).…”

Vitamin C mitigates heat damage by reducing oxidative stress, inducing HSP expression in TM4 Sertoli cells

“…Nonetheless, both mRNA and protein expression of CryAB, Hsp27, Hsp70, and Hsp110 was observed. The production of Hsp70 and Hsp110 has been shown to effectively improve cellular survival and resistance to heat stress (Xu, Tang, Song, Yin, & Bao, ; Xu et al, ; Yamagishi, Ishihara, Saito, & Hatayama, ).…”

“…Furthermore, the ability of HSPs to scavenge ROS and maintain a redox balance is well-recognized (Tian et al, 2016;Venkatakrishnan, Cardounel, Zweier, Kuppusamy, & Llangovan, 2006). Our previous studies have reported that pretreatment with aspirin or coenzyme Q10 can induce HSP expression, consequently enhancing the heat resistance of the heart tissue and cardiomyocytes (Tang et al, 2014;Tang et al, 2016;Xu, Tang, Song, Yin, & Wu, 2017).…”

Wnt/β‐catenin‐mediated heat exposure inhibits intestinal epithelial cell proliferation and stem cell expansion through endoplasmic reticulum stress

“…High ambient temperature, especially above 35°C, has been demonstrated to disturb intestinal mucosal homeostasis and impair the barrier function yielding mucosal malabsorption, ulcerations, and inflammation (Song et al, 2014; Xia et al, 2017). Accumulating evidence indicates that intestinal epithelial cells respond to heat stress (HS) in several ways to increases their survival, such as expression of heat shock protein 70 (HSP70) which participates in the folding and assembly of nascent or stress denatured proteins as a molecular chaperone (Daugaard, Rohde, & Jaattela, 2007; Piri, Kwong, Gu, & Caprioli, 2016; Xu et al, 2017). Interestingly, Alemu et al (2018) found that heat exposure (41°C) triggered endoplasmic reticulum stress (ERS) accompanied by the accumulation of glucose‐regulated protein 78 (GRP78), a member of Hsp70 subfamily.…”

“…epithelial cells respond to heat stress (HS) in several ways to increases their survival, such as expression of heat shock protein 70 (HSP70) which participates in the folding and assembly of nascent or stress denatured proteins as a molecular chaperone (Daugaard, Rohde, & Jaattela, 2007;Piri, Kwong, Gu, & Caprioli, 2016;Xu et al, 2017). Interestingly, Alemu et al (2018) found that heat exposure (41°C) triggered endoplasmic reticulum stress (ERS) accompanied by the accumulation of glucose-regulated protein 78 (GRP78), a member of Hsp70 subfamily.…”