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.
