The present study aimed to analyze the expression levels and localizations of heat shock protein (HSP) 60 and HSP10 in the heart tissue of rats subjected to heat stress (42°C) for 0, 20, 80 and 100 min. Histopathological injuries and increased serum activities of serum lactate dehydrogenase and creatine kinase isoenzyme MB were detected in the heated rat myocardial cells. These results suggested that heat stress-induced acute degeneration may be sufficient to cause sudden death in animals by disrupting the function and permeability of the myocardial cell membrane. In addition, the expression levels of HSP60 were significantly increased following 20 min heat stress, whereas the expression levels of its cofactor HSP10 were not. Furthermore, the location of HSP60, but not of HSP10, was significantly altered during periods of heat stress. These results suggested that HSP60 in myocardial tissue may be more susceptive to the effects of heat stress as compared with HSP10, and that HSP10 is constitutively expressed in the heart of rats. The expression levels and localizations of HSP60 and HSP10 at the different time points of heat stress were not similar, which suggested that HSP60 and HSP10 may not form a complex in the heart tissue of heat-stressed rats.
Keywords: expression; heart; heat shock protein 10; heat shock protein 60; heat stress; rats.