Effects of heat shock protein 90 expression on pectoralis major oxidation in broilers exposed to acute heat stress

文献类型： 外文期刊

第一作者： Hao, Y.

作者： Hao, Y.;Gu, X. H.

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期刊名称：POULTRY SCIENCE （ 影响因子：3.352； 五年影响因子：3.679 ）

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收录情况： SCI

摘要： This study was conducted to determine the effects of heat shock protein 90 (HSP90) expression on pH, lipid peroxidation, heat shock protein 70 (HSP70), and glucocorticoid receptor (GR) expression of pectoralis major in broilers exposed to acute heat stress. In total, 90 male broilers were randomly allocated to 3 groups: control (CoN), heat stress (HS), or geldanamycin treatment (GA). on d 41, the broilers in the GA group were injected intraperitoneally with GA (5 mu g/kg of BW), and the broilers in the CoN and HS groups were injected intraperitoneally with saline. Twenty-four hours later, the broilers in the CoN group were moved to environmental chambers controlled at 22 degrees C for 2 h, and the broilers in the HS and GA groups were moved to environmental chambers controlled at 40 degrees C for 2 h. The pH values of the pectoralis major after 30 min and 24 h of chilling after slaughter of HS and GA broilers were significantly lower (P < 0.01) than those of the CoN broilers. Heat stress caused significant increases in sera corticosterone and lactic dehydrogenase, the activity of malondialdehyde and superoxide dismutase, the expression of HSP90 and HSP70, and nuclear expression of GR protein in the pectoralis major (P < 0.05). Heat stress induced a significant decrease in GR protein expression in the cytoplasm and GR mRNA expression. Furthermore, the low expression of HSP90 significantly increased levels of lactic dehydrogenase and malondialdehyde and GR protein expression in the cytoplasm under heat stress (P < 0.01), and significantly decreased nuclear GR protein expression (P < 0.01). Heat shock protein 90 was positively correlated with corticosterone and superoxide dismutase activities (P < 0.01), and HSP90 mRNA was negatively correlated with pH after chilling for 24 h. The results demonstrated that HSP90 plays a pivotal role in protecting cells from oxidation.

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