Zhang X, Qian Z, Zhu H, Tang S, Wu D, Zhang M, Kemper N, Hartung J, Bao E
a College of Veterinary Medicine , Nanjing Agricultural University , Nanjing , China.
b College of Animal Science and Technology , Jinling Institute of Technology , Nanjing , China.
Br Poult Sci. 2016 Aug;57(4):462-73. doi: 10.1080/00071668.2016.1174978. Epub 2016 Jun 16.
To understand the potential protection of heat shock protein 90 (HSP90) induced by aspirin against heat stress damage in chicken myocardial cells, enzyme activities related to stress damage, cytopathological changes, the expression and distribution of HSP90, and HSP90 mRNA levels in the myocardial cells exposed to heat stress (42°C) for different durations with or without aspirin administration (1 mg/ml, 2 h prior) in vitro were investigated. Significant increase of enzyme levels in the supernatant of heat-stressed myocardial cells and cellular lesions characterised by acute degeneration, karyopyknosis and karyorrhexis were observed, compared to non-treated cells. However, the lesions of cells treated with aspirin were milder, characterised by earlier recovery of enzyme levels to the control levels and no obvious heat stress-related cellular necrosis. Stronger positive signals in the cytoplasm and longer retention of HSP90 signal in nuclei were observed in aspirin-treated myocardial cells than those of only heat-stressed cells. HSP90 level in the aspirin-treated myocardial cells was 11.1-fold higher than that in non-treated cells, and remained at a high level at the early stage of heat stress, whereas it was just 4.1-fold higher in only heat-stressed cells and returned rapidly to a low level. Overexpression of HSP90 mRNA in aspirin-treated cells was observed throughout the experiment, whereas HSP90 mRNA decreased significantly only in heat-stressed cells. The early higher HSP90 expression induced by aspirin during heat stress was accompanied by decreased heat stress damage, suggesting that aspirin might play an important role in preventing myocardial cells from heat stress damage in vitro.
为了解阿司匹林诱导的热休克蛋白90（HSP90）对鸡心肌细胞热应激损伤的潜在保护作用，研究了体外给予或不给予阿司匹林（1mg/ml，提前2小时），热应激（42°C）不同持续时间下，心肌细胞中与应激损伤相关的酶活性、细胞病理变化、HSP90的表达和分布以及HSP90 mRNA水平。与未处理的细胞相比，热应激心肌细胞上清液中的酶水平显著升高，细胞出现以急性变性、核固缩和核溶解为特征的病变。然而，用阿司匹林处理的细胞病变较轻，表现为酶水平较早恢复到对照水平，且无明显的热应激相关细胞坏死。与仅热应激的细胞相比，阿司匹林处理的心肌细胞胞质中阳性信号更强，细胞核中HSP90信号保留时间更长。阿司匹林处理的心肌细胞中HSP90水平比未处理的细胞高11.1倍，在热应激早期保持在高水平，而仅热应激的细胞中HSP90水平仅高4.1倍，并迅速恢复到低水平。在整个实验过程中，观察到阿司匹林处理的细胞中HSP90 mRNA过表达，而仅热应激的细胞中HSP90 mRNA显著下降。热应激期间阿司匹林诱导的早期较高HSP90表达伴随着热应激损伤的减少，这表明阿司匹林可能在体外预防心肌细胞热应激损伤中起重要作用。
