Airaksinen S, Råbergh C M, Sistonen L, Nikinmaa M
Laboratory of Animal Physiology, Department of Biology, University of Turku, FIN-20014 Turku, Finland.
J Exp Biol. 1998 Sep;201(Pt 17):2543-51. doi: 10.1242/jeb.201.17.2543.
We examined the effects of heat stress (from 18 degreesC to 26 degreesC) and low oxygen tension (1% O2=1 kPa) on protein synthesis in primary cultures of hepatocytes, gill epithelial cells and fibroblast-like RTG-2 cells of rainbow trout Oncorhynchus mykiss. All these cell types displayed elevated levels of 67, 69 and 92 kDa proteins, whereas a 104 kDa protein was induced only in RTG-2 cells. Hypoxia induced a cell-type-specific response, increasing the synthesis of 36, 39 and 51 kDa proteins in the gill epithelial cells. The regulation of the heat-shock response in fish hepatocytes showed that an HSF1-like factor is involved in the transcriptional induction of the hsp70 gene. Consequently, there was a pronounced accumulation of hsp70 mRNA. Furthermore, the kinetics of activation of DNA binding and the increase in hsp70 gene expression showed a remarkable correlation, indicating that hsp70 expression is regulated at the transcriptional level in these trout cells.
我们研究了热应激（从18摄氏度升至26摄氏度）和低氧张力（1%氧气=1千帕）对虹鳟Oncorhynchus mykiss原代培养的肝细胞、鳃上皮细胞和成纤维样RTG-2细胞中蛋白质合成的影响。所有这些细胞类型中67、69和92千道尔顿蛋白质的水平均升高，而104千道尔顿的蛋白质仅在RTG-2细胞中被诱导产生。低氧诱导了细胞类型特异性反应，增加了鳃上皮细胞中36、39和51千道尔顿蛋白质的合成。鱼类肝细胞中热休克反应的调节表明，一种类HSF1因子参与了hsp70基因的转录诱导。因此，hsp70 mRNA有明显积累。此外，DNA结合激活的动力学与hsp70基因表达的增加显示出显著相关性，表明hsp70表达在这些鳟鱼细胞中是在转录水平上受到调控的。
