Heikkila J J, Darasch S P, Mosser D D, Bols N C
Biochem Cell Biol. 1987 Apr;65(4):310-6. doi: 10.1139/o87-040.
Heat shock protein (HSP) synthesis was studied in the Xenopus epithelial cell line A6 in response to heat and sodium arsenite, either singly or together. Temperatures of 33-35 degrees C consistently brought about the synthesis of HSPs at 87, 73, 70, 54, 31, and 30 kilodaltons (kDa), whereas sodium arsenite at 25-100 microM induced the synthesis of HSPs at 73 and 70 kDa. In cultures exposed to 10 microM sodium arsenite at 30 degrees C, HSP synthesis in the 68- to 73-kDa and 29- to 31-kDa regions was much greater than the HSP synthesis in response to each treatment individually. RNA dot blot analysis using homologous genomic subclones revealed that heat shock induced the accumulation of HSP 70 and 30 mRNAs. The sizes of the HSP 70 and 30 mRNAs determined by Northern hybridization were 2.7 and 1.5 kilobases, respectively. Sodium arsenite (10-100 microM) also induced the accumulation of both HSP 70 and 30 mRNAs. Finally, a mild heat shock (30 degrees C) plus a low concentration of sodium arsenite (10 microM) acted synergistically on HSP 70 and 30 mRNA accumulation in A6 cells. Thus sodium arsenite and heat act synergistically at the level of both HSP synthesis and HSP mRNA accumulation.
研究了非洲爪蟾上皮细胞系A6中热休克蛋白(HSP)在单独或同时暴露于热和亚砷酸钠时的合成情况。33 - 35摄氏度的温度持续诱导87、73、70、54、31和30千道尔顿(kDa)的热休克蛋白合成,而25 - 100微摩尔的亚砷酸钠诱导73和70 kDa的热休克蛋白合成。在30摄氏度下暴露于10微摩尔亚砷酸钠的培养物中,68至73 kDa和29至31 kDa区域的热休克蛋白合成比单独对每种处理的热休克蛋白合成要多得多。使用同源基因组亚克隆进行的RNA斑点印迹分析表明,热休克诱导了热休克蛋白70和30 mRNA的积累。通过Northern杂交确定的热休克蛋白70和30 mRNA的大小分别为2.7和1.5千碱基。亚砷酸钠(10 - 100微摩尔)也诱导了热休克蛋白70和30 mRNA的积累。最后,轻度热休克(30摄氏度)加低浓度亚砷酸钠(10微摩尔)对A6细胞中热休克蛋白70和30 mRNA的积累具有协同作用。因此,亚砷酸钠和热在热休克蛋白合成和热休克蛋白mRNA积累水平上具有协同作用。