Heikkila J J, Schultz G A, Iatrou K, Gedamu L
J Biol Chem. 1982 Oct 25;257(20):12000-5.
Elevation of the incubation temperature of Chinook salmon embryo cells from 20 to 24 degrees C or exposure to heavy metals such as CdCl2 (5 microM) or ZnCl2 (100 to 500 microM) induces the reversible expression of a set of heat shock or stress proteins. Continuous exposure of the cells to either metal ions or heat shock results in recovery of protein synthesis to a control-like pattern. Treatment of these cells with either ZnCl2 or CdCl2 also induces the protein metallothionein. Heat shock, however, does not induce metallothionein, suggesting that it does not belong to the common group of heat shock or stress proteins. The induction of these stress proteins can be inhibited by pretreatment with actinomycin D, suggesting that their expression is regulated at the transcriptional level. The major stress proteins are detectable in the products of an in vitro translation system programmed with RNA isolated from heat shock- or metal ion-treated cells. A recombinant DNA probe complementary to Drosophila mRNA coding for the 70,000-dalton heat shock protein was found to hybridize to RNA isolated from heat shock-or metal ion-treated cells but not from control cells. The fish mRNA coding for the heat shock protein with a molecular weight of 70,000 appears to be of similar size to the corresponding Drosophila mRNA.
将奇努克鲑鱼胚胎细胞的培养温度从20摄氏度提高到24摄氏度，或使其暴露于重金属如氯化镉（5微摩尔）或氯化锌（100至500微摩尔）中，会诱导一组热休克或应激蛋白的可逆表达。细胞持续暴露于金属离子或热休克中会导致蛋白质合成恢复到类似对照的模式。用氯化锌或氯化镉处理这些细胞也会诱导金属硫蛋白的产生。然而，热休克不会诱导金属硫蛋白，这表明它不属于热休克或应激蛋白的常见类别。这些应激蛋白的诱导可以通过放线菌素D预处理来抑制，这表明它们的表达在转录水平上受到调控。主要的应激蛋白可以在用热休克或金属离子处理过的细胞分离的RNA编程的体外翻译系统产物中检测到。发现与果蝇编码70,000道尔顿热休克蛋白的mRNA互补的重组DNA探针与从热休克或金属离子处理过的细胞分离的RNA杂交，但不与对照细胞的RNA杂交。鱼类编码分子量为70,000的热休克蛋白的mRNA似乎与相应的果蝇mRNA大小相似。
