Dubois M F, Mezger V, Morange M, Ferrieux C, Lebon P, Bensaude O
Unité de Recherches sur les Infections Virales, INSERM U 43, Hôpital St. Vincent de Paul, France.
J Cell Physiol. 1988 Oct;137(1):102-9. doi: 10.1002/jcp.1041370112.
Interferon (IFN) is not able to induce heat-shock protein (HSP) synthesis. However IFN pretreatment of mouse L cells has been shown to enhance the decrease of overall protein synthesis which follows a heat shock, and to stimulate the accumulation of HSPs. We show here that the synthesis of a protein (the hepatitis B virus surface antigen) under the control of a Drosophila HSP 70 promoter is also stimulated in IFN-pretreated cells. The regulation by IFN takes place at two levels: first, the rate of HSP gene transcription is increased in nuclei isolated from IFN-treated cells; second, the synthesis of HSPs is prolonged after pretreatment with IFN. Experiments performed in the presence of actinomycin D show that this effect is due to a stabilization by IFN of mRNAs coding for HSPs.
干扰素（IFN）不能诱导热休克蛋白（HSP）的合成。然而，已证明对小鼠L细胞进行IFN预处理可增强热休克后整体蛋白质合成的减少，并刺激HSP的积累。我们在此表明，在果蝇HSP 70启动子控制下的一种蛋白质（乙肝病毒表面抗原）的合成在IFN预处理的细胞中也受到刺激。IFN的调节发生在两个层面：第一，从IFN处理的细胞中分离出的细胞核中，HSP基因转录速率增加；第二，用IFN预处理后，HSP的合成时间延长。在放线菌素D存在的情况下进行的实验表明，这种效应是由于IFN对编码HSP的mRNA的稳定作用。
