Regulation of the heat-shock response by interferon in mouse L cells

• Published in: Journal of cellular physiology Vol. 137; no. 1; p. 102
• Main Authors: Dubois, M F, Mezger, V, Morange, M, Ferrieux, C, Lebon, P, Bensaude, O
• Format: Journal Article
• Language: English
• Published: United States 01-10-1988
• Subjects: Animals; Blotting, Northern; Dactinomycin - pharmacology; Drosophila; Electrophoresis, Polyacrylamide Gel; Gene Expression Regulation - drug effects; Heat-Shock Proteins - biosynthesis; Heat-Shock Proteins - genetics; Hepatitis B Surface Antigens - genetics; Hot Temperature; Interferons - pharmacology; Kinetics; L Cells (Cell Line); Mice; Plasmids; Promoter Regions, Genetic; Protein Biosynthesis; RNA - analysis; RNA, Messenger - drug effects; RNA, Messenger - metabolism; Transcription, Genetic; Transfection
• ISSN: 0021-9541
• 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.