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Regulation of the heat‐shock response by interferon in mouse L cells
Author(s) -
Dubois M. F.,
Mezger V.,
Morange M.,
Ferrieux C.,
Lebon P.,
Bensaude O.
Publication year - 1988
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041370112
Subject(s) - heat shock protein , interferon , biology , transcription (linguistics) , protein biosynthesis , gene , microbiology and biotechnology , virology , biochemistry , linguistics , philosophy
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 stablization by IFN of mRNAs coding for HSPs.