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Protein synthesis is required for stabilization of hsp70 mRNA upon exposure to both hydrostatic pressurization and elevated temperature
Author(s) -
Kaarniranta Kai,
Holmberg Carina I.,
Helminen Heikki J.,
Eriksson John E.,
Sistonen Lea,
Lammi Mikko J.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01693-8
Subject(s) - hsf1 , hsp70 , messenger rna , hydrostatic pressure , heat shock factor , heat shock protein , heat shock , microbiology and biotechnology , transcription (linguistics) , protein biosynthesis , chemistry , gene expression , hela , gene , biology , biochemistry , cell , physics , linguistics , philosophy , thermodynamics
We have recently described that in chondrocytic cells high hydrostatic pressure (HP) causes a heat shock response via mRNA stabilization without a transcriptional activation of the hsp70 gene. In this study, we investigated whether this exceptional regulatory mechanism occurs more generally in different types of cells. Indeed, hsp70 mRNA and protein accumulated in HeLa, HaCat and MG‐63 cells under 30 MPa HP, without DNA‐binding of heat shock transcription factor 1 (HSF1) to the heat shock element of the hsp70 gene or formation of nuclear HSF1 granules, revealing a lack of transcriptional activation. Moreover, we observed that protein synthesis is needed for mRNA stabilization. Thus, high HP offers a model to study the mechanisms of hsp70 mRNA stabilization without HSF1‐mediated induction of the heat shock gene response.