Effects of heat shock and hypoxia on protein synthesis in rainbow trout (Oncorhynchus mykiss) cells.
We examined the effects of heat stress (from 18 degreesC to 26 degreesC) and low oxygen tension (1% O2=1 kPa) on protein synthesis in primary cultures of hepatocytes, gill epithelial cells and fibroblast-like RTG-2 cells of rainbow trout Oncorhynchus mykiss. All these cell types displayed elevated levels of 67, 69 and 92 kDa proteins, whereas a 104 kDa protein was induced only in RTG-2 cells. Hypoxia induced a cell-type-specific response, increasing the synthesis of 36, 39 and 51 kDa proteins in the gill epithelial cells. The regulation of the heat-shock response in fish hepatocytes showed that an HSF1-like factor is involved in the transcriptional induction of the hsp70 gene. Consequently, there was a pronounced accumulation of hsp70 mRNA. Furthermore, the kinetics of activation of DNA binding and the increase in hsp70 gene expression showed a remarkable correlation, indicating that hsp70 expression is regulated at the transcriptional level in these trout cells.
Laboratory of Animal Physiology, Department of Biology, University of Turku, FIN-20014 Turku, Finland. susair@utu.fi
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Airaksinen
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Råbergh
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Sistonen
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Nikinmaa
D000818:Animals; D002478:Cells, Cultured; D005347:Fibroblasts / Q000378:metabolism; D005786:Gene Expression Regulation; D005880:Gills / Q000166:cytology / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D000860:Hypoxia / Q000378:metabolism*; D008099:Liver / Q000166:cytology / Q000378:metabolism; D017686:Oncorhynchus mykiss / Q000378:metabolism*; D014176:Protein Biosynthesis; D013312:Stress, Physiological / Q000378:metabolism*
D018840:HSP70 Heat-Shock Proteins