Abstract
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.
Original language | English |
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Pages (from-to) | 2543–2551 |
Number of pages | 9 |
Journal | Journal of Experimental Biology |
Volume | 201 |
Issue number | Pt 17 |
DOIs | |
Publication status | Published - Sept 1998 |
MoE publication type | A1 Journal article-refereed |
Keywords
- Animals
- Cells, Cultured
- Fibroblasts/metabolism
- Gene Expression Regulation
- Gills/cytology
- HSP70 Heat-Shock Proteins/biosynthesis
- Hot Temperature
- Hypoxia/metabolism
- Liver/cytology
- Oncorhynchus mykiss/metabolism
- Protein Biosynthesis
- Stress, Physiological/metabolism