Heat shock protein (Hsp70) induced by a mild heat shock slightly moderates plasma osmolarity increases upon salinity transfer in rainbow trout (Oncorhynchus mykiss)

Author(s):  
C.J. Niu ◽  
J.L. Rummer ◽  
C.J. Brauner ◽  
P.M. Schulte
Author(s):  
Barbara Shayne Washburn ◽  
Jason J. Moreland ◽  
Ann M. Slaughter ◽  
Inge Werner ◽  
David E. Hinton ◽  
...  

2013 ◽  
Vol 44 (5) ◽  
pp. 655-668 ◽  
Author(s):  
Wendy M. Sealey ◽  
Frederic T. Barrows ◽  
Charles E. Smith ◽  
Jurij M. Wacyk ◽  
Madison S. Powell ◽  
...  

2018 ◽  
Vol 69 (11) ◽  
pp. 1674 ◽  
Author(s):  
Binpeng Xia ◽  
Zhe Liu ◽  
Yanjing Zhou ◽  
Yongjie Wang ◽  
Jinqiang Huang ◽  
...  

Rainbow trout (Oncorhynchus mykiss) is a cold-water species of salmonid, and high temperatures are a significant threat to its aquaculture. In order to understand the degree of the heat stress response and the mechanisms involved, full-sibling inbred O. mykiss individuals were sampled at 18, 21, 23, 24, 25 and 26°C to investigate changes in some serum biochemical parameters, as well as in the mRNA expression of heat shock protein family A (Hsp70) member 5 (HSPA5; also known as glucose regulated protein 78 (GRP78)) in different tissues (liver, mid-kidney, heart, spleen and brain). At 21°C, there was a significant increase in the spleen macrophage respiratory burst and a significant decrease in superoxide dismutase activity compared with 18°C (P<0.05). Malondialdehyde peaked at 23°C, whereas alanine transaminase and aspartate aminotransferase activity were both twofold higher at 25 and 26°C compared with that at 18°C. The Ca2+, Mg2+, PO43– and glucose (Glu) content of serum declined significantly at 21°C relative to 18°C (P<0.05). The expression of HSPA5 mRNA responded in a temperature- and tissue-specific manner to heat stress. Except for in the spleen, HSPA5 mRNA expression was significantly higher in all tissues at 25 and 26°C than that at 18°C (P<0.05). These results indicate that heat stress causes oxidative damage, decreases the Ca2+, Mg2+, PO43– and Glu content of serum and induces HSPA5 mRNA expression.


2002 ◽  
Vol 21 (3) ◽  
pp. 557-560 ◽  
Author(s):  
Barbara Shayne Washburn ◽  
Jason J. Moreland ◽  
Ann M. Slaughter ◽  
Inge Werner ◽  
David E. Hinton ◽  
...  

1997 ◽  
Vol 200 (3) ◽  
pp. 607-614 ◽  
Author(s):  
S Currie ◽  
B Tufts

Unlike enucleated mammalian red blood cells (rbcs), the nucleated rbcs of lower vertebrates are capable of protein synthesis and may, therefore, serve as a valuable model to investigate the adaptive significance of stress protein synthesis in cells. This study examined the synthesis of stress protein 70 (Hsp70) in rbcs of the temperature-sensitive rainbow trout Oncorhynchus mykiss in response to heat shock and anoxia. Through western blot analysis, we have demonstrated that rainbow trout rbcs synthesize Hsp70 both constitutively and in response to an increase in temperature. Radioisotopic labelling experiments indicated that the temperature at which Hsp70 synthesis was induced in fish acclimated to 10 &deg;C was between 20 and 25 &deg;C. Actinomycin D blocked de novo Hsp70 synthesis, implying that synthesis of Hsp70 is regulated at the level of transcription in rainbow trout rbcs. Since trout rbcs rely heavily on aerobic metabolism, but may also experience very low oxygen levels within the circulation, we also examined the relative importance of (1) anoxia as a stimulus for Hsp70 synthesis and (2) oxygen as a requirement for protein synthesis under control and heat-shock conditions. We found that trout rbcs were capable of protein synthesis during 2 h of anoxia, but did not increase Hsp70 synthesis. Moreover, rbcs subjected to combined anoxia and heat shock exhibited increases in Hsp70 synthesis that were similar in magnitude to those in cells exposed to heat shock alone. The latter results suggest that rainbow trout rbcs are (1) able to synthesize non-stress proteins during anoxia, (2) capable of tolerating periods of reduced oxygen availability without increased synthesis of stress proteins and (3) able to maintain the integrity of their heat-shock response even during periods of anoxia.


1998 ◽  
Vol 201 (17) ◽  
pp. 2543-2551 ◽  
Author(s):  
S Airaksinen ◽  
C M Råbergh ◽  
L Sistonen ◽  
M Nikinmaa

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.


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