Starvation reduces the heat shock protein responses in white sturgeon larvae |
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Authors: | Dong Han Susie S Y Huang Wei-Fang Wang Dong-Fang Deng Silas S O Hung |
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Institution: | (1) State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, 430072, People’s Republic of China;(2) Department of Animal Science, University of California, Davis, One Shields Avenue, Davis, CA 95616-8521, USA;(3) Qingdao Key Laboratory for Marine Fish Breeding and Biotechnology, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, 266071, People’s Republic of China;(4) Aquatic Feeds and Nutrition Department, Oceanic Institute, Hawaii, 96795, USA; |
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Abstract: | This study investigates the responses of white sturgeon larvae (Acipenser transmontanus) to starvation and thermal stress, through the measurement of nutritional status (i.e. growth performances) and cellular
biomarkers: heat shock proteins (Hsp) 70 and 90. White sturgeon larvae (25 day post hatch; initial weight 179.0 ± 5.1 mg)
were fed (20% body weight per day) or starved for 24, 48 or 72 hrs. Every 24 hrs, five larvae from each of the starved or
fed treatment replicates were exposed to heat shock resulting from an increase in water temperature from 19°C to 26°C, at
a rate of 1°C per 15 min, and maintained at 26°C for 4 hrs. No mortality was observed in this study. Starvation significantly
(p < 0.05) decreased the body weight and body contents of energy, protein, and lipid of the experimental larvae, compared to
the fed larvae. Heat shock induced the expressions of Hsp70 and Hsp90 in both the fed and starved group; however, starvation
reduced the induction at all sampling points. The current study demonstrates that poor larval nutritional status, assessed
by the aforementioned parameters, reduced heat shock responses to thermal stress, as measured by heat shock protein levels.
Furthermore, Hsp70 and 90 are more sensitive to heat shock and starvation, respectively. This may be, in part, a result of
the different functioning of the heat shock proteins in cellular stress response and warrants further study. |
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