Short-term cold stress and heat shock proteins in the crustacean Artemia franciscana
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ORIGINAL PAPER
Short-term cold stress and heat shock proteins in the crustacean Artemia franciscana Yayra A. Gbotsyo 1
&
Nathan M. Rowarth 1 & Laura K. Weir 2 & Thomas H. MacRae 1
Received: 17 April 2020 / Revised: 2 July 2020 / Accepted: 28 July 2020 # Cell Stress Society International 2020
Abstract In their role as molecular chaperones, heat shock proteins (Hsps) mediate protein folding thereby mitigating cellular damage caused by physiological and environmental stress. Nauplii of the crustacean Artemia franciscana respond to heat shock by producing Hsps; however, the effects of cold shock on Hsp levels in A. franciscana have not been investigated previously. The effect of cold shock at 1 °C followed by recovery at 27 °C on the amounts of ArHsp90, Hsp70, ArHsp40, and ArHsp40-2 mRNA and their respective proteins in A. franciscana nauplii was examined by quantitative PCR (qPCR) and immunoprobing of western blots. The same Hsp mRNAs and proteins were also quantified during incubation of nauplii at their optimal growth temperature of 27 °C. qPCR analyses indicated that the abundance of ArHsp90, Hsp70, and ArHsp40 mRNA remained relatively constant during both cold shock and recovery and was not significantly different compared with levels at optimal temperature. Western blotting revealed that ArHsp90, ArHsp40, and ArHsp40-2 were generally below baseline, but at detectable levels during the 6 h of cold shock, and persisted in early recovery stages before declining. Hsp70 was the only protein that remained constant in quantity throughout cold shock and recovery. By contrast, all Hsps declined rapidly during 6 h when nauplii were incubated continuously at 27 °C optimal temperature. Generally, the amounts of ArHsp90, ArHsp40, and ArHsp40-2 were higher during cold shock/recovery than those during continuous incubation at 27 °C. Our data support the conclusion that low temperature preserves Hsp levels, making them available to assist in protein repair and recovery after cold shock. Keywords Cold shock . Molecular chaperones . qPCR . Western blotting . Nauplii . Brine shrimp
Introduction An organism’s ability to tolerate extreme temperatures determines its abundance and geographical distribution by affecting growth, motility, and reproduction (Ramløv 2000; Huang et al. 2007; Bale and Hayward 2010). Changes in temperature beyond physiologically normal levels adversely affect metabolism, gene expression, and protein synthesis, ultimately
Electronic supplementary material The online version of this article (https://doi.org/10.1007/s12192-020-01147-4) contains supplementary material, which is available to authorized users. * Laura K. Weir [email protected] 1
Department of Biology, Dalhousie University, Halifax, N. S. B3H 4R2, Canada
2
Biology Department, Saint Mary’s University Halifax, Halifax, N. S. B3H 3C3, Canada
decreasing the overall performance of an organism within its environment (Ramløv 2000; Teets and Denlinger 2013; Overgaard et al. 2014). At high and low temperatures, such effects may damage lipids, prote
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