Meeting Abstract
Thermal stress can be a consequence of a fish’s natural environment or a result of anthropogenic activities such as industrial thermal pollution. The production of heat shock proteins (hsp) is an important and highly conserved cellular response to thermal and other stressors. In this study, we assessed the kinetics of the heat shock response by quantifying changes in gene expression of hsp90α, hsp70, hsp47, hsp90β, and heat shock cognate 70 (hsc70) in embryonic and young of the year (YOY) juvenile Round Whitefish (Prosopium cylindraceum; RWF). RWF embryos and YOY juveniles were subjected to two different heat shock temperatures (+6 and +9° C) for 1 to 4 h. Embryo and YOY RWF were allowed to recover at control temperatures for 0 to 48 h prior to sampling and quantifying hsp mRNA levels using RT-qPCR. Of the 3 typically inducible hsps, only hsp70 was increased in embryos following heat shock. By comparison, both hsp70 and hsp47 increased in YOY juveniles. mRNA levels of the inducible hsp90α, the constitutive hsp90β, and hsc70 did not vary significant in comparison to controls. Data on recovery from heat shock and on the ontogeny of the heat shock in RWF embryos will also be presented and discussed in the context of RWF being exposed to developing in industrial thermal effluents. A better understanding of the impact of thermal fluctuations which can arise from thermal effluents or climate change on key life history stages of a sensitive cold water species may aid in predicting and mediating anthropogenic influences on these and other near shore spawning fishes.
