Abstract
Accumulating evidence indicates that heat shock protein 90 (HSP90) plays essential roles in modulation of phenotypic plasticity in vertebrate development, however, the roles of HSP90 in modulation of cold tolerance capacity in fish are still unclear. In the present study, we showed that transient inhibition of embryonic HSP90 function by a chemical inhibitor or low conductivity stress promoted variation of cold tolerance capacity in adult zebrafish. Further work showed that embryonic HSP90 inhibition enhanced cold tolerance in adult zebrafish could be transmitted to their offspring. RNA-seq data showed that embryonic HSP90 inhibition enhanced cold tolerance involves variation of gene expression related to proteasome, lysosome, autophagy, and ribosome. Experiments with zebrafish ZF4 cells showed that two differentially expressed genes atg9b and psmd12 were up-regulated by radicicol treatment and provided protective roles for cells under cold stress, indicating that up-regulation of autophagy and proteasome function contributes to enhanced cold tolerance. The present work sheds a light on the roles of HSP90 in regulation of phenotypic plasticity associated with thermal adaptation in fish.
Highlights
Heat shock proteins (HSPs) are a family of stress proteins that are expressed in prokaryote and eukaryote cells and tissues both constitutively and in response to biotic and abiotic stressors, acting as molecular chaperones that protect the cell against denatured proteins (Terasawa et al, 2005)
Inhibition of heat shock protein 90 (HSP90) function was confirmed by significantly increased a decrease of the median lethal time (LT50) was observed in zebrafish from radicicol group (Figure 2B), suggesting globally impaired cold tolerance for radicicol group despite the fact that some zebrafish showed extended survival times
We observed no significant correlation between body weight or body length and survival time for both groups (Figures 2C,D), excluding the possibility that observed variation of cold tolerance is attributed to body weight
Summary
Heat shock proteins (HSPs) are a family of stress proteins that are expressed in prokaryote and eukaryote cells and tissues both constitutively and in response to biotic and abiotic stressors, acting as molecular chaperones that protect the cell against denatured proteins (Terasawa et al, 2005). Cold Tolerance Induced by HSP90 Inhibitor (Hoekstra et al, 1998; Lei et al, 2009; Li and Mak, 2009) In addition to their immediate action after stress exposure, compromised HSP90 activity during development results in generation of novel phenotypes. Zebrafish embryos were subjected to a transient treatment with a HSP90 chemical inhibitor radicicol, and increased variation of cold tolerance capacity of adult zebrafish was observed. Further work showed that HSP90 inhibition enhanced cold tolerance in adult zebrafish could be transmitted to the generation. Low conductivity condition perturbed HSP90 function in zebrafish embryos and resulted in enhanced variation of cold tolerance capacity in adult zebrafish. Our data indicated that interference of HSP90 function during development by chemical inhibitor or environmental stress promotes variation of cold tolerance in zebrafish
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