HSP70, HSP90A, and HSP90B are Differentially Regulated in Response to Thermal, Osmotic and Hypoxic Stressors

The Heat shock proteins, Hsp70 and Hsp90 are highly conserved and play a significant role in cellular response to a variety of stressors. In response to stressors, cellular expression levels of these heat shock proteins are increased to stabilize degrading proteins and to initiate thermotolerance among other complex functions. Maintenance of physiological temperature in all organisms is imperative to ensure that biological systems function normally. This is especially critical for cold-blooded organisms whose internal temperature is subject to their environmental conditions. High temperatures and other stressors can deleteriously affect animal motility, its ability to avoid predators, neuronal activity and affect neuropeptide populations. However, the effect of stressors on muscle and on neuronal activity are not always equal. Here we use the important commercially important Jonah crab, Cancer borealis as a model to assess the effect of different stressors on transcript levels of the major heat shock proteins, HSP70, HSP90A and HSP90B. Since these genes have not been identified or sequenced in C borealis, we cloned each gene and we demonstrate that a) these genes have different expression profiles in thermal, osmotic and hypoxic stresses and that b) these genes are differentially expressed in muscle and brain cells.