The influence of environmental stressful conditions on the interaction between heat shock proteins and chaperone-assisted proteins in land snails, Helix pomatia L.

Abstract

Snails are often exposed to high variability of ambient temperatures, thus in response to that, they function for prolonged periods in a dormant state. It is known that molecular chaperones (like heat shock proteins (HSPs)) fulfill important functions in maintaining cell homeostasis and the cellular responses to stress, and that they are activated in many different species upon exposition to various environmental stressors. HSPs defend organisms from the harmful consequences of heat shock and potentially alternative stressors too. After thorough consideration, we decided to identify proteins that interact with HSP70 and HSP90 in Helix pomatia Linnaeus, 1758 snails under extreme thermal (low and high) and photoperiod (short and long) conditions and at hypometabolic/active states as a response to environmental stress. Identification of proteins that interact with HSPs can define a new tool in molecular basis of adaptation to temperature stress in snails. After performing co-immunoprecipitation and Western blot, we obtained results showing that HSP70 interacts with hemocyanin alphaN and alphaD, and with other isoforms of hemocyanin–hemocyanin beta as well as with Na+/K+-ATPase, whereas HSP90 interacts with hemocyanin alphaN. It means that the chaperones are likely to affect the most important life-supporting systems of snails like respiration and ionic conductivity.