qPCR Data for Sarcolipin, Phospholamban, and 70-kDa Heat Shock Protein Response to In-Vivo Heat Stress

Sarco/endoplasmic reticulum Ca²⁺ ATPase (SERCA) pumps are found on the membrane of the sarcoplasmic reticulum (SR) and function to actively transport Ca²⁺ from the cytosol into the SR. The 70-kDa heat shock protein (Hsp70), sarcolipin (SLN) and phospholamban (PLN) can also preserve SERCA function in the face of heat stress (HS). However, it remains unknown if SLN and PLN can be stress-induced proteins like Hsp70. Therefore, the purpose of this study was to compare the SLN and PLN gene and protein time course (0, 24, and 48 hours) response to <i>in-vivo</i> HS with that of Hsp70 in rat soleus (SOL) and white gastrocnemius (WG) muscles. The HS protocol involved submerging the lower limbs of the animals either in a 37ºC (control) or 44-45ºC (HS) water bath to either maintain core temperature at 37ºC (control) or between 41-41.5ºC (HS) for 30 minutes. We detected increases in <i>Hsp70</i> gene expression in the male WG immediately post-HS and in the female SOL 48-hours post-HS. Similarly, protein expression was induced after 24 hours in both the muscles of males and in the female WG, and after 48 hours in the male SOL. SLN gene expression was induced in the male WG after 48 hours and protein expression in the male SOL after 24 hours. In contrast, PLN did not show any signs of stress-induction in either muscle or sex. These results suggest that like Hsp70, SLN, but not PLN, is a stress-induced protein that responds to <i>in-vivo</i> HS in a sex- and muscle-specific manner.<br>