BRIEF RESEARCH REPORT article
Front. Physiol.
Sec. Striated Muscle Physiology
Sarcolipin but not Phospholamban Responds to In-Vivo Heat Stress in Rat Skeletal Muscle Similar to the 70-kDa Heat Shock Protein
Aditya Nirav Brahmbhatt 1
John Zewen Chan 2
Michelle Tomczewski 2
Aeron Humaid 2
Hannah Irene Gallichan 2
Jean Flanagan 3
Robin E Duncan 2
Arthur Russell Tupling 2
1. York University School of Kinesiology and Health Science, Toronto, Canada
2. University of Waterloo Department of Kinesiology and Health Sciences, Waterloo, Canada
3. University of Waterloo, Waterloo, Canada
Select one of your emails
You have multiple emails registered with Frontiers:
Notify me on publication
Please enter your email address:
If you already have an account, please login
You don't have a Frontiers account ? You can register here
Abstract
Sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) pumps are found on the membrane of the sarcoplasmic reticulum (SR) which actively transport Ca2+ from the cytosol into the SR. The 70-kDa heat shock protein (Hsp70), sarcolipin (SLN) and phospholamban (PLN) can 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 in-vivo HS with that of Hsp70 in rat soleus (SOL) and white gastrocnemius (WG). The HS protocol involved submerging the lower limbs of the animals either in a 37ºC (control) or 44-45ºC (HS) water bath for 30 minutes. We detected increases in Hsp70 gene expression in the male WG immediately post-HS and in the female SOL after 48-hours. Similarly, protein expression was induced after 24 hours in both the muscles of males and in the female WG, and remained elevated after 48 hours in the male SOL. SLN gene expression was induced in the male WG after 48 hours and a trending increase was found for protein expression in the male SOL following HS. 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 in-vivo HS in a sex-and muscle-specific manner.
Summary
Keywords
70-kDa heat shock protein, Heat stress, Phospholamban, Sarco(endo)plasmicreticulum Ca2+-ATPase, Sarcolipin
Received
09 December 2025
Accepted
19 February 2026
Copyright
© 2026 Brahmbhatt, Chan, Tomczewski, Humaid, Gallichan, Flanagan, Duncan and Tupling. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
*Correspondence: Arthur Russell Tupling
Disclaimer
All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.