Heat therapy preserves myofibre size and SERCA‐mediated Ca2+ uptake in the mouse soleus after tenotomy surgery

Abstract Heat therapy (HT) has been shown to induce physiological adaptations in muscle, including a reduction in the severity of muscle atrophy resulting from unloading. The muscle atrophy caused by unloading can be partially attributed to the dysregulation of Ca2+ in the muscle cell, which can act...

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Main Authors: Michael K. Barfoot, Jessica L. Braun, Phillip J. Wallace, Bianca M. Marcella, Ryan W. Baranowski, Rebecca E. K. MacPherson, Stephen S. Cheung, Val A. Fajardo
Format: Article
Language:English
Published: Wiley 2025-05-01
Series:Physiological Reports
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Online Access:https://doi.org/10.14814/phy2.70385
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author Michael K. Barfoot
Jessica L. Braun
Phillip J. Wallace
Bianca M. Marcella
Ryan W. Baranowski
Rebecca E. K. MacPherson
Stephen S. Cheung
Val A. Fajardo
author_facet Michael K. Barfoot
Jessica L. Braun
Phillip J. Wallace
Bianca M. Marcella
Ryan W. Baranowski
Rebecca E. K. MacPherson
Stephen S. Cheung
Val A. Fajardo
author_sort Michael K. Barfoot
collection DOAJ
description Abstract Heat therapy (HT) has been shown to induce physiological adaptations in muscle, including a reduction in the severity of muscle atrophy resulting from unloading. The muscle atrophy caused by unloading can be partially attributed to the dysregulation of Ca2+ in the muscle cell, which can activate calpain‐mediated proteolysis. The sarco(endo)plasmic reticulum Ca2+‐ATPase (SERCA) is a primary regulator of Ca2+ in muscle, and SERCA dysfunction has been repeatedly demonstrated in various models of muscle unloading. Heat shock protein 70 (HSP70) is a heat‐inducible chaperone protein that binds to SERCA and protects against its dysfunction. While previous research has shown HT to upregulate HSP70 in rodent muscle, even in the unloaded state, the effects of HT on SERCA function in rodent skeletal muscle under these conditions remain unknown. Here, we characterized the effects of 4 weeks of HT on soleus muscle size, HSP70 expression, SERCA function, and maximal calpain activity in male C57BL/6J mice subjected to muscle unloading through tenotomy. Four weeks of HT preserved the cross‐sectional area of soleus myofibres following tenotomy, while also upregulating HSP70, maintaining SERCA‐mediated Ca2+ uptake, and reducing maximal calpain activity. Therefore, our research offers new insights into the advantages of HT for muscle health and physiology.
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spelling doaj-art-57cfc043497d4046966d012c62dd763b2025-08-20T04:27:55ZengWileyPhysiological Reports2051-817X2025-05-011310n/an/a10.14814/phy2.70385Heat therapy preserves myofibre size and SERCA‐mediated Ca2+ uptake in the mouse soleus after tenotomy surgeryMichael K. Barfoot0Jessica L. Braun1Phillip J. Wallace2Bianca M. Marcella3Ryan W. Baranowski4Rebecca E. K. MacPherson5Stephen S. Cheung6Val A. Fajardo7Department of Kinesiology Brock University St. Catharines Ontario CanadaDepartment of Kinesiology Brock University St. Catharines Ontario CanadaDepartment of Kinesiology Brock University St. Catharines Ontario CanadaDepartment of Kinesiology Brock University St. Catharines Ontario CanadaDepartment of Kinesiology Brock University St. Catharines Ontario CanadaCentre for Bone and Muscle Health Brock University St. Catharines Ontario CanadaDepartment of Kinesiology Brock University St. Catharines Ontario CanadaDepartment of Kinesiology Brock University St. Catharines Ontario CanadaAbstract Heat therapy (HT) has been shown to induce physiological adaptations in muscle, including a reduction in the severity of muscle atrophy resulting from unloading. The muscle atrophy caused by unloading can be partially attributed to the dysregulation of Ca2+ in the muscle cell, which can activate calpain‐mediated proteolysis. The sarco(endo)plasmic reticulum Ca2+‐ATPase (SERCA) is a primary regulator of Ca2+ in muscle, and SERCA dysfunction has been repeatedly demonstrated in various models of muscle unloading. Heat shock protein 70 (HSP70) is a heat‐inducible chaperone protein that binds to SERCA and protects against its dysfunction. While previous research has shown HT to upregulate HSP70 in rodent muscle, even in the unloaded state, the effects of HT on SERCA function in rodent skeletal muscle under these conditions remain unknown. Here, we characterized the effects of 4 weeks of HT on soleus muscle size, HSP70 expression, SERCA function, and maximal calpain activity in male C57BL/6J mice subjected to muscle unloading through tenotomy. Four weeks of HT preserved the cross‐sectional area of soleus myofibres following tenotomy, while also upregulating HSP70, maintaining SERCA‐mediated Ca2+ uptake, and reducing maximal calpain activity. Therefore, our research offers new insights into the advantages of HT for muscle health and physiology.https://doi.org/10.14814/phy2.70385calpainHSP70muscle unloadingSERCA
spellingShingle Michael K. Barfoot
Jessica L. Braun
Phillip J. Wallace
Bianca M. Marcella
Ryan W. Baranowski
Rebecca E. K. MacPherson
Stephen S. Cheung
Val A. Fajardo
Heat therapy preserves myofibre size and SERCA‐mediated Ca2+ uptake in the mouse soleus after tenotomy surgery
Physiological Reports
calpain
HSP70
muscle unloading
SERCA
title Heat therapy preserves myofibre size and SERCA‐mediated Ca2+ uptake in the mouse soleus after tenotomy surgery
title_full Heat therapy preserves myofibre size and SERCA‐mediated Ca2+ uptake in the mouse soleus after tenotomy surgery
title_fullStr Heat therapy preserves myofibre size and SERCA‐mediated Ca2+ uptake in the mouse soleus after tenotomy surgery
title_full_unstemmed Heat therapy preserves myofibre size and SERCA‐mediated Ca2+ uptake in the mouse soleus after tenotomy surgery
title_short Heat therapy preserves myofibre size and SERCA‐mediated Ca2+ uptake in the mouse soleus after tenotomy surgery
title_sort heat therapy preserves myofibre size and serca mediated ca2 uptake in the mouse soleus after tenotomy surgery
topic calpain
HSP70
muscle unloading
SERCA
url https://doi.org/10.14814/phy2.70385
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