Document Detail

Acute heat stress prior to downhill running may enhance skeletal muscle remodeling.
MedLine Citation:
PMID:  22589083     Owner:  NLM     Status:  MEDLINE    
Heat shock proteins (HSPs) are chaperones that are known to have important roles in facilitating protein synthesis, protein assembly and cellular protection. While HSPs are known to be induced by damaging exercise, little is known about how HSPs actually mediate skeletal muscle adaption to exercise. The purpose of this study was to determine the effects of a heat shock pretreatment and the ensuing increase in HSP expression on early remodeling and signaling (2 and 48 h) events of the soleus (Sol) muscle following a bout of downhill running. Male Wistar rats (10 weeks old) were randomly assigned to control, eccentric exercise (EE; downhill running) or heat shock + eccentric exercise (HS; 41°C for 20 min, 48 h prior to exercise) groups. Markers of muscle damage, muscle regeneration and intracellular signaling were assessed. The phosphorylation (p) of HSP25, Akt, p70s6k, ERK1/2 and JNK proteins was also performed. As expected, following exercise the EE group had increased creatine kinase (CK; 2 h) and mononuclear cell infiltration (48 h) compared to controls. The EE group had an increase in p-HSP25, but there was no change in HSP72 expression, total protein concentration, or neonatal MHC content. Additionally, the EE group had increased p-p70s6k, p-ERK1/2, and p-JNK (2 h) compared to controls; however no changes in p-Akt were seen. In contrast, the HS group had reduced CK (2 h) and mononuclear cell infiltration (48 h) compared to EE. Moreover, the HS group had increased HSP72 content (2 and 48 h), total protein concentration (48 h), neonatal MHC content (2 and 48 h), p-HSP25 and p-p70s6k (2 h). Lastly, the HS group had reduced p-Akt (48 h) and p-ERK1/2 (2 h). These data suggest that heat shock pretreatment and/or the ensuing HSP72 response may protect against muscle damage, and enhance increases in total protein and neonatal MHC content following exercise. These changes appear to be independent of Akt and MAPK signaling pathways.
Chad D Touchberry; Anisha A Gupte; Gregory L Bomhoff; Zachary A Graham; Paige C Geiger; Philip M Gallagher
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Publication Detail:
Type:  Journal Article     Date:  2012-05-17
Journal Detail:
Title:  Cell stress & chaperones     Volume:  17     ISSN:  1466-1268     ISO Abbreviation:  Cell Stress Chaperones     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-10-11     Completed Date:  2013-03-05     Revised Date:  2013-06-25    
Medline Journal Info:
Nlm Unique ID:  9610925     Medline TA:  Cell Stress Chaperones     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  693-705     Citation Subset:  IM    
University of Missouri-Kansas City, School of Medicine-Basic Medical Science, 2464 Charlotte Street, Kansas City, MO 64108, USA.
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MeSH Terms
Creatine Kinase / metabolism
HSP72 Heat-Shock Proteins / metabolism
Intracellular Signaling Peptides and Proteins / metabolism
Mitogen-Activated Protein Kinase 1 / metabolism
Mitogen-Activated Protein Kinase 3 / metabolism
Muscle, Skeletal / metabolism*,  pathology
Physical Conditioning, Animal
Protein-Serine-Threonine Kinases / metabolism
Proto-Oncogene Proteins c-akt / metabolism
Rats, Wistar
Ribosomal Protein S6 Kinases, 70-kDa / metabolism
Signal Transduction
Stress, Physiological
Grant Support
Reg. No./Substance:
0/HSP72 Heat-Shock Proteins; 0/Intracellular Signaling Peptides and Proteins; EC 2.7.1.-/MAP-kinase-activated kinase 2; EC Kinases; EC Proteins c-akt; EC Protein S6 Kinases, 70-kDa; EC Protein Kinase 1; EC Protein Kinase 3; EC Kinase

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