Effect of exercise on activation of the p38 mitogen-activated protein kinase pathway, c-Jun NH2 terminal kinase, and heat shock protein 27 in equine skeletal muscle.
Abstract: To investigate the effects of exercise on activation of mitogen-activated protein kinase (MAPK) signaling proteins in horses. Methods: 6 young trained Standardbred geldings. Methods: Horses performed a 20-minute bout of exercise on a treadmill at 80% of maximal heart rate. Muscle biopsy specimens were obtained from the vastus lateralis and pectoralis descendens muscles before and after exercise. Amount of expression and intracellular location of phosphospecific MAPK pathway intermediates were determined by use of western blotting and immunofluorescence staining. Results: Exercise resulted in a significant increase in phosphorylation of p38 pathway intermediates, c-Jun NH2 terminal kinase (JNK), and heat shock protein 27 (HSP27) in the vastus lateralis muscle, whereas no significant changes were found in phosphorylation of extracellular regulated kinase. In the pectoralis descendens muscle, phosphorylation of p38 and HSP27 was significantly increased after exercise. Immunohistochemical analysis revealed fiber-type- specific locations of phosphorylated JNK in type 2a/b intermediate and 2b fibers and phosphorylated p38 in type 1 fibers. Phosphorylated HSP27 was strongly increased after exercise in type 1 and 2a fibers. Conclusions: The p38 pathway and JNK are activated in the vastus lateralis muscle after a single 20-minute bout of submaximal exercise in trained horses. Phosphorylation of HSP27 as detected in the study reported here is most likely induced through the p38 signaling pathway.
Publication Date: 2006-05-03 PubMed ID: 16649919DOI: 10.2460/ajvr.67.5.837Google Scholar: Lookup
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- Clinical Trial
- Journal Article
Summary
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The research study investigates how the proteins in the mitogen-activated protein kinase (MAPK) pathway in horses are affected by exercise. The study finds increases in the activation of specific proteins following exercise, indicating a role of these proteins in muscle response to physical activity.
Study Methods
- Six trained young Standardbred geldings comprised the research subjects.
- Each horse performed a 20-minute round of exercise on a treadmill, operating at 80% of their maximum heart rate.
- Biopsy samples were taken from two muscle groups, the vastus lateralis and pectoralis descendens, before and after the exercise session.
- The levels and intracellular locations of phosphorylation in the MAPK pathway intermediates were ascertained using western blotting and immunofluorescence staining techniques.
Findings
- The vastus lateralis muscle exhibited a significant upsurge in the phosphorylation levels of p38 pathway intermediates, c-Jun NH2 terminal kinase (JNK), and heat shock protein 27 (HSP27) post-exercise.
- No notable alterations were witnessed in the phosphorylation of extracellular regulated kinase in the same muscle group.
- In the pectoralis descendens muscle, the phosphorylation of p38 and HSP27 experienced a significant increase after exercise.
- Immunohistochemical analysis exposed specific locations of the phosphorylated JNK and p38 proteins in differing muscle fiber types, with an increase in the phosphorylated HSP27 in type 1 and 2a fibers after the exercise.
Conclusions
- Both the p38 pathway and JNK are activated within the vastus lateralis muscle post a single 20-minute session of submaximal exercise in the Standardbred geldings.
- The researchers believe the increased phosphorylation of HSP27 visualized in the study is likely an effect of the activation of the p38 signaling pathway.
Implications of study
- The research provides valuable insights into the ways exercise influences the protein pathways within horse muscle tissue. Such discoveries could be vital in understanding how to optimize performance and recovery in equine athletes.
- The findings also help enhance understanding of the cellular effects of exercise more generally, which may have implications for human muscle dynamics as well.
Cite This Article
APA
van Ginneken MM, de Graaf-Roelfsema E, Keizer HA, van Dam KG, Wijnberg ID, van der Kolk JH, van Breda E.
(2006).
Effect of exercise on activation of the p38 mitogen-activated protein kinase pathway, c-Jun NH2 terminal kinase, and heat shock protein 27 in equine skeletal muscle.
Am J Vet Res, 67(5), 837-844.
https://doi.org/10.2460/ajvr.67.5.837 Publication
Researcher Affiliations
- Department of Equine Sciences, Medicine Section, Faculty of Veterinary Medicine, Utrecht University, PO Box 80153, NL3508 TD Utrecht, The Netherlands.
MeSH Terms
- Animals
- Enzyme Activation
- Heat-Shock Proteins / metabolism
- Horses / metabolism
- Horses / physiology
- JNK Mitogen-Activated Protein Kinases / metabolism
- MAP Kinase Signaling System
- Male
- Muscle, Skeletal / cytology
- Muscle, Skeletal / metabolism
- Phosphorylation
- Physical Conditioning, Animal / physiology
- p38 Mitogen-Activated Protein Kinases / metabolism
Citations
This article has been cited 6 times.- Kim JS, Lee YH, Choi DY, Yi HK. Expression of Heat Shock Proteins (HSPs) in Aged Skeletal Muscles Depends on the Frequency and Duration of Exercise Training. J Sports Sci Med 2015 Jun;14(2):347-53.
- Rodriguez-Miguelez P, Fernandez-Gonzalo R, Almar M, Mejías Y, Rivas A, de Paz JA, Cuevas MJ, González-Gallego J. Role of Toll-like receptor 2 and 4 signaling pathways on the inflammatory response to resistance training in elderly subjects. Age (Dordr) 2014;36(6):9734.
- Powers SK, Ji LL, Kavazis AN, Jackson MJ. Reactive oxygen species: impact on skeletal muscle. Compr Physiol 2011 Apr;1(2):941-69.
- Touchberry CD, Gupte AA, Bomhoff GL, Graham ZA, Geiger PC, Gallagher PM. Acute heat stress prior to downhill running may enhance skeletal muscle remodeling. Cell Stress Chaperones 2012 Nov;17(6):693-705.
- Hu S, Ying Z, Gomez-Pinilla F, Frautschy SA. Exercise can increase small heat shock proteins (sHSP) and pre- and post-synaptic proteins in the hippocampus. Brain Res 2009 Jan 16;1249:191-201.
- Bao E, Sultan KR, Nowak B, Hartung J. Expression and distribution of heat shock proteins in the heart of transported pigs. Cell Stress Chaperones 2008 Dec;13(4):459-66.
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