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Differential expression of calcineurin and SR Ca2+ handling proteins in equine muscle fibers during early postnatal growth.

Abstract: During early postnatal development, the myosin heavy chain (MyHC) expression pattern in equine gluteus medius muscle shows adaptation to movement and load,resulting in a decrease in the number of fast MyHC fibers and an increase in the number of slow MyHC fibers. In the present study we correlated the expression of MyHC isoforms to the expression of sarcoplasmic(endo)reticulum Ca2+-ATPase 1 and 2a (SERCA), phospholamban (PLB), calcineurin A (CnA), and calcineurin B (CnB). Gluteus medius muscle biopsies were taken at 0, 2, 4, and 48 weeks and analyzed using immunofluorescence. Both SERCA isoforms and PLB were expressed in almost all fiber types at birth. From 4 weeks of age onward, SERCA1 was exclusively expressed in fast MyHC fibers and SERCA2a and PLB in slow MyHC fibers. At all time points, CnA and CnB proteins were expressed at a basal level in all fibers, but with a higher expression level in MyHC type 1 fibers. From 4 weeks onward, expression of only CnA was also higher in MyHC type 2a and 2ad fibers. We propose a double function of calcineurin in calcium homeostasis and maintenance of slow MyHC fiber type identity. Although equine muscle is already functional at birth, expression patterns of the monitored proteins still show adaptation, depending on the MyHC fiber type.
Publication Date: 2006-11-13 PubMed ID: 17101725DOI: 10.1369/jhc.6A7039.2006Google Scholar: Lookup
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  • Journal Article

Summary

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The research article discusses the changes in muscle fibers in horses during early postnatal growth and how calcineurin and various calcium handling proteins play a role in this process.

Overview of the Study

  • The research focused on the changes happening in the gluteus medius muscle of young horses after birth. The term ‘postnatal’ refers to the period of time following the birth of an organism.
  • The researchers observed a decrease in the number of fast myosin heavy chain (MyHC) fibers and an increase in the number of slow MyHC fibers. MyHC is a type of protein that plays a fundamental role in muscle contraction. ‘Fast’ and ‘slow’ fibers refer to their contraction speed and endurance.
  • The study aimed to provide a correlation between these changes and the expression of various proteins, namely, Sarcoplasmic(endo)reticulum Ca2+ – ATPase 1 and 2a (SERCA 1 and 2a), phospholamban (PLB), calcineurin A (CnA), and calcineurin B (CnB).

Experimental Details

  • Biopsies were taken from the gluteus medius muscle of horses at 0, 2, 4, and 48 weeks after birth. These samples were then analyzed using immunofluorescence, a technique that uses antibodies to tag specific proteins so they can be visualized under a microscope.
  • At birth, almost all fiber types expressed both SERCA isoforms and PLB. As the horses grew older, SERCA1 was primarily found in fast MyHC fibers, while SERCA2a and PLB were mainly in slow MyHC fibers.
  • The two types of calcineurin proteins – CnA and CnB – were expressed at basal levels in all fibers at every time point, although they were more prominent in the type 1 MyHC fibers. However, after 4 weeks, only CnA expression was found to be higher in MyHC types 2a and 2ad fibers.

Interpretation and Conclusions

  • The researchers surmised that calcineurin plays a dual role – regulating calcium homeostasis (the balance of calcium in the body) and maintaining the slow MyHC fiber type identity.
  • Although equine muscle is functional at birth, the expression patterns of these proteins still underwent changes, depending on the MyHC fiber type.
  • In conclusion, this study indicates how integral these calcium handling proteins and calcineurin are for the development of equine muscle post-birth and the potential changes in fiber types during early growth.

Cite This Article

APA
Eizema K, van der Wal DE, van den Burg MM, de Jonge HW, Everts ME. (2006). Differential expression of calcineurin and SR Ca2+ handling proteins in equine muscle fibers during early postnatal growth. J Histochem Cytochem, 55(3), 247-254. https://doi.org/10.1369/jhc.6A7039.2006

Publication

ISSN: 0022-1554
NlmUniqueID: 9815334
Country: United States
Language: English
Volume: 55
Issue: 3
Pages: 247-254

Researcher Affiliations

Eizema, Karin
  • Department of Pathobiology, Division of Anatomy and Physiology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.158, NL-3508 TD, Utrecht, The Netherlands. c.g.h.eizema@vet.uu.nl
van der Wal, Dianne E
    van den Burg, Maarten M M
      de Jonge, Henriëtte W
        Everts, Maria E

          MeSH Terms

          • Animals
          • Calcineurin / biosynthesis
          • Calcium / metabolism
          • Calcium-Binding Proteins / biosynthesis
          • Fluorescent Antibody Technique
          • Horses
          • Muscle Fibers, Skeletal / metabolism
          • Muscle, Skeletal / growth & development
          • Muscle, Skeletal / metabolism
          • Myosin Heavy Chains / biosynthesis
          • Protein Isoforms / biosynthesis
          • Protein Subunits / metabolism
          • Sarcoplasmic Reticulum / metabolism
          • Sarcoplasmic Reticulum Calcium-Transporting ATPases / biosynthesis

          Citations

          This article has been cited 1 times.
          1. Pae EK. Response of masticatory muscles to passive stretch stimulus - from perspectives of functional appliances.. Korean J Orthod 2012 Apr;42(2):64-72.
            doi: 10.4041/kjod.2012.42.2.64pubmed: 23112934google scholar: lookup