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Experimental physiology2008; 94(1); 117-129; doi: 10.1113/expphysiol.2008.043877

Myonuclear domain size and myosin isoform expression in muscle fibres from mammals representing a 100,000-fold difference in body size.

Abstract: This comparative study of myonuclear domain (MND) size in mammalian species representing a 100,000-fold difference in body mass, ranging from 25 g to 2500 kg, was undertaken to improve our understanding of myonuclear organization in skeletal muscle fibres. Myonuclear domain size was calculated from three-dimensional reconstructions in a total of 235 single muscle fibre segments at a fixed sarcomere length. Irrespective of species, the largest MND size was observed in muscle fibres expressing fast myosin heavy chain (MyHC) isoforms, but in the two smallest mammalian species studied (mouse and rat), MND size was not larger in the fast-twitch fibres expressing the IIA MyHC isofom than in the slow-twitch type I fibres. In the larger mammals, the type I fibres always had the smallest average MND size, but contrary to mouse and rat muscles, type IIA fibres had lower mitochondrial enzyme activities than type I fibres. Myonuclear domain size was highly dependent on body mass in the two muscle fibre types expressed in all species, i.e. types I and IIA. Myonuclear domain size increased in muscle fibres expressing both the beta/slow (type I; r = 0.84, P < 0.001) and the fast IIA MyHC isoform (r = 0.90; P < 0.001). Thus, MND size scales with body size and is highly dependent on muscle fibre type, independent of species. However, myosin isoform expression is not the sole protein determining MND size, and other protein systems, such as mitochondrial proteins, may be equally or more important determinants of MND size.
Publication Date: 2008-09-26 PubMed ID: 18820003DOI: 10.1113/expphysiol.2008.043877Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • N.I.H.
  • Extramural
  • Research Support
  • Non-U.S. Gov't

Summary

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This research analyzes the size of the myonuclear domain (MND) in the muscle fibers of mammals, considering a wide span of animal sizes. The study reveals that MND size scales with body size and is heavily influenced by muscle fiber type, regardless of the species, although it’s not solely determined by myosin isoform expression.

Understanding the Research

  • The researchers compared the size of the myonuclear domain (MND) in muscle fibers from various mammals. This was a comparative examination involving mammals ranging in body mass from 25 grams to 2500 kilograms – a significant variation in size.
  • The MND size was calculated from three-dimensional reconstructions of 235 single muscle fiber segments at a specific sarcomere length. Sarcomeres are the basic unit of muscle tissue.
  • Myosin heavy chain (MyHC) isoforms are the motor proteins in muscle cells responsible for muscle contraction. The researchers observed the highest MND sizes in muscle fibers expressing fast MyHC isoforms. However, in smaller mammals (like mice and rats), the MND size in fast-twitch muscle fibers expressing the IIA MyHC isoform was not larger than in the slow-twitch type I fibers.

Findings of the Study

  • In larger mammals, type-I fibers (slow-twitch fibers) usually had the smallest average MND size. Interestingly, contrary to what was observed in smaller mammals, type IIA fibers (fast-twitch fibers) in larger mammals had lower mitochondrial enzyme activities than type I fibers.
  • MND size was highly related to body mass in both muscle fiber types (types I and IIA) present in all the studied species. The MND size increased in muscle fibers expressing both the beta/slow (type I) and the fast IIA MyHC isoforms.
  • The research concluded that MND size scales with body size and varies strongly with muscle fiber type, irrespective of the species. Nonetheless, myosin isoform expression alone does not determine MND size; other protein systems like mitochondrial proteins may equally or potentially more significantly influence MND size.

Cite This Article

APA
Liu JX, Höglund AS, Karlsson P, Lindblad J, Qaisar R, Aare S, Bengtsson E, Larsson L. (2008). Myonuclear domain size and myosin isoform expression in muscle fibres from mammals representing a 100,000-fold difference in body size. Exp Physiol, 94(1), 117-129. https://doi.org/10.1113/expphysiol.2008.043877

Publication

ISSN: 1469-445X
NlmUniqueID: 9002940
Country: England
Language: English
Volume: 94
Issue: 1
Pages: 117-129

Researcher Affiliations

Liu, Jing-Xia
  • Department of Neurosciences, Uppsala University, Uppsala, Sweden.
Höglund, Anna-Stina
    Karlsson, Patrick
      Lindblad, Joakim
        Qaisar, Rizwan
          Aare, Sudhakar
            Bengtsson, Ewert
              Larsson, Lars

                MeSH Terms

                • Animals
                • Body Mass Index
                • Body Size / physiology
                • DNA / metabolism
                • Female
                • Horses
                • Humans
                • Male
                • Mice
                • Mice, Inbred C57BL
                • Muscle Fibers, Fast-Twitch / metabolism
                • Muscle Fibers, Slow-Twitch / metabolism
                • Myosin Heavy Chains / metabolism
                • Perissodactyla
                • Protein Isoforms / metabolism
                • Rats
                • Rats, Sprague-Dawley
                • Species Specificity
                • Swine
                • Young Adult

                Grant Funding

                • AR 47318 / NIAMS NIH HHS

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