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Zoological science2004; 21(5); 589-596; doi: 10.2108/zsj.21.589

Absence of the functional Myosin heavy chain 2b isoform in equine skeletal muscles.

Abstract: Nucleotide sequences which included the full coding region for three types of myosin heavy chain (MyHC) isoforms were determined from equine skeletal muscles. The deduced amino acid sequences were 1937, 1938, and 1935 residues for the MyHC-2a, -2x, and -slow, respectively. No MyHC-2b isoform was amplified from the equine muscle cDNA except for one pseudogene fragment. One nucleotide was inserted in the coding region of the equine pseudogene product, a minute amount of which was expressed in the skeletal muscle. The 596 bp sequence of the equine MyHC pseudogene was categorized into the MyHC-2b genes on the phylogenetic tree of the mammalian MyHC genes. These results suggest that an ancestral MyHC-2b gene had lost its function and changed to a pseudogene during the course of horse history. The MyHC genes in some ungulates were analyzed through the PCR amplifications using the MyHC isoform-specific primers to confirm the presence of the MyHC-2b and -2x genes. The exon coding the 3' untranslated region of the MyHC-2x was successfully amplified from the all ungulates examined; however, that of the MyHC-2b gene was amplified only from horses, pigs and lesser mouse deer. The PCR analyses from rhinoceros, sika deer, moose, giraffes, water buffalo, bovine, Japanese serow and sheep genes implied the absence of the MyHC-2b-specific sequence in their genomes. These results suggest that the MyHC-2b gene independently lost its function in some ungulate species.
Publication Date: 2004-06-01 PubMed ID: 15170063DOI: 10.2108/zsj.21.589Google Scholar: Lookup
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  • Comparative Study
  • Journal Article

Summary

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The research article investigates the absence of the Myosin heavy chain (MyHC) 2b isoform in equine skeletal muscles, implying that the MyHC-2b gene lost its function in horses and some other ungulate species during evolution.

Methodology

The researchers conducted a study on equine skeletal muscles’ nucleotide sequences, determining the full coding regions for three types of myosin heavy chain (MyHC) isoforms. They sought MyHC-2a, -2x, and -slow, specific genes that produce proteins responsible for muscle contraction. The researchers then analyzed the results using PCR amplifications and specific primers to confirm the presence of the MyHC-2b and -2x genes.

  • PCR (polymerase chain reaction) is a laboratory method used to make millions of copies of a specific DNA segment in order to analyze it more easily.
  • Primers are short pieces of DNA that serve as a starting point for DNA synthesis, crucial to the PCR process.

Findings

The research revealed that there was no amplification of the MyHC-2b isoform from the equine muscle cDNA except for a pseudogene fragment. A pseudogene is a DNA sequence that resembles a gene but has been mutated and, as a result, does not function as regular genes do.

  • In this case, the pseudogene had one inserted nucleotide in its coding region, with only a small amount expressing in the skeletal muscle.
  • This pseudogene’s sequence was categorized into the MyHC-2b genes on the phylogenetic tree, linking it to evolutionary relationships among species.

The results from the PCR analyses of other ungulates (hoofed mammals) like rhinoceros, sika deer, moose, giraffes, water buffalo, bovine, Japanese serow, and sheep indicated an absence of the MyHC-2b-specific sequence in their genomes.

Conclusion

The findings suggest the absence of the functional MyHC-2b isoform in equine skeletal muscles and in some other ungulate species. This indicates that the MyHC-2b gene may have independently lost its function over evolutionary history. The reason behind this genetic loss and the potential impacts on the species’ muscle function, however, was not explained and might require further investigation.

Cite This Article

APA
Chikuni K, Muroya S, Nakajima I. (2004). Absence of the functional Myosin heavy chain 2b isoform in equine skeletal muscles. Zoolog Sci, 21(5), 589-596. https://doi.org/10.2108/zsj.21.589

Publication

ISSN: 0289-0003
NlmUniqueID: 8702287
Country: Japan
Language: English
Volume: 21
Issue: 5
Pages: 589-596

Researcher Affiliations

Chikuni, Koichi
  • Meat Science Laboratory, National Institute of Livestock and Grassland Science, Tsukuba, Ibaraki, Japan. chikuni@affrc.go.jp
Muroya, Susumu
    Nakajima, Ikuyo

      MeSH Terms

      • Amino Acid Sequence
      • Animals
      • Base Sequence
      • DNA Primers
      • DNA, Complementary / genetics
      • Horses / genetics
      • Horses / metabolism
      • Molecular Sequence Data
      • Muscle, Skeletal / metabolism
      • Myosin Heavy Chains / genetics
      • Myosin Heavy Chains / metabolism
      • Phylogeny
      • Pseudogenes / genetics
      • Sequence Alignment
      • Sequence Analysis, DNA

      Citations

      This article has been cited 6 times.
      1. Hoh JFY. Developmental, physiologic and phylogenetic perspectives on the expression and regulation of myosin heavy chains in mammalian skeletal muscles.. J Comp Physiol B 2023 Aug;193(4):355-382.
        doi: 10.1007/s00360-023-01499-0pubmed: 37277594google scholar: lookup
      2. Wu X, Zhou X, Ding X, Chu M, Liang C, Pei J, Xiong L, Bao P, Guo X, Yan P. Reference gene selection and myosin heavy chain (MyHC) isoform expression in muscle tissues of domestic yak (Bos grunniens).. PLoS One 2020;15(2):e0228493.
        doi: 10.1371/journal.pone.0228493pubmed: 32027673google scholar: lookup
      3. Knych HK, Harrison LM, Steinmetz SJ, Chouicha N, Kass PH. Differential expression of skeletal muscle genes following administration of clenbuterol to exercised horses.. BMC Genomics 2016 Aug 9;17:596.
        doi: 10.1186/s12864-016-2945-2pubmed: 27506674google scholar: lookup
      4. Butcher MT, Chase PB, Hermanson JW, Clark AN, Brunet NM, Bertram JE. Contractile properties of muscle fibers from the deep and superficial digital flexors of horses.. Am J Physiol Regul Integr Comp Physiol 2010 Oct;299(4):R996-R1005.
        doi: 10.1152/ajpregu.00510.2009pubmed: 20702801google scholar: lookup
      5. Moreno-Sánchez N, Díaz C, Carabaño MJ, Rueda J, Rivero JL. A comprehensive characterisation of the fibre composition and properties of a limb (flexor digitorum superficialis, membri thoraci) and a trunk (psoas major) muscle in cattle.. BMC Cell Biol 2008 Dec 15;9:67.
        doi: 10.1186/1471-2121-9-67pubmed: 19077313google scholar: lookup
      6. Hayashi S, Miyake M, Watanabe K, Aso H, Hayashi S, Ohwada S, Yamaguchi T. Myostatin preferentially down-regulates the expression of fast 2x myosin heavy chain in cattle.. Proc Jpn Acad Ser B Phys Biol Sci 2008;84(8):354-62.
        doi: 10.2183/pjab.84.354pubmed: 18941308google scholar: lookup