Differential expression of equine myosin heavy-chain mRNA and protein isoforms in a limb muscle.
Abstract: The horse is one of the few animals kept and bred for its athletic performance and is therefore an interesting model for human sports performance. The regulation of the development of equine locomotion in the first year of life, and the influence of early training on later performance, are largely unknown. The major structural protein in skeletal muscle, myosin heavy-chain (MyHC), is believed to be primarily transcriptionally controlled. To investigate the expression of the MyHC genes at the transcriptional level, we isolated cDNAs encoding the equine MyHC isoforms type 1 (slow), type 2a (fast oxidative), and type 2d/x (fast glycolytic). cDNAs encoding the 2b gene were not identified. The mRNA expression was compared to the protein expression on a fiber-to-fiber basis using in situ hybridization (non-radioactive) and immunohistochemistry. Marked differences were detected between the expression of MyHC transcripts and MyHC protein isoforms in adult equine gluteus medius muscle. Mismatches were primarily due to the presence of hybrid fibers expressing two fast (2ad) MyHC protein isoforms, but only one fast (mainly 2a) MyHC RNA isoform. This discrepancy was most likely not due to differential mRNA expression of myonuclei.
Publication Date: 2003-08-19 PubMed ID: 12923246DOI: 10.1177/002215540305100911Google Scholar: Lookup
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- Journal Article
Summary
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The study aims to examine the expression of myosin heavy-chain (MyHC) proteins and their corresponding genes in the skeletal muscle of horses. The research uncovers significant differences between the two, chiefly in fibers expressing multiple MyHC protein isoforms but only one complimentary messenger RNA (mRNA) isoform.
Research Background
- The horse, being bred particularly for athletic performance, is a useful animal model for studying sports performance in humans. This research particularly investigates the genetic factors that likely influence a horse’s motion development and performance.
- The study focuses on MyHC, the main structural protein found in skeletal muscle, as it is thought to be primarily controlled at the transcriptional level. The transcriptional level refers to the process by which a segment of DNA is copied into RNA by the enzyme RNA polymerase.
Methodology
- CDNA’s encoding three isoforms of equine MyHC (type 1, type 2a, and type 2d/x) were isolated. An isoform is any of several different forms of the same protein.
- The researchers compared the mRNA expression to the protein expression of these isolated MyHCs. This was done on a fiber-to-fiber basis, using in-situ hybridization (non-radioactive) and immunohistochemistry, both of which provide methods to visualize specific genes or proteins within tissues.
Research Findings
- Significant differences were found between the expression of MyHC transcripts (the copied mRNA) and MyHC protein isoforms. This discrepancy was observed mainly in hybrid fibers where two fast MyHC protein isoforms were expressed, but only one fast MyHC RNA isoform was present.
- The study did not identify cDNAs encoding the 2b gene, another isoform of the MyHC.
- The researchers concluded that the observed discrepancy in the MyHC expressions was likely not due to differential mRNA expression of myonuclei, i.e., the mRNA levels of the genes in muscle cells were not affected to cause differences in the protein levels.
Implications
- The findings highlight intricate genetic factors that might influence a horse’s athletic performance and provide insights for further research in human sports performance.
- This discrepancy between gene and protein isoforms suggests an additional level of complexity in protein expression regulation, likely beyond the transcriptional control.
Cite This Article
APA
Eizema K, van den Burg M, Kiri A, Dingboom EG, van Oudheusden H, Goldspink G, Weijs WA.
(2003).
Differential expression of equine myosin heavy-chain mRNA and protein isoforms in a limb muscle.
J Histochem Cytochem, 51(9), 1207-1216.
https://doi.org/10.1177/002215540305100911 Publication
Researcher Affiliations
- Department of Pathobiology, Division of Anatomy, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands. c.g.h.eizema@vet.uu.nl
MeSH Terms
- Amino Acid Sequence
- Animals
- Base Sequence
- Extremities
- Horses
- Immunohistochemistry
- In Situ Hybridization
- Molecular Sequence Data
- Muscle Fibers, Skeletal / metabolism
- Muscle, Skeletal / metabolism
- Myosin Heavy Chains / genetics
- Myosin Heavy Chains / metabolism
- Polymerase Chain Reaction
- Protein Isoforms / genetics
- Protein Isoforms / metabolism
- RNA, Messenger / metabolism
- Skeletal Muscle Myosins / genetics
- Skeletal Muscle Myosins / metabolism
Citations
This article has been cited 8 times.- Queeno SR, Sterner KN, O'Neill MC. Meta-analysis data of skeletal muscle slow fiber content across mammalian species.. Data Brief 2023 Oct;50:109520.
- Mahzabin T, Pillow JJ, Pinniger GJ, Bakker AJ, Noble PB, White RB, Karisnan K, Song Y. Influence of antenatal glucocorticoid on preterm lamb diaphragm.. Pediatr Res 2017 Sep;82(3):509-517.
- García Liñeiro JA, Graziotti GH, Rodríguez Menéndez JM, Ríos CM, Affricano NO, Victorica CL. Structural and functional characteristics of the thoracolumbar multifidus muscle in horses.. J Anat 2017 Mar;230(3):398-406.
- 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.
- Goyal R, Lister R, Leitzke A, Goyal D, Gheorghe CP, Longo LD. Antenatal maternal hypoxic stress: adaptations of the placental renin-angiotensin system in the mouse.. Placenta 2011 Feb;32(2):134-9.
- Resnicow DI, Deacon JC, Warrick HM, Spudich JA, Leinwand LA. Functional diversity among a family of human skeletal muscle myosin motors.. Proc Natl Acad Sci U S A 2010 Jan 19;107(3):1053-8.
- Brown AC, Hallouane D, Mawby WJ, Karet FE, Saleem MA, Howie AJ, Toye AM. RhCG is the major putative ammonia transporter expressed in the human kidney, and RhBG is not expressed at detectable levels.. Am J Physiol Renal Physiol 2009 Jun;296(6):F1279-90.
- 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.
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