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Molecular biology reports2010; 38(1); 461-469; doi: 10.1007/s11033-010-0129-8

Molecular characterization of glycogen synthase 1 and its tissue expression profile with type II hexokinase and muscle-type phosphofructokinase in horses.

Abstract: Muscle glycogen synthase (GYS1) is the rate-limiting enzyme in glycogen synthesis, and its activity is regulated by the phosphorylation states of certain amino acid residues encoded by the GYS1 gene. In the present study, the authors molecularly characterized the full-length equine GYS1 (eGYS1) cDNA and found that it contains a less common polyadenylation signal (AATACA). An amino acid alignment with other mammalian GYS1 showed that the phosphorylation sites in eGYS1 are completely conserved. Genomic DNA analysis revealed that the equine-specific substitutions (Glu 16 Asp and Ala 252 Thr) were completely conserved among six equine species. The tissue expression profiles of eGYS1, equine type II hexokinase (eHKII) and muscle-type phosphofructokinase (ePFKM) were determined by real-time PCR and western blot analysis. The mRNA expression level of eGYS1 was significantly higher in the cervical muscle as compared to other tissues. The cervical muscle and heart tissue samples contained a broad range of eGYS1 protein bands that appeared to reflect multiple phosphorylation states. eHKII was predominately expressed only in the cervical muscle; unlike its expression in other mammals, eHKII was not substantially expressed in the insulin-responsive heart or adipose tissue of horse. The expression level of ePFKM mRNA was significantly higher in the heart than in the cervical muscle, which differs from the PFKM expression pattern of other mammals. These tissue expression profiles are fundamental for the understanding of equine glucose metabolism.
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Publication Date: 2010-04-11 PubMed ID: 20383748DOI: 10.1007/s11033-010-0129-8Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article talks about the molecular characterization of a specific gene called glycogen synthase 1 (GYS1) in horses. The research identifies the way this gene behaves and its importance in understanding the metabolism of glucose in equine species.

Understanding the Role of eGYS1

  • The research looks at the full-length cGYS1, identifying how it behaves in different ways. Molecularly, the gene contains a less common polyadenylation signal (AATACA).
  • The eGYS1 gene is found to be conserved or similar in structure across different mammalian species. The study identifies that the phosphorylation sites in eGYS1 are completely conserved.
  • The research also analyzes the DNA of this gene. The equine-specific substitutions (Glu 16 Asp and Ala 252 Thr) were found to be completely unchanged across six equine species.

Tissue Expression Profiles of eGYS1, eHKII, and ePFKM

  • The team determined the tissue expression profiles of eGYS1 alongside equine type II hexokinase (eHKII) and muscle-type phosphofructokinase (ePFKM) through the use of real-time PCR and western blot analysis.
  • eGYS1 mRNA’s expression rate was significantly higher in the cervical muscle compared to other tissues, indicating its relevance to equine muscle functionality.
  • eHKII, on the other hand, was predominantly expressed in the cervical muscle. This divergence from other mammals, where eHKII is substantially expressed in insulin-responsive heart or adipose tissue, highlights unique aspects of equine biology.
  • ePFKM mRNA’s expression rate differed depending on the tissue. Despite being higher in the heart than in the cervical muscle, the ePFKM mRNA expression pattern manifested in horses in contrast to what is typically observed in other mammals.

Significance of the Findings

  • This research provides important insight into equine glucose metabolism, a crucial factor in understanding equine health and muscle performance.
  • Understanding the molecular characterization and tissue expression profiles of eGYS1, eHKII, and ePFKM allows for better comparison across species and may help to improve veterinary treatments and performance-related practices in horses.

Cite This Article

APA
Echigoya Y, Okabe H, Itou T, Endo H, Sakai T. (2010). Molecular characterization of glycogen synthase 1 and its tissue expression profile with type II hexokinase and muscle-type phosphofructokinase in horses. Mol Biol Rep, 38(1), 461-469. https://doi.org/10.1007/s11033-010-0129-8

Publication

Molecular biology reports
ISSN: 1573-4978
NlmUniqueID: 0403234
Country: Netherlands
Language: English
Volume: 38
Issue: 1
Pages: 461-469

Researcher Affiliations

Echigoya, Yusuke
  • Nihon University Veterinary Research Center, 1866 Kameino, Fujisawa, Kanagawa, 252-8510, Japan.
Okabe, Hirotarou
    Itou, Takuya
      Endo, Hideki
        Sakai, Takeo

          MeSH Terms

          • Animals
          • Blotting, Western
          • Breeding
          • Exons / genetics
          • Gene Expression Profiling
          • Gene Expression Regulation
          • Genome / genetics
          • Glycogen Synthase / genetics
          • Glycogen Synthase / metabolism
          • Hexokinase / genetics
          • Hexokinase / metabolism
          • Horses / genetics
          • Organ Specificity / genetics
          • Phosphofructokinase-1, Muscle Type / genetics
          • Phosphofructokinase-1, Muscle Type / metabolism
          • RNA, Messenger / genetics
          • RNA, Messenger / metabolism
          • Sequence Analysis, DNA
          • Species Specificity

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          Citations

          This article has been cited 2 times.
          1. Austin MMP, Ivey JLZ, Shepherd EA, Myer PR. Methodologies to Identify Metabolic Pathway Differences Between Emaciated and Moderately Conditioned Horses: A Review of Multiple Gene Expression Techniques. Animals (Basel) 2025 Oct 10;15(20).
            doi: 10.3390/ani15202933pubmed: 41153862google scholar: lookup
          2. Ishaq AR, Younis T, Lin S, Usman M, Wang T, Chen ZS. Phosphofructokinase-1 in Cancer: A Promising Target for Diagnosis and Therapy. Recent Pat Anticancer Drug Discov 2025;20(5):667-680.
            doi: 10.2174/0115748928321372240813080131pubmed: 39171598google scholar: lookup
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