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Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology1997; 117(4); 531-534; doi: 10.1016/s0305-0491(97)00213-7

Hydrolysis of extracellular adenine nucleotides by equine epidydimal spermatozoa.

Abstract: Ectoenzymic activities capable of hydrolyzing ATP sequentially to adenosine are present on equine epidydimal spermatozoa membranes. Kinetic parameters for ATPase, ADPase and 5'-nucleotidase were obtained by analysis of progress reactions curve when ATP, ADP and AMP were supplied as initial substrates. These values are not different from those found when the substrates were supplied from the preceding reactions. Feed-forward inhibition on 5'-nucleotidase by ATP/ADP was taken into account to fit simulated data to the experimental results. None of the substrates supplied by the preceding reactions showed a preferential delivery to ADPase and/or 5'-nucleotidase. We therefore conclude that the model that fits the equine spermatozoa is that already proposed for pig aortic endothelial cells.
Publication Date: 1997-08-01 PubMed ID: 9297797DOI: 10.1016/s0305-0491(97)00213-7Google Scholar: Lookup
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Summary

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The study examines the ability of enzymes present on the membranes of horse epidydimal sperm cells to break down ATP (adenosine triphosphate) into adenosine. The researchers determined that these enzymatic activities and their behaviours do not differ when the substrates were offered by preceding reactions, leading them to adopt a model previously proposed for pig aortic endothelial cells.

Study background and methods

  • This study focuses on the functioning of specific enzymes, known as ectoenzymes, on the membranes of equine (horse) epidydimal spermatozoa (sperm cells).
  • These ectoenzymes are capable of hydrolyzing ATP, which is a molecule that serves as the main source of energy for cellular reactions. Hydrolyzing ATP means breaking it down into simpler compounds.
  • The enzymatic activities examined in this study include ATPase, ADPase, and 5′-nucleotidase. Each of these enzymes plays a role in the sequential hydrolysis of ATP to adenosine.
  • By using a process known as kinetic parameter analysis, the researchers determined the reaction rates of these enzymes when ATP, ADP (adenosine diphosphate), and AMP (adenosine monophosphate) were supplied as initial substrates, or starting materials.

Findings and implications

  • The results show that the kinetic parameters, or reaction rates, of these enzymes are not different when the substrates (ATP, ADP, AMP) are supplied from the preceding reactions.
  • Further analysis reveals a feed-forward inhibition on 5′-nucleotidase by ATP and ADP. This is when the production of a product (in this case, ATP or ADP) inhibits the reactions that produce it (5′-nucleotidase in this case).
  • This study also suggests that no preferential delivery of substrates to ADPase and/or 5′-nucleotidase occurred when those substrates were supplied by preceding reactions.
  • These findings lead the researchers to conclude that the model that best represents these enzymatic processes on equine spermatozoa is the one proposed for pig aortic endothelial cells.

Overall significance

  • This study enhances our understanding of enzymatic activities on equine sperm cell membranes and their influence on ATP hydrolysis. The findings could potentially be applied to further research in related fields like animal reproduction and biochemistry.
  • The conclusion that a model used to describe similar enzymatic processes in a different cell type (pig aortic endothelial cells) applies to horse sperm cells might be a step towards a broader, more unified understanding of these cellular processes across species.

Cite This Article

APA
Minelli A, Moroni M, Trinari D, Mezzasoma I. (1997). Hydrolysis of extracellular adenine nucleotides by equine epidydimal spermatozoa. Comp Biochem Physiol B Biochem Mol Biol, 117(4), 531-534. https://doi.org/10.1016/s0305-0491(97)00213-7

Publication

ISSN: 1096-4959
NlmUniqueID: 9516061
Country: England
Language: English
Volume: 117
Issue: 4
Pages: 531-534

Researcher Affiliations

Minelli, A
  • Department of Cellular and Molecular Biology, University of Perugia, Italy.
Moroni, M
    Trinari, D
      Mezzasoma, I

        MeSH Terms

        • Adenine / chemistry
        • Adenine / metabolism
        • Adenosine / metabolism
        • Adenosine / pharmacokinetics
        • Adenosine Diphosphate / metabolism
        • Adenosine Monophosphate / metabolism
        • Adenosine Triphosphatases / metabolism
        • Adenosine Triphosphate / metabolism
        • Animals
        • Apyrase / metabolism
        • Epididymis
        • Horses
        • Hydrolysis
        • Kinetics
        • Male
        • Nucleotidases / metabolism
        • Nucleotides / chemistry
        • Nucleotides / metabolism
        • Spermatozoa / chemistry
        • Spermatozoa / metabolism
        • Time Factors

        Citations

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