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Research in veterinary science2000; 69(2); 113-118; doi: 10.1053/rvsc.2000.0398

Localization of the lectin reactive sites in adult and prepubertal horse testes.

Abstract: The testes of prepubertal and adult horses were investigated using 10 horseradish peroxidase conjugated lectins combined with sialidase digestion and potassium hydroxide treatment, to localise the oligosaccharide sequences of glycoconjugates during spermatid maturation. In adult animals, the lectins showed a variable affinity for spermatids and Sertoli cell apical extensions. Soybean agglutinin (SBA), peanut agglutinin (PNA), Ricinus communis agglutinin (RCA-I) and wheat germ agglutinin (WGA) bound to the acrosomal structures of spermatids, whereas Griffonia simplicifolia agglutinin (GSA-II) labelled these structures only during Golgi and cap phases. These results suggested that glycoproteins of mature acrosomes contain both N- and O-linked oligosaccharides and that these carbohydrate chains undergo modifications during spermiogenesis. Sialic acid residues were not detected throughout the acrosomal development. The lectin binding pattern of Sertoli cells was very similar to that of acrosome of spermatids during the maturation phase. In sexually immature horses, only the degenerated germinal cells and the Leydig cells showed reactivity towards lectins. The first cells reacted with SBA and Dolichos biflorus agglutinin (DBA), the latter with SBA, PNA, WGA, GSA-II, Canavalia ensiformis agglutinin (ConA), Lens culinaris agglutinin (LCA) and also with DBA after sialidase digestion.
Publication Date: 2000-10-06 PubMed ID: 11020360DOI: 10.1053/rvsc.2000.0398Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The article discusses a study exploring the locations of oligosaccharides sequences in the teses of prepubertal and adult horses during spermatid maturation by employing different horseradish peroxidase-conjugated lectins. The findings of the study suggest alterations in carbohydrate chains in proteins during spermiogenesis.

Methodology

  • The researchers used the testes from adult and prepubertal horses for the investigation.
  • They applied horseradish peroxidase-conjugated lectins in combination with sialidase digestion and potassium hydroxide treatment.
  • The purpose was to identify and locate the oligosaccharide sequences in glycoconjugates during the development of spermatids into sperm cells, a process called spermatogenesis.
  • The lectins employed in the research included Soybean agglutinin (SBA), peanut agglutinin (PNA), Ricinus communis agglutinin (RCA-I), wheat germ agglutinin (WGA), and Griffonia simplicifolia agglutinin (GSA-II).

Findings

  • The lectins displayed an inconsistent affinity for spermatids and Sertoli cell’s apical extensions in adult animals.
  • Lectins like SBA, PNA, RCA-I, and WGA bound to the acrosomal structure of spermatids. In contrast, GSA-II only labeled these structures during certain phases (the Golgi and cap phases).
  • This indicates that acrosomal proteins in adult horses contain both N- and O-linked oligosaccharides.
  • The research did not find sialic acid residues in any stage of acrosomal development. This supports the notion that these carbohydrate chains undergo modifications during spermiogenesis.
  • The lectin binding pattern in Sertoli cells was very similar to that of acrosome of spermatids during their maturation.

Prepubertal Findings

  • In sexually immature horses, only the degenerated germinal cells and the Leydig cells displayed reactivity towards the lectins.
  • The degenerated germinal cells reacted with SBA and Dolichos biflorus agglutinin (DBA).
  • Leydig cells reacted with SBA, PNA, WGA, GSA-II, Canavalia ensiformis agglutinin (ConA), Lens culinaris agglutinin (LCA) and also with DBA after sialidase digestion.

Conclusion

  • The study provides valuable insights into the changes that occur in the carbohydrate chains of acrosomal proteins during horse spermiogenesis.
  • The reactivity of lectins in prepubertal horses was limited to the degenerative germinal and Leydig cells only.
  • Further research is required to better understand the implications of these findings in the spermatogenic process and overall fertility in horses.

Cite This Article

APA
Verini-Supplizi A, Stradaioli G, Fagioli O, Parillo F. (2000). Localization of the lectin reactive sites in adult and prepubertal horse testes. Res Vet Sci, 69(2), 113-118. https://doi.org/10.1053/rvsc.2000.0398

Publication

ISSN: 0034-5288
NlmUniqueID: 0401300
Country: England
Language: English
Volume: 69
Issue: 2
Pages: 113-118

Researcher Affiliations

Verini-Supplizi, A
  • Centro di Studio del Cavallo Sportivo, Facoltà di Medicina Veterinaria, Università degli Studi di Perugia, Perugia, Italy. vete2@unipg.it
Stradaioli, G
    Fagioli, O
      Parillo, F

        MeSH Terms

        • Age Factors
        • Animals
        • Biomarkers
        • Castor Bean / chemistry
        • Horses
        • Hydroxides
        • Immunoenzyme Techniques / veterinary
        • Lectins / chemistry
        • Male
        • Neuraminidase / metabolism
        • Peanut Agglutinin / chemistry
        • Plant Lectins
        • Plants, Toxic
        • Potassium Compounds
        • Sexual Maturation
        • Soybean Proteins
        • Spermatids / chemistry
        • Spermatids / ultrastructure
        • Testis / chemistry
        • Testis / ultrastructure

        Citations

        This article has been cited 1 times.
        1. Costa GM, Avelar GF, Rezende-Neto JV, Campos-Junior PH, Lacerda SM, Andrade BS, Thomé RG, Hofmann MC, Franca LR. Spermatogonial stem cell markers and niche in equids.. PLoS One 2012;7(8):e44091.
          doi: 10.1371/journal.pone.0044091pubmed: 22937157google scholar: lookup