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Changes in the plasma membrane proteins of stallion spermatozoa during maturation in the epididymis.

Abstract: The present paper reports modifications in the electrophoretic and cytochemical characteristics of mature and immature stallion spermatozoa. Some sperm surface glycoproteins (36, 32, 29, 21, 20, 18 kDa) detected in cauda epididymidis spermatozoa, were either absent or present in a very low relative concentration in immature sperm cells. A major 14 kDa protein band, observed in sperm extracts obtained from ductus efferentes, progressively decreased along the epididymal ductus. The nature and distribution of carbohydrate residues on the sperm membrane, during epididymal maturation, was also studied by use of lectin probes. Some protein bands bound concanavalin A while others, as the 36, 32 and 20 kDa proteins, exhibited higher affinity for WGA lectin. The distribution and relative density of mannose-, galactose-, N-acetylglucosamine-, N-acetylgalactosamine-, fucose- and sialic acid-containing macromolecules showed a characteristic pattern depending on the sperm membrane domain and on its origin. Some sperm surface domains displayed affinity for more than one lectin, indicating a diversity in their exposed carbohydrate residues, whereas others bound only one or no lectin. The passage of spermatozoa through the epididymidis was accompanied by changes in the accessibility or abundance of lectin ligands. Some lectins (UEA, WGA, LPA) gave stronger reaction in mature spermatozoa, while others (RCA, WFH, PNA) stained better immature spermatozoa. This remodeling of sperm surface molecules is probably a consequence of interactions between spermatozoa and the epididymal secretions, and may reflect addition or adsorption of new molecules, space configurations changes or biochemical modifications of pre-existing compounds. Our results suggest that the distribution and density of terminal oligosaccharidic residues on the sperm plasma membrane have species-specific characteristics. These post testicular developmental changes may be of significance in the overall understanding of the stallion fertility.
Publication Date: 2000-11-21 PubMed ID: 11085212
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research article discusses the changes in proteins of stallion spermatozoa during maturation in the epididymis. It focuses specifically on how sperm surface glycoproteins and the nature and distribution of carbohydrate residues on the sperm membrane alter through this process.

Electrophoretic and Cytochemical Characteristics

  • The scientists observed modifications in the electrophoretic and cytochemical characteristics of mature and immature stallion spermatozoa. This led them to identify specific sperm surface glycoproteins that are either absent or appear in very low relative concentration in immature sperm cells but can be detected in mature sperm cells from the cauda epididymidis.
  • A predominant 14 kDa protein band found in sperm extracts from the ductus efferentes showed a progressive decrease as it moved along the epididymal ductus.

Study of Carbohydrate Residues

  • The nature and distribution of carbohydrate residues on the sperm membrane during epididymal maturation was also examined using lectin probes.
  • The scientists found that while certain protein bands were able to bind to concanavalin A, others showed a higher affinity for WGA lectin.
  • The distribution and relative density of specific carbohydrate-containing macromolecules displayed a characteristic pattern based on the sperm membrane domain and origin.

Sperm Surface Domains

  • Some sperm surface domains showed affinity for more than one lectin, indicating diversity in the exposed carbohydrate residues. However, others were found to bind only one or no lectin.
  • As spermatozoa passed through the epididymidis, changes were noted in the accessibility or abundance of lectin ligands. Certain lectins gave stronger reactions in mature spermatozoa, while others stained immature spermatozoa more effectively.

Consequence of Interactions

  • The researchers suggest that these modifications to sperm surface molecules likely result from interactions between the spermatozoa and epididymal secretions. This could indicate the addition or adsorption of new molecules, changes in space configurations, or biochemical modifications of existing compounds.
  • These findings imply that the distribution and density of terminal oligosaccharidic residues on the sperm plasma membrane could have species-specific characteristics.

Significance in Stallion Fertility

  • The study concludes that understanding these post-testicular developmental changes could have significant implications for better comprehending the fertility of stallions.

Cite This Article

APA
Retamal C, Urzúa J, Lorca C, López ML, Alves EW. (2000). Changes in the plasma membrane proteins of stallion spermatozoa during maturation in the epididymis. J Submicrosc Cytol Pathol, 32(2), 229-239.

Publication

ISSN: 1122-9497
NlmUniqueID: 8804312
Country: Italy
Language: English
Volume: 32
Issue: 2
Pages: 229-239

Researcher Affiliations

Retamal, C
  • Faculty of Medicine, University of Chile, Santiago.
Urzúa, J
    Lorca, C
      López, M L
        Alves, E W

          MeSH Terms

          • Animals
          • Cell Differentiation
          • Epididymis / cytology
          • Epididymis / metabolism
          • Horses
          • Male
          • Membrane Proteins / metabolism
          • Spermatogenesis
          • Spermatozoa / cytology
          • Spermatozoa / metabolism

          Citations

          This article has been cited 2 times.
          1. Orsolini MF, Meyers SA, Dini P. An Update on Semen Physiology, Technologies, and Selection Techniques for the Advancement of In Vitro Equine Embryo Production: Section I. Animals (Basel) 2021 Nov 13;11(11).
            doi: 10.3390/ani11113248pubmed: 34827983google scholar: lookup
          2. Gervasi MG, Visconti PE. Molecular changes and signaling events occurring in spermatozoa during epididymal maturation. Andrology 2017 Mar;5(2):204-218.
            doi: 10.1111/andr.12320pubmed: 28297559google scholar: lookup