Histochemistry

, Volume 97, Issue 5, pp 439–449

Cytochemical characterization of glycoproteins in the developing acrosome of rats

An ultrastructural study using lectin histochemistry, enzymes and chemical deglycosylation

Authors

  • J. A. Martínez-Menárguez
    • Section of Histology and General Embryology, Department of Cell Biology, Medical SchoolUniversity of Murcia
  • J. Ballesta
    • Section of Histology and General Embryology, Department of Cell Biology, Medical SchoolUniversity of Murcia
  • M. Avilés
    • Section of Histology and General Embryology, Department of Cell Biology, Medical SchoolUniversity of Murcia
  • M. T. Castells
    • Section of Histology and General Embryology, Department of Cell Biology, Medical SchoolUniversity of Murcia
  • J. F. Madrid
    • Department of Cell Biology and Morphological Science, Medical SchoolUniversity of Pais Vasco
Article

DOI: 10.1007/BF00270391

Cite this article as:
Martínez-Menárguez, J.A., Ballesta, J., Avilés, M. et al. Histochemistry (1992) 97: 439. doi:10.1007/BF00270391

Summary

The composition and distribution of rat acrosomal glycoproteins during spermiogenesis have been investigated at light and electron microscopic level by means of a variety of morphological techniques including the application of lectins conjugated to peroxidase, digoxigenin and colloidal gold, enzyme and chemical deglycosylation procedures and conventional histochemistry. Results obtained with lectin histochemistry in combination with β-elimination reaction and endoglucosaminidase F/peptide N-glycosidase F digestion suggest that glycoproteins of mature acrosomes contain both N- and O-linked oligosaccharides. N-linked chains of acrosomal glycoproteins contain mannose and external residues of N-acetylglucosamine and galactose. They also have fucose residues linked to the core region of the oligosaccharide side chains. O-linked oligosaccharide chains contain external residues of both galactose and N-acetylgalactosamine. Mannose, fucose, galactose and N-acetylglucosamine residues were detected in acrosomes at all steps of spermiogenesis. N-acetylgalactosamine residues were only observed in the late steps of the spermiogenesis. N-acetylneuraminic acid residues were not detected throughout the acrosomal development. At initial stages of acrosome formation, glycoproteins were preferentially distributed over the acrosomic granules. In cap phase spermatids, lectin binding sites were homogeneously distributed throughout the acrosomes; however, in mature spermatozoa, glycoproteins were predominantly located over the outer acrosomal membrane.

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Copyright information

© Springer-Verlag 1992