Cytochemical detection of receptors specific for N-linked oligosaccharides of glycoproteins in the membrane of the human spermatozoon and their distribution in the different zones of that membrane.

The horseradish peroxidase (HRP), a glycoprotein rich in mannose and N-acetylglucosamine residues has been used as a ligand to detect receptors for N-glycosidic linked oligosaccharides of glycoproteins in the human spermatozoon. Specific binding of HRP occurred to the membrane and the binding sites were visualized with 3,3'-diaminobenzidine-H2O2 (DAB-H2O2) reagent, and by fluorescence when the FITC-peroxidase was used. This specific binding was suppressed by alpha-D-methyl-mannoside and human chorionic gonadotropin, decreased by follicle stimulating and luteinizing hormones and slightly diminished by N-acetylglucosamine. The distribution of the N-linked oligosaccharide specific receptors for glycoproteins in the different zones of the membrane of the spermatozoon was determined by counting the spermatozoa labeled in those zones. The pattern of the distribution is similar to that found for N-linked oligosaccharides containing glycoproteins of the same membrane. The similarity of these distributions together with the general model for cell-to-cell recognition suggest that the sperm-egg interaction mechanism could consist of dual interactions by double binding receptors.