Immunoserological, immunohistochemical and immunobiological studies on an antigenic glycoprotein isolated from human seminal plasma

Cerezo, Josefina M.S. De; Bueno, María P.; Skowroñski, B.; Cerezo, Alberto S.

doi:10.1016/0165-0378(82)90019-5

Cited by 5 publications

(1 citation statement)

References 15 publications

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“…All these terminal groups (not the N-acety 1-13-D-glucosamine) have been determined in fractions of the seminal plasma. 4,5,[28][29][30] The blood group activities A and B indicate the presence of the following antigenic determinants: a) N-acetyl-a-D-galactosaminyl-…”

Section: Csmentioning

confidence: 99%

The Antigenic Mucin‐Like Glycoproteins of Human Seminal Plasma*

Tortorella

Josefina²,

Cerezo³

et al. 1983

American Journal of Reproductive Immunology

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Immunodiffusion, immunoelectrophoresis, SDS-polyacrylamide gel electrophoresis, polyacrylamide gel electrophoresis, ultracentrifugation analysis, and gel permeation chromatography in chaotropic and detergent mediums showed that the human seminal plasma obtained and stored in the usual way is mainly composed by heterodispersed glycoproteins of low molecular weight. The glycoprotein components of the human seminal plasma which do not interact specifically with concanavalin A (con A) were separated by column chromatography on Con A-Sepharose according to nonspecific ion exchange and hydrophobic interactions with the protein. The carbohydrate composition of the glycoproteins and the existence of the N-acetylgalactosaminylserine (or threonine) linkage, as well as their aggregation properties show that they are mucin-type glycoproteins. They resulted "immunologically pure" although the carbohydrate chains show the structural heterodispersion usually found in mucins. The glycoproteins have a common structural pattern for the terminal nonreducing, determinant-bearing sequences of their oligosaccharide chains which, together with the low molecular weights and the known fact that mucus secretions of normal cells contain only one or two types of glycoproteins, suggest that they are fragments produced by endogenous proteolytic degradation of a native mucin.

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Section: Csmentioning

confidence: 99%

The Antigenic Mucin‐Like Glycoproteins of Human Seminal Plasma*

Tortorella

Josefina²,

Cerezo³

et al. 1983

American Journal of Reproductive Immunology

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Immunohistochemical Localization of Concanavalin A and Wheat Germ Lectin Receptors in the Normal Human Spermatozoa*

Cerezo¹,

Bueno²,

Skowronki³

et al. 1982

American Journal of Reproductive Immunology

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A semiquantitative immunohistochemical technique for the detection of N‐acetyl α‐D‐neuraminic acid, N‐acetyl β‐D‐glucosamine and its β‐(1 ŕ 4)‐linked internal chains, α‐D‐glucopyranosyl and α‐D‐mannopyranosyl and its α‐(1 ŕ 2)‐linked internal chains and sterically related, nonreducing, end‐chain residues of oligosaccharide chains of glycoproteins or glycolipids on the surface of membranes was developed using Con A and wheat germ lectins.When this method was applied to the localization of carbohydrate receptors on the membrane of the normal human spermatozoa, it was found that the Con A and wheat germ lectin receptors were mainly located in the equatorial and post nuclear cap with few receptors located in the acrosome and neck. None of them were found in the intermediate segment plus tail.Con A receptors were α‐D‐mannopyranosyl end‐chain residues and wheat germ lectin receptors were N‐acetyl β‐D‐glucosamine (1 ŕ 4)‐linked internal chains. These groups occur together in the oligomannosidic type of N‐glycosidic‐linked oligosaccharide chains of glycoproteins and so the use of both lectins on desialycated membranes or on those which contain nonclustered N‐acetyl neuraminic acid residues may be of help to localize this type of glycoprotein oligosaccharide chains.Con A receptors were not removed after proteases digestion, suggesting the possibility that they are part of intrinsic spermatozoal antigens.

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Cytochemical Characterization and Localization of Oligomannosidic Oligosaccharide Receptors on the Normal Human Spermatozoa Using Fluorescent Lectins: Comparison of Different Fixation Procedures

Nardone

Cerezo

1985

American Journal of Reproductive Immunology and Microbiology

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Similar locations of the Con A and wheat germ lectin receptors were obtained by using fluorescent lectins, in nonfixed spermatozoa and in spermatozoa fixed with formaldehyde and methanol, showing that in samples with the same previous treatment, worked out by the same operator, in which enough determinations have been performed to eliminate individual variations, the different procedures of fixation produced similar results. The locatizations obtained with fluorescent lectins confirm previous results, produced with the peroxidase technique, indicating that the lectins interact with oligomannosidic oligosaccharide receptors situated mainly in the equatorial segment of the acrosome and postnuclear cap. They also indicate the presence of similar receptors that were not detected previously on the neck and intermediate segment. The larger size of the lectin-peroxidase-diaminebenzidine reagent compared to that of the fluorescent lectins suggests that the new receptors are semicriptic and were not detected by steric effects in the first case, but were able to interact with lower volume, fluorescent probes. It is suggested that these oligomannosidic chains could be recognition signals for the elimination of incompetent sperm during their passage through the female reproductive track. Also these oligosaccharides and its possible metabolic variations could be involved in the interaction between the acrosome-reacted spermatozoa with the zone pellucida.

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Immunoserological, immunohistochemical and immunobiological studies on an antigenic glycoprotein isolated from human seminal plasma

Cited by 5 publications

References 15 publications

The Antigenic Mucin‐Like Glycoproteins of Human Seminal Plasma*

The Antigenic Mucin‐Like Glycoproteins of Human Seminal Plasma*

Immunohistochemical Localization of Concanavalin A and Wheat Germ Lectin Receptors in the Normal Human Spermatozoa*

Cytochemical Characterization and Localization of Oligomannosidic Oligosaccharide Receptors on the Normal Human Spermatozoa Using Fluorescent Lectins: Comparison of Different Fixation Procedures

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