Human Sperm Coating Antigen From Seminal Plasma Origin

Iborra, A.; Morte, Carles; Fuentes, P.; García-Framis, V.; Andolz, P.; Martı́nez, Paz

doi:10.1111/j.1600-0897.1996.tb00150.x

Cited by 9 publications

(3 citation statements)

References 30 publications

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“…The fact that noncapacitated sperm bind LSA and are rendered incapable of zona binding suggests that some form of one or more sperm receptors for the zona pellucida is exposed on the surface of noncapacitated sperm. This evidence appears to be in conflict with the results of other studies that have suggested sperm receptors for zona ligands are not exposed until after capacitation (Iborra et al, 1996;Youssef et al, 1997;Fraser, 1998). LSA may provide a useful tool for elucidating the relationship between capacitation and the sperm functions involved in binding to the zona pellucida.…”

Section: Discussioncontrasting

confidence: 57%

Lignosulfonic Acid Blocks In Vitro Fertilization of Macaque Oocytes When Sperm Are Treated Either Before or After Capacitation

TOLLNER,

OVERSTREET,

et al. 2002

Journal of Andrology

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Lignin‐derived macromolecules (LDMs) are biologically active compounds that affect a variety of cell‐to‐cell interactions including the inhibition of fertilization and embryo development in a number of nonmammalian species. The effect of lignosulfonic acid (LSA), a highly sulfonated LDM, on cynomolgus macaque sperm‐oocyte interaction was evaluated with a zona pellucida binding assay and by in vitro fertilization (IVF). Sperm were treated with LSA (1.5 mg/mL) either before washing or after capacitation. Capacitation included centrifugation through 80% Percoll followed by 2 consecutive washes with medium, overnight incubation, and activation with dibutyryl cyclic adenosine monophosphate and caffeine. The zona binding assay was performed using immature oocytes that had adhered to the center of glass “binding chambers.” The number of capacitated sperm that attached to the zona over a 3‐minute period was recorded. Sperm attachment was significantly inhibited by LSA as compared to controls whether treatment occurred after capacitation (92.5%; P < .001) or before washing (82.5%; P < .001). When sperm were treated similarly with fucoidin, a sulfated polysaccharide known to inhibit sperm‐oocyte interaction, sperm‐zona binding was significantly inhibited by postcapacitation treatment but not by prewash treatment. Treatment of sperm with LSA consistently blocked fertilization over 4 IVF cycles both before washing and after capacitation. Fertilization rate for controls was 65% ± 17%. No LSA‐treated sperm were observed on the surface of lightly rinsed oocytes after 4 hours of coincubation. Localization of biotinylated LSA showed labeling over the entire sperm surface with the greatest intensity observed over the head and midpiece. LSA treatment had no effect on the percentage of motile sperm or quality of sperm motility. Due to the antifertility properties of this nontoxic molecule, LSA appears to have potential as a vaginal contraceptive.

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Section: Discussioncontrasting

confidence: 57%

Lignosulfonic Acid Blocks In Vitro Fertilization of Macaque Oocytes When Sperm Are Treated Either Before or After Capacitation

TOLLNER,

OVERSTREET,

et al. 2002

Journal of Andrology

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“…Various individual studies have identified glycoproteins in human seminal plasma and their role in fertility/infertility related processes is also documented. Seminal plasma glycoproteins are known to participate in sperm-egg recognition [22], modulation of capacitation [23,24] and acrosome reaction inhibition [25]. It is a known fact that glycosylation modulates the physicochemical properties and conformation of the proteins, which in turn can modulate the biological activity and immunological properties.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Identification of Concanavalin A Binding Glycoproteins from Human Seminal Plasma: A Step Towards Identification of Male Infertility Marker Proteins

et al. 2011

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Human seminal plasma contains a large array of proteins of clinical importance which are essentially needed to maintain the reproductive physiology of spermatozoa and for successful fertilization. Thus, isolation and identification of seminal plasma proteins is of paramount significance for their biophysical characterization and functional analysis in reproductive physiological processes. In this study, we have isolated Concanavalin-A binding glycoproteins from human seminal plasma and subsequently identified them by MALDI-TOF/MS analysis. The major proteins, as identified in this study, are Aminopeptidase N, lactoferrin, prostatic acid phosphatase, zinc-alpha-2-glycoprotein, prostate specific antigen, progestagen-associated endometrial protein, Izumo sperm-egg fusion protein and prolactin inducible protein. This paper also reports preliminary studies to identify altered expression of these proteins in oligospermia and azoospermia in comparison to normospermia. In oligospermia, five proteins were found to be downregulated while in azoospermia, four proteins were downregulated and two proteins were upregulated. Thus, this study is of immense biomedical interest towards identification of potential male infertility marker proteins in seminal plasma.

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“…Human seminal plasma contains a large array of proteins of clinical importance which are essentially needed to maintain the reproductive physiology of spermatozoa and for successful fertilization. Seminal plasma glycoproteins are known to participate in sperm-egg recognition [5], modulation of capacitation [6, 7] and acrosome reaction inhibition [8]. Moreover, Con A-interacting fraction of human seminal plasma is reported to have decapacitating activity [9].…”

Section: Introductionmentioning

confidence: 99%

Computational analysis of Concanavalin A binding glycoproteins of human seminal plasma

Tomar¹,

Sooch²,

Yadav³

2011

Bioinformation

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Glycoproteins have immense clinical importance and comparative glycoproteomics has become a powerful tool for biomarker discovery and disease diagnosis. Seminal plasma glycoproteins participate in fertility related processes including sperm-egg recognition, modulation of capacitation and acrosome reaction inhibition. Affinity chromatography using broad specificity lectin such as Con A is widely applied for glycoproteins enrichment. More notably, Con A-interacting fraction of human seminal plasma has decapacitating activity which makes this fraction critically important. In our previous study, we isolated Con A-interacting glycoproteins from human seminal plasma and subsequently identified them by mass spectrometry. Here, we report the computational analysis of these proteins using bioinformatics tools. The analysis includes: prediction of glycosylation sites using sequence information (NetNGlyc 1.0), functional annotations to cluster these proteins into various functional groups (InterProScan and Blast2GO) and identification of protein interaction networks (STRING database). The results indicate that these proteins are involved in various biological processes including transport, morphogenesis, metabolic processes, cell differentiation and homeostasis. The clusters illustrate two major molecular functions - hydrolase activity (6) and protein (4)/carbohydrate (1)/lipid binding (1). The large interactomes of proteins point towards their versatile roles in wide range of biological processes.

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Human Sperm Coating Antigen From Seminal Plasma Origin

Cited by 9 publications

References 30 publications

Lignosulfonic Acid Blocks In Vitro Fertilization of Macaque Oocytes When Sperm Are Treated Either Before or After Capacitation

Lignosulfonic Acid Blocks In Vitro Fertilization of Macaque Oocytes When Sperm Are Treated Either Before or After Capacitation

Isolation and Identification of Concanavalin A Binding Glycoproteins from Human Seminal Plasma: A Step Towards Identification of Male Infertility Marker Proteins

Computational analysis of Concanavalin A binding glycoproteins of human seminal plasma

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