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Open AccessJournal ArticleDOI

Binding of zona binding inhibitory factor-1 (ZIF-1) from human follicular fluid on spermatozoa.

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TLDR
The carbohydrate moieties derived from ZIF-1 reduced the binding of native Zif-1 on human spermatozoa as well as the zona binding inhibitory activity of the glycoprotein, although the intensity of the effects are lower when compared with the native protein.
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This article is published in Journal of Biological Chemistry.The article was published on 2003-04-11 and is currently open access. It has received 46 citations till now. The article focuses on the topics: Zona pellucida & Acrosome reaction.

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Citations
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Journal ArticleDOI

Glycodelin-S in Human Seminal Plasma Reduces Cholesterol Efflux and Inhibits Capacitation of Spermatozoa

TL;DR: Glycodelin-S in seminal plasma maintains the uncapacitated state of human spermatozoa, indicating that the carbohydrate moiety of glycodelin -S is critical for the function of the molecule.
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Glycosylation related actions of glycodelin: gamete, cumulus cell, immune cell and clinical associations

TL;DR: This review updates the recent research and clinical associations of glycodelin and highlights the role of glycosylation, which may be involved in the protection of spermatozoa against maternal immune reactions, and glyCodelin also has apoptogenic activity.
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Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding.

TL;DR: Observations suggest that human sperm FUT5 is a receptor of glycodelin-A and zona pellucida proteins, and that glycodzin-A inhibits spermatozoa-zona binding by blocking the binding of sperm Fut5 to the zonapellucIDA.
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Roles of glycodelin in modulating sperm function.

TL;DR: Different isoforms of glycodelin have different biological roles on sperm function, and they act in succession to contribute to the success of fertilization.
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Cumulus oophorus-associated glycodelin-C displaces sperm-bound glycodelin-A and -F and stimulates spermatozoa-zona pellucida binding.

TL;DR: Glycodelin-C stimulated spermatozoazona pellucida binding in a dose-dependent manner, and it effectively displaced sperm-bound gly codelin-A and -F and enhances the zona binding capacity of spermatozosa passing through the cumulus oophorus.
References
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Journal ArticleDOI

Glycodelin from seminal plasma is a differentially glycosylated form of contraceptive glycodelin-A

TL;DR: The evidence indicates that gly codelin-A mediated its biological activities via its unusual oligosaccharide sequences that are not associated with glycodelin-S, and the results of sugar analysis and neuraminidase digestion lead us to conclude that glycodelo-S and glycodel-A are differentially glycosylated forms of similar proteins.
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Human sperm plasma membranes possess alpha-D-mannosidase activity but no galactosyltransferase activity.

TL;DR: It is shown that a very small amount of the total galactosyltransferase activity present in human semen is associated with spermatozoa, and the failure to find a significant amounts of the enzyme on sperm plasma membranes suggests that the enzyme is not associated with the sperm surface.
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Inducing the human acrosome reaction with a calcium ionophore A23187 decreases sperm-zona pellucida binding with oocytes that failed to fertilize in vitro.

TL;DR: The sperm-ZP binding ratio of test to control spermatozoa was significantly decreased and the sperm-oolemma binding ratio was significantly increased with A23187 treatment, suggesting that acrosome-reacted spermatozosa do not bind to the human ZP.
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Human oviductal cells and their conditioned medium maintain the motility and hyperactivation of human spermatozoa in vitro

TL;DR: The data suggested that human oviductal cells could maintain the motility of spermatozoa in vitro, and similar effects were also observed when conditioned medium was used to treat subnormal spermutozoa.
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Expression and topographical localization of cell surface fucosyltransferase activity during epididymal sperm maturation in the mouse

TL;DR: The data demonstrate that FT activity is retained selectively on the different topological regions of sperm, with losses during sperm maturation in the epididymis being restricted to the tail segment.
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