The involvement of beta-1,4-Galactosyltransferase and N-Acetylglucosamine residues in fertilization has been lost in the horse.
Abstract: In human and rodents, sperm-zona pellucida binding is mediated by a sperm surface Galactosyltransferase that recognizes N-Acetylglucosamine residues on a glycoprotein ZPC. In large domestic mammals, the role of these molecules remains unclear: in bovine, they are involved in sperm-zona pellucida binding, whereas in porcine, they are not necessary. Our aim was to clarify the role of Galactosyltransferase and N-Acetylglucosamine residues in sperm-zona pellucida binding in ungulates. For this purpose, we analyzed the mechanism of sperm-zona pellucida interaction in a third ungulate: the horse, since the Galactosyltransferase and N-Acetylglucosamine residues have been localized on equine gametes. Methods: We masked the Galactosyltransferase and N-Acetylglucosamine residues before the co-incubation of gametes. Galactosyltransferase was masked either with an anti-Galactosyltransferase antibody or with the enzyme substrate, UDP Galactose. N-Acetylglucosamine residues were masked either with a purified Galactosyltransferase or with an anti-ZPC antibody. Conclusions: The number of spermatozoa bound to the zona pellucida did not decrease after the masking of Galactosyltransferase or N-Acetylglucosamine. So, these two molecules may not be necessary in the mechanism of in vitro sperm-zona pellucida interaction in the horse. Conclusions: The involvement of Galactosyltransferase and N-Acetylglucosamine residues in sperm-zona pellucida binding may have been lost during evolution in some ungulates, such as porcine and equine species.
Publication Date: 2008-11-14 PubMed ID: 19014565PubMed Central: PMC2607279DOI: 10.1186/1477-7827-6-51Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study explores the role of Galactosyltransferase and N-Acetylglucosamine in the binding of sperm to the zona pellucida – a membrane surrounding the oocyte (egg) – in horses. The researchers found that neither molecule appears to be necessary for this binding process in horses, suggesting that the use of these molecules for this purpose may have been lost in the evolution of some ungulates, such as horses and pigs.
Research aim and context
- This research was motivated by the aim to elucidate the role of Galactosyltransferase and N-Acetylglucosamine in the binding of sperm to the zona pellucida in ungulates (hoofed mammals), focusing specifically on horses.
- The zona pellucida is a membrane that surrounds the oocyte (egg) and is integral to fertilization in mammals.
- Previous research had found that in humans and rodents, a sperm surface Galactosyltransferase interacts with N-Acetylglucosamine on the ZPC glycoprotein in the zona pellucida to enable sperm binding. However, the relevance of this mechanism to larger domestic mammals was unclear.
Methodology
- The researchers used anti-Galactosyltransferase antibodies or the enzyme substrate UDP Galactose to mask Galactosyltransferase on the sperm surface, and a purified Galactosyltransferase or an anti-ZPC antibody to mask the N-Acetylglucosamine residues.
- They then observed the effect of this masking on the ability of sperm to bind to the zona pellucida.
Results
- The researchers found that the masking of these two molecules did not reduce the number of sperm cells able to bind to the zona pellucida.
- This suggested that Galactosyltransferase and N-Acetylglucosamine may not play a necessary role in this binding process in the horse.
Conclusion
- The researchers concluded that the involvement of Galactosyltransferase and N-Acetylglucosamine in sperm-zona pellucida binding may have been lost during evolution in some ungulates, such as horses and pigs.
- This suggests a divergent evolution of fertilization mechanisms among different species, potentially influenced by various biological and environmental factors.
Cite This Article
APA
Mugnier S, Boittin S, Douet C, Monget P, Magistrini M, Goudet G.
(2008).
The involvement of beta-1,4-Galactosyltransferase and N-Acetylglucosamine residues in fertilization has been lost in the horse.
Reprod Biol Endocrinol, 6, 51.
https://doi.org/10.1186/1477-7827-6-51 Publication
Researcher Affiliations
- INRA, UMR85 Physiologie de la Reproduction et des Comportements, CNRS, Haras Nationaux, Université de Tours, Nouzilly, France. sylvie.mugnier@tours.inra.fr
MeSH Terms
- Acetylglucosamine / chemistry
- Acetylglucosamine / immunology
- Acetylglucosamine / metabolism
- Acetylglucosamine / physiology
- Animals
- Antibodies / pharmacology
- Biological Evolution
- Cells, Cultured
- Female
- Fertilization / physiology
- Freezing
- Horses / genetics
- Horses / physiology
- Male
- N-Acetyllactosamine Synthase / antagonists & inhibitors
- N-Acetyllactosamine Synthase / immunology
- N-Acetyllactosamine Synthase / physiology
- Semen Preservation
- Sperm-Ovum Interactions / drug effects
- Sperm-Ovum Interactions / immunology
- Spermatozoa / drug effects
- Spermatozoa / immunology
- Uridine Diphosphate Galactose / pharmacology
- Zona Pellucida / immunology
- Zona Pellucida / metabolism
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Citations
This article has been cited 1 times.- Mugnier S, Kervella M, Douet C, Canepa S, Pascal G, Deleuze S, Duchamp G, Monget P, Goudet G. The secretions of oviduct epithelial cells increase the equine in vitro fertilization rate: are osteopontin, atrial natriuretic peptide A and oviductin involved?. Reprod Biol Endocrinol 2009 Nov 19;7:129.
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