Galactosyltransferase activity is restricted to the plasma membranes of equine and bovine sperm.
Abstract: beta 1, 4-Galactosyltransferase (GalTase) is localized to the plasma membrane of mouse sperm, in which it mediates the binding of sperm to glycoconjugate residues in the egg zona pellucida. In this study, the presence of subcellular distribution of sperm GalTase were determined in two other mammalian species that yield sufficient sperm for subcellular fractionation. Equine and bovine semen were collected, and the plasma membranes (PM), outer acrosomal membranes (OAM), and inner acrosomal membranes (IAM) were sequentially removed. The purities of the isolated membrane preparations were determined by transmission electron microscopy and found to be greater than or equal to 90%, 96%, and 98% for equine PM, OAM, and IAM, respectively, and greater than or equal to 80%, 94%, and 97% for bovine PM, OAM, and IAM, respectively. GalTase activity was assayed under optimal conditions in all membrane preparations and was preferentially localized to the isolated PM both in equine and in bovine spermatozoa. The selective localization of GalTase to the sperm PM in two other species suggest that it may serve as a generalized gamete receptor during initial sperm-egg binding in mammals.
Publication Date: 1991-01-01 PubMed ID: 1899795DOI: 10.1002/mrd.1080280112Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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The research examined the localization of a specific enzyme (beta 1,4-Galactosyltransferase, or GalTase) in equine and bovine sperm cells that could play a significant role in sperm-egg binding in mammals.
Objective and method of Study
- This study delves into the subcellular distribution of GalTase, an enzyme originally found in mouse sperm that facilitates binding of the sperm to egg. The authors sought to detect and determine the location of this enzyme in sperm of other mammals, which they hoped would suggest its possible function as a common receptor during initial sperm-egg binding.
- Due to their ability to produce large amounts of sperm, horses and cows were selected for the study. The sperm membranes, including the plasma membrane (PM), outer acrosomal membranes (OAM), and inner acrosomal membranes (IAM), were isolated, and the purity of these isolated membrane preparations was then confirmed via transmission electron microscopy.
Results of the Study
- The researchers initially confirmed a high level of purity in the separated membranes: over 90% for equine PM, OAM, and IAM; and 80% or more for bovine PM, OAM, and IAM.
- Through assays conducted under optimal conditions for all membrane preparations, they discovered a predominant localization of GalTase activity within the isolated PM of both equine and bovine sperm cells.
Implications of the Study
- The fact that GalTase was primarily found in the plasma membrane, a key site for sperm-egg interaction, in two more species suggests the enzyme may play a universal role in the initial binding of mammalian sperm to the egg.
- The study provides valuable insights for future research on fertility and the process of fertilization in mammals, by highlighting the potential role of GalTase in sperm-egg binding. This could potentially lead to advancements in fertility treatments and even new contraceptive strategies.
Cite This Article
APA
Fayrer-Hosken RA, Caudle AB, Shur BD.
(1991).
Galactosyltransferase activity is restricted to the plasma membranes of equine and bovine sperm.
Mol Reprod Dev, 28(1), 74-78.
https://doi.org/10.1002/mrd.1080280112 Publication
Researcher Affiliations
- Department of Large Animal Medicine; College of Veterinary Medicine, University of Georgia, Athens 30602.
MeSH Terms
- Animals
- Cattle / metabolism
- Cell Fractionation
- Cell Membrane / enzymology
- Cell Membrane / ultrastructure
- Galactosyltransferases / metabolism
- Horses / metabolism
- Kinetics
- Male
- Microscopy, Electron
- Spermatozoa / enzymology
- Spermatozoa / ultrastructure
Grant Funding
- HD23479 / NICHD NIH HHS
Citations
This article has been cited 4 times.- Tumova L, Zigo M, Sutovsky P, Sedmikova M, Postlerova P. Ligands and Receptors Involved in the Sperm-Zona Pellucida Interactions in Mammals. Cells 2021 Jan 12;10(1).
- Mugnier S, Boittin S, Douet C, Monget P, Magistrini M, Goudet G. The involvement of beta-1,4-Galactosyltransferase and N-Acetylglucosamine residues in fertilization has been lost in the horse. Reprod Biol Endocrinol 2008 Nov 14;6:51.
- Shur BD. Reassessing the role of protein-carbohydrate complementarity during sperm-egg interactions in the mouse. Int J Dev Biol 2008;52(5-6):703-15.
- Shur BD, Evans S, Lu Q. Cell surface galactosyltransferase: current issues. Glycoconj J 1998 Jun;15(6):537-48.
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