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Home > Medicine & Health Science textbooks > Medical specialties, branches of medicine > Gynaecology and obstetrics > Identification of a Glycodelin-C Binding Molecule on Human Spermatozoa
Identification of a Glycodelin-C Binding Molecule on Human Spermatozoa

Identification of a Glycodelin-C Binding Molecule on Human Spermatozoa


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This dissertation, "Identification of a Glycodelin-C Binding Molecule on Human Spermatozoa" by Vernon Craig Goodheart, Tam, was obtained from The University of Hong Kong (Pokfulam, Hong Kong) and is being sold pursuant to Creative Commons: Attribution 3.0 Hong Kong License. The content of this dissertation has not been altered in any way. We have altered the formatting in order to facilitate the ease of printing and reading of the dissertation. All rights not granted by the above license are retained by the author. Abstract: Abstract of thesis entitled Identification of a Glycodelin-C binding molecule on Human Spermatozoa Submitted by Tam Vernon Craig Goodheart For the Degree of Master of Philosophy at the University of Hong Kong August 2007 Glycodelin is a glycoprotein with 4 reported isoforms, namely glycodelin-A (amniotic fluid isoform), glycodelin-S (seminal plasma isoform), glycodelin-F (follicular fluid isoform) and glycodelin-C (cumulus matrix isoform). During the passage to the fertilization site, spermatozoa are exposed successively to different glycodelin isoforms modulating various aspects of sperm functions important for fertilization. Glycodelin-C is the latest isoform identified (Chiu et al., 2007). Like other glycodelin isoform, it contains the same glycodelin protein core as the other isoforms but with different glycosylation. Instead of having inhibitory activity on spermatozoa-zona pellucida binding as glycodelin-A and -F, glycodelin-C 3stimulates such binding. The objective of this study was to identify the receptor of glycodelin-C on human spermatozoa. In this study, the surface molecules of live spermatozoa were biotinlyated before incubation with glycodelin-C and subsequent solubilization with detergent. The glycodelin-C binding complexes were isolated by avidin-coupled affinity column followed by immunoprecipitation by anti-glycodelin antibody. The identity of the isolated biotinylated molecules were analysed by mass spectrometry. One of the glycodelin-C binding proteins on human spermatozoa was asialoglycoprotein receptor-2. It is a C-type lectin with molecular size of 60 kDa. Anti-asialoglycoprotein receptor-2 antibody recognized a 60 kDa protein band in western blot analysis of the isolated fractions. Indirect immunofluorescence staining using the same antibody localized asialoglycoprotein receptor-2 immunoreactivity to the acrosome region and equatorial segment of human spermatozoa, a region that also binds glycodelin-C. The interaction between asialoglycoprotein receptor-2 in sperm extract and glycodelin-C was further demonstrated by co-immunoprecipitation using anti-glycodelin and anti-asialoglycoprotein receptor-2 antibodies, and competition assay using asialoglycoprotein receptor-2 acceptors. The binding was abolished in the presence of calcium chelator, showing that calcium ions were essential for the 4interaction. The inability of deglycosylated glycodelin to co-immunoprecipitate with sperm asialoglycoprotein receptor-2 was in line with the documented importance of carbohydrate moieties on spermatozoa-glycodelin interaction. Acceptors of asialoglycoprotein receptor-2, including p-aminophenyl-D-thiogalactopyranoside, bovine albumin galactosamide and desialylated alpha-1-acid glycoprotein, compete with glycodelin-C for the binding to recombinant asialoglycoprotein receptor 2 as well as intact live spermatozoa. Glycodelin-C but not glycodelin-A was found to bind asialoglycoprotein receptor-2. Glycodelin-C induced tyrosine phosphorylation of human spermatozoa and stimulated spermatozoa-zona pellucida binding. However, similar biological activities were not found when asialoglycoprotein receptor-2 acceptors were used. These results suggest that asialoglycoprotein receptor-2 may only serve as an anchoring protein but not the biological active receptor of glycodelin-C. The presence of other receptor(s) on spermatozoa that determines glycodelin-C


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Product Details
  • ISBN-13: 9781374664883
  • Publisher: Open Dissertation Press
  • Publisher Imprint: Open Dissertation Press
  • Height: 279 mm
  • Weight: 354 gr
  • ISBN-10: 137466488X
  • Publisher Date: 27 Jan 2017
  • Binding: Paperback
  • Spine Width: 8 mm
  • Width: 216 mm


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Identification of a Glycodelin-C Binding Molecule on Human Spermatozoa
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