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Updated: Jul 15, 2026
08:58
Fluorimetric Techniques for the Assessment of Sperm Membranes
Published on: November 28, 2018
Glycodelin binding to human ejaculated spermatozoa is correlated with sperm morphology
Nadja Gneist1, Gudrun Keck, Anja Zimmermann
1Department of Gynecology and Obstetrics, Medical Center, Technical University Dresden, Dresden, Germany. nadja.gneist@uniklinikum-dresden.de
Fertility and Sterility
|May 8, 2007
Summary
Glycodelin (Gd) binding to sperm cells is linked to sperm shape. This study found that normal-shaped sperm bind less Gd, suggesting variations in sperm quality affect Gd adherence.
Area of Science:
- Reproductive biology
- Spermatozoa function
- Glycobiology
Background:
- Glycodelin (Gd) is a protein found in seminal plasma.
- Its role in sperm function and its interaction with sperm surface are not fully understood.
- Understanding Gd-sperm interaction may provide insights into male fertility.
Purpose of the Study:
- To investigate the relationship between glycodelin (Gd) binding on sperm surface and sperm morphology.
- To assess the correlation between seminal plasma Gd levels and Gd binding to sperm.
- To explore how sperm quality influences Gd adherence.
Main Methods:
- Retrospective analysis of 5,749 spermatozoa from 42 patients.
- Sperm morphology assessed using World Health Organization criteria.
- Gd binding measured via immunocytochemical staining; Gd levels determined by ELISA.
Main Results:
- Significant variability in sperm surface Gd binding and seminal plasma Gd levels observed.
- No overall correlation between seminal plasma Gd and sperm surface Gd.
- Gd binding to sperm surface was dependent on sperm morphology, with reduced binding on normal-shaped sperm.
Conclusions:
- Glycodelin binding to human spermatozoa is correlated with sperm morphology.
- Variability in Gd adherence suggests differences in sperm membrane properties related to sperm quality.
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