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Sperm surface galactosyltransferase activities during in vitro capacitation
The Journal of Cell Biology
|November 1, 1982
Summary
Sperm surface galactosyltransferases bind egg zona pellucida N-acetylglucosamine (GlcNAc). Capacitation releases inhibitory substrates, enabling sperm-egg binding. Decapacitation factors block this by competing for the enzyme.
Area of Science:
- Reproductive Biology
- Glycobiology
- Cell Biology
Background:
- Sperm surface galactosyltransferases are implicated in fertilization.
- Binding to egg zona pellucida N-acetylglucosamine (GlcNAc) residues is a key step.
Purpose of the Study:
- To investigate sperm surface galactosyltransferase activity during in vitro capacitation.
- To correlate changes in enzymatic activity with fertilizing ability.
Main Methods:
- Examined sperm surface galactosyltransferase activity during in vitro capacitation.
- Utilized Ca(++)-containing and Ca(++)-free media for capacitation.
- Tested inhibition by pronase-digested polyactosaminyl glycosides.
Main Results:
- Uncapacitated sperm show galactosyltransferases loaded with poly N-acetyllactosamine substrates.
- Capacitation releases these substrates, exposing galactosyltransferases for zona pellucida binding.
- High molecular weight polyactosaminyl glycosides act as decapacitation factors by inhibiting sperm-egg binding.
Conclusions:
- Sperm capacitation involves the release of inhibitory substrates from surface galactosyltransferases.
- Decapacitation factors, identified as polyactosaminyl glycosides, compete with the zona pellucida for sperm galactosyltransferase binding.
- This defines a molecular mechanism for sperm capacitation and egg- zona pellucida interaction.