Competition between zonae pellucidae and a proteinase inhibitor for sperm binding.
Murine sperm bind a proteinase inhibitor of seminal vesicle origin at ejaculation. The inhibitor binds in the acrosomal region of the sperm head and is removed during in utero or in vitro incubation. Adding inhibitor to sperm reduces their ability to bind zonae, while adding the purified inhibitor binding site to cumulus-free, zona-intact oocytes reduces the ability of the oocytes to bind sperm. Immuno-aggregation of the inhibitor binding site results in exocytosis of the acrosome. These observations suggest that the inhibitor binding site may participate in zona binding and the acrosome reaction. If the inhibitor binding site binds both the zona and the seminal inhibitor, then these components should compete with each other for that site on the sperm. We show that purified seminal inhibitor, as well as other proteinase inhibitors, block zona-induced acrosome reactions. Likewise, zona glycopeptides block inhibitor/anti-inhibitor-induced acrosome reactions in a concentration-dependent fashion. The inhibitor/anti-inhibitor-induced acrosome reaction is sensitive to pertussis toxin and proteinase inhibitor and thus is similar to zona-induced reactions. These findings support the suggestion that the trypsin inhibitor binding site on the head of the sperm functions to insure sperm-zona binding and induction of the acrosome reaction.
Boettger-Tong
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H
Department of Biology, University of Alabama, Birmingham 35294-1170.
Aarons
D
D
Biegler
B
B
Lee
T
T
Poirier
G R
GR
D000177:Acrosome / Q000502:physiology; D000818:Animals; D000925:Anticoagulants / Q000378:metabolism; D001667:Binding, Competitive; D015153:Blotting, Western; D004305:Dose-Response Relationship, Drug; D004527:Egg Proteins; D005260:Female; D005307:Fertilization in Vitro; D005455:Fluorescent Antibody Technique; D007074:Immunoglobulin G / Q000096:biosynthesis; D008297:Male; D008562:Membrane Glycoproteins / Q000494:pharmacology; D051379:Mice; D008813:Mice, Inbred ICR; D010059:Ovomucin / Q000378:metabolism; D037342:Pertussis Toxin; D011134:Polysaccharides / Q000378:metabolism; D011480:Protease Inhibitors / Q000378:metabolism*; D011956:Receptors, Cell Surface; D013084:Sperm-Ovum Interactions / Q000187:drug effects / Q000502:physiology*; D013094:Spermatozoa / Q000378:metabolism*; D010566:Virulence Factors, Bordetella / Q000494:pharmacology; D015044:Zona Pellucida / Q000276:immunology / Q000378:metabolism*; D000072216:Zona Pellucida Glycoproteins
D000925:Anticoagulants; D004527:Egg Proteins; D007074:Immunoglobulin G; D008562:Membrane Glycoproteins; D011134:Polysaccharides; D011480:Protease Inhibitors; D011956:Receptors, Cell Surface; D010566:Virulence Factors, Bordetella; D000072216:Zona Pellucida Glycoproteins; D010059:Ovomucin; C007789:fucoidan; D037342:Pertussis Toxin