| Autor: |
Boettger-Tong H; Department of Biology, University of Alabama, Birmingham 35294-1170., Aarons D, Biegler B, Lee T, Poirier GR |
| Jazyk: |
angličtina |
| Zdroj: |
Biology of reproduction [Biol Reprod] 1992 Nov; Vol. 47 (5), pp. 716-22. |
| DOI: |
10.1095/biolreprod47.5.716 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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