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透明带中猪精子受体与公猪精子顶体的结合。

Binding of pig sperm receptor in the zona pellucida to the boar sperm acrosome.

作者信息

Yonezawa N, Hatanaka Y, Takeyama H, Nakano M

机构信息

Department of Chemistry, Faculty of Science, Chiba University, Japan.

出版信息

J Reprod Fertil. 1995 Jan;103(1):1-8. doi: 10.1530/jrf.0.1030001.

Abstract

Pig zona pellucida (ZP) contains three families of glycoproteins: PZP2, PZP3 alpha and PZP3 beta. PZP3 alpha mediates the binding of the ZP to spermatozoa. In this study, the binding site of pig ZP on boar spermatozoa and the zona-binding proteins of boar spermatozoa were studied using chemically modified zona glycoproteins or anti-pig ZP antiserum. Endo-beta-galactosidase-digested PZP3 alpha (E beta G-PZP3 alpha), which is deficient in sulfated N-acetylpolyactosamine, as well as solubilized ZP, bound to the acrosomal region of acrosome-damaged or partially acrosome-reacted spermatozoa. However, they did not bind to acrosome-intact or fully acrosome-reacted spermatozoa. Solubilized ZP did bind to the acrosomal cap released upon acrosome reaction. In western blot analyses, E beta G-PZP3 alpha bound to the sperm proteins with molecular masses similar to proacrosin-acrosin and the binding was inhibited by fucoidan and anti-pig acrosin antiserum. These results suggest that the binding site of solubilized pig ZP and E beta G-PZP3 alpha on spermatozoa is located mainly in the acrosomal matrix and on the membranous compartments in the acrosome and suggest that E beta G-PZP3 alpha binds to proacrosin-acrosin. The binding of E beta G-PZP3 alpha to proacrosin-acrosin may be involved in the binding of the ZP to the acrosome of partially acrosome-reacted spermatozoa.

摘要

猪透明带(ZP)包含三类糖蛋白:PZP2、PZP3α和PZP3β。PZP3α介导透明带与精子的结合。在本研究中,使用化学修饰的透明带糖蛋白或抗猪ZP抗血清研究了猪透明带在公猪精子上的结合位点以及公猪精子的透明带结合蛋白。内切β-半乳糖苷酶消化的PZP3α(EβG-PZP3α)缺乏硫酸化的N-乙酰多聚乳糖胺,以及溶解的透明带,与顶体受损或部分顶体反应的精子的顶体区域结合。然而,它们不与顶体完整或完全顶体反应的精子结合。溶解的透明带确实与顶体反应时释放的顶体帽结合。在蛋白质印迹分析中,EβG-PZP3α与分子量类似于前顶体蛋白酶-顶体蛋白酶的精子蛋白结合,并且这种结合被岩藻依聚糖和抗猪顶体蛋白酶抗血清抑制。这些结果表明,溶解的猪透明带和EβG-PZP3α在精子上的结合位点主要位于顶体基质以及顶体中的膜性区室,并表明EβG-PZP3α与前顶体蛋白酶-顶体蛋白酶结合。EβG-PZP3α与前顶体蛋白酶-顶体蛋白酶的结合可能参与透明带与部分顶体反应精子的顶体的结合。

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