Characterization of the rabbit sperm membrane autoantigen, RSA, as a lectin-like zona binding protein.
Characterization of the rabbit sperm membrane autoantigen, RSA, as a lectin-like zona binding protein.
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兔精子膜自身抗原 RSA 的表征，作为凝集素样透明带结合蛋白。
DOI：
10.1016/0012-1606(88)90177-7
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发表时间：
1988
影响因子：
2.7
通讯作者：
Fisher,SJ
中科院分区：
文献类型：
--
作者：
O'Rand,MG;Widgren,EE;Fisher,SJ
精子与卵子胞外涂层透明带之间的黏附涉及精子的透明带结合蛋白(ZBP)及其与透明带碳水化合物残基的相互作用。为了更详细地研究这种相互作用，我们使用了纯化的非酶ZBP，兔精子膜自身抗原RSA。硝酸纤维素膜印迹和Denny-Jaffe交联剂证实了RSA-zona的结合，确定了一个87000分子量的zona组分是RSA的配基。RSAZA结合亲和力强，解离常数为5.6×10−13M。此外，在RSA存在的情况下，获能精子与完整小带的结合被抑制。对RSA-zona与多种简单和复杂碳水化合物相互作用的表征表明，复合碳水化合物岩藻糖素、葡聚糖硫酸盐、硫酸软骨素B和肝素强烈抑制RSA-zona结合，而硫酸软骨素A和C、胆固醇-3-硫酸盐和半乳糖等单糖仅弱抑制RSA-zona结合。结论：RSA是一种精子凝集素样分子，可将精子与透明带结合。
Adhesion between spermatozoa and the egg's extracellular coat, the zona pellucida, involves the sperm's zona binding proteins (ZBP) and their interaction with the carbohydrate residues of the zona. To investigate this interaction in more detail, a purified nonenzymatic ZBP, the rabbit sperm membrane autoantigen, RSA, was used. RSA-zona binding was demonstrated on nitrocellulose blots and by using the Denny-Jaffe crosslinking reagent which identified an 87,000 molecular weight zona component as the ligand for RSA. The RSA-zona binding was of high affinity with a dissociation constant of 5.6 × 10−13M. Furthermore, the binding of capacitated spermatozoa to intact zona was inhibited in the presence of RSA. Characterization of the RSA-zona interaction with a variety of simple and complex carbohydrates indicated that the sulfated, complex carbohydrates fucoidin, dextran sulfate, chondroitin sulfate B, and heparin strongly inhibited RSA-zona binding while chondroitin sulfates A and C, cholesterol-3-sulfate, and monosaccarides such as galactose inhibited RSA-zona binding only weakly. It is concluded that RSA functions as a sperm lectin-like molecule to bind the spermatozoon to the zona pellucida.