Glycoprotein fucosylation is increased in seminal plasma of subfertile men
低生育力男性精浆中岩藻糖蛋白增加作者机构:Department of Chemistry and Immunochemistry Medical University of Wrociaw Wroclaw Poland Department and Clinic of Gynecology and Obstetrics Medical University of Wrodaw Wrodaw Poland.
出 版 物:《Asian Journal of Andrology》 (亚洲男性学杂志(英文版))
年 卷 期:2015年第17卷第2期
页 面:274-280,I0010页
核心收录:
学科分类:10[医学]
基 金:Wroclaw Medical University project Pbmn81
主 题:fucose glycosylation infertility seminal plasma
摘 要:Fucose, the monosaccharide frequent in N- and O-glycans, is a part of Lewis-type antigens that are known to mediate direct sperm binding to the zona pellucida. Such interaction was found to be inhibited in vitro by fucose-containing oligo- and polysaccharides, as well as neoglycoproteins. The objective of this study was to screen seminal plasma proteins of infertile/subfertile men for the content and density of fucosylated glycoepitopes, and compare them to samples of fertile normozoospermic subjects. Seminal proteins were separated in polyacrylamide gel electrophoresis and blotted onto nitrocellulose membrane and probed with fucose-specific Aleuria aurantia lectin (AAL). Twelve electrophoretic bands were selected for quantitative densitometric analysis. It was found that the content, and especially the density of fucosylated glycans, were higher in glycoproteins present in seminal plasma of subfertile men. No profound differences in fucosylation density were found among the groups of normozoospermic, oligozoospermic, asthenozoospermic, and oligoasthenozoospermic subfertile men. According to the antibody probing, AAL-reactive bands can be attributed to male reproductive tract glycoproteins, including prostate-specific antigen, prostatic acid phosphatase, glycodelin and chorionic gonadotropin. Fibronectin, a1-acid glycoprotein, a1-antitrypsin, immunoglobulin G and antithrombin III may also contribute to this high fucosylation. It is suggested that the abundant fucosylated glycans in the sperm environment could interfere with the sperm surface and disturb the normal course of the fertilization cascade.