正常精子男性精浆中γ -谷氨酰转移酶相关的糖蛋白模式:生物标志物异质性的新方面。

Pub Date : 2023-07-17 DOI:10.5507/bp.2023.031
Tamara Jankovic, Jelena Danilovic Lukovic, Sanja Goc, Ninoslav Mitic, Ljiljana Hajdukovic, Miroslava Jankovic
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引用次数: 0

摘要

背景:γ -谷氨酰转移酶(GGT)是一种众所周知的实验室生物标志物。尽管GGT在人精浆(hSP)中的浓度很高,并且可能具有重要的生物医学意义,但它在生殖生理学方面尚未得到广泛的探讨。本研究旨在通过分析hSP的匹配可溶性部分来补充先前在精子细胞外囊泡中获得的关于其多样性的现有数据。分析了选定的糖蛋白的GGT相关模式,以便建立一个辅助参考参数来区分已知的GGT的高分子质量形式。深入了解不同的ggt相关糖蛋白模式将有助于将它们一起定义为可能的多标记物。方法:采用凝胶过滤和小麦胚芽凝集素(WGA)和麦豆蛋白A (Con A)凝集素印迹法,对正常精子男性热sp分离的可溶性无膜组分中GGT的形态进行分析。结果:GGT分布广泛(有2 ~ 3个部分分解峰),可能与高分子质量聚集体相对应。选定的糖蛋白的ggt相关模式(在大、中、小ggt的位置)都包含高分子量的wga反应性涂片,但在Con -a反应性聚糖以及粘蛋白相关抗原CA19-9和CA125的存在方面有所不同。结论:GGT对热休克蛋白可溶性和细胞外囊泡组分之间的不同分子模式有贡献。它们的糖生化异质性是由于存在不同的唾液化和甘露糖基化聚糖。此外,GGT相关的糖蛋白模式区分了热sp可溶性部分GGT的高分子质量形式。它们有望成为增加GGT生物标志物潜力的可能靶点。
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Gamma-glutamyltransferase-associated glycoprotein patterns in human seminal plasma of normozoospermic men: a new aspect of biomarker heterogeneity.

Background: Gamma-glutamyltransferase (GGT) is a well-known laboratory biomarker. In spite of high concentration and the possible biomedical importance of estimating GGT in human seminal plasma (hSP), it has not been widely explored in reproductive physiology. This study aimed to complement existing data on its diversity, previously obtained on seminal extracellular vesicles, by analyzing matched soluble fraction of hSP. The GGT-associated patterns of selected glycoproteins were analyzed in order to establish an adjunct referent parameter for differentiation between known high molecular mass forms of GGT. Getting insight into distinct GGT-associated glycoprotein patterns should contribute to define them together as possible multimarkers.

Methods: GGT forms in soluble, membrane-free-fraction isolated form hSP of normozoospermic men were analyzed using gel filtration and lectin blotting using WGA (wheat germ agglutinin) and Con A (concanavalin A).

Results: Widely distributed GGT (with two to three partially resolved peaks), which may correspond to high molecular mass aggregates, were detected. GGT-associated patterns of selected glycoproteins (at position of big, medium, and small-GGT) all comprised high molecular mass WGA-reactive smears, but differed in the presence of Con A-reactive glycans, as well as mucin-associated antigens CA19-9 and CA125.

Conclusions: GGT contributes to several molecular patterns that differ between the soluble and extracellular vesicle fractions of hSP. Their glycobiochemical heterogeneity is due to difference in the presence of distinct sialylated and mannosylated glycans. Moreover, GGT-associated glycoprotein patterns differentiate between high molecular mass forms of GGT in the soluble fraction of hSP. They hold promise as possible targets for increasing biomarker potential of GGT.

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