Parillo F, Mancuso R, Vullo C, Catone G
Department of Veterinary Science, Faculty of Veterinary Medicine, University of Camerino-UNICAM, Matelica, Italy.
Reprod Domest Anim. 2010 Oct;45(5):821-31. doi: 10.1111/j.1439-0531.2009.01362.x.
This work was undertaken to determine the glycoconjugates secreted by the epithelium of the prostate in the intact stallion and castrated horse using lectin histochemical procedures in conjunction with enzymatic digestion and deglycosylation treatments. Additionally, anti-5 and 13-16-cytokeratin antibodies were used to localize epithelial basal cells. In the stallion, lectin histochemistry showed the following sugar residues in the Golgi zone of the glandular cells: α-Glu/Man, α-Fuc and β-Gal included in both O- and N-linked oligosaccharides as well as β-GalNAc, GlcNAc and α-Gal, which belonged to O-glycoproteins. β-Gal and β-GalNAc moieties were also noted subterminal to sialyl residues. Sialic acid specific lectins identified Neu-5Ac(α2,3-6)-β-Gal or Neu5Ac(α2,6)-β-GalNAc sequences in both N- and O-bound glycoproteins. The prostatic glandular cells of the castrated horse expressed some of the same sugar moieties found in the stallions, such as α-Glu/Man, α-Gal and GlcNAc, but significant differences were also noted. In particular, β-D-GalNAc was only detected subterminal to sialic acid, β-D-Gal-(1-3)-D-GalNAc was found in N-linked glycans, whereas β-D-Gal-(1-4)-D-GlcNAc and Neu5Acα2,6Gal/GalNAc were noted only in O-glycoproteins. These results indicate that the lectin binding patterns in glandular cells may be modified by sex hormones. No specific lectin labelling of basal cells was found in either the stallion or the castrated horse even though they were immunostained with specific anti-cytokeratin antibodies. These cells stained more strongly in the castrated horse than in the intact stallion suggesting that they are androgen responsive. The glycomolecules detected in the equine prostate secretions may contribute to the remodelling of the sperm surface, which occurs during sperm transit through the male genital tract and also after ejaculation in the seminal plasma. These changes may be important in the understanding of the stallion fertility.
本研究旨在利用凝集素组织化学方法,结合酶消化和去糖基化处理,确定完整种马和阉割马前列腺上皮分泌的糖缀合物。此外,使用抗5和13 - 16细胞角蛋白抗体定位上皮基底细胞。在种马中,凝集素组织化学显示腺细胞高尔基体区域存在以下糖残基:O - 连接和N - 连接寡糖中均含有的α - Glu/Man、α - Fuc和β - Gal,以及属于O - 糖蛋白的β - GalNAc、GlcNAc和α - Gal。β - Gal和β - GalNAc部分也存在于唾液酸残基的次末端。唾液酸特异性凝集素在N - 连接和O - 连接糖蛋白中均鉴定出Neu - 5Ac(α2,3 - 6)-β - Gal或Neu5Ac(α2,6)-β - GalNAc序列。阉割马的前列腺腺细胞表达了一些与种马相同的糖部分,如α - Glu/Man、α - Gal和GlcNAc,但也存在显著差异。特别是,β - D - GalNAc仅在唾液酸的次末端被检测到,β - D - Gal-(1 - 3)-D - GalNAc存在于N - 连接聚糖中,而β - D - Gal-(1 - 4)-D - GlcNAc和Neu5Acα2,6Gal/GalNAc仅在O - 糖蛋白中被发现。这些结果表明,腺细胞中的凝集素结合模式可能受性激素影响。在种马和阉割马中均未发现基底细胞有特异性凝集素标记,尽管它们用特异性抗细胞角蛋白抗体进行了免疫染色。这些细胞在阉割马中比在完整种马中染色更强,表明它们对雄激素有反应。在马前列腺分泌物中检测到的糖分子可能有助于精子表面的重塑,这一过程发生在精子通过雄性生殖道期间以及射精后在精浆中。这些变化可能对理解种马的生育能力很重要。