ArticleGlycoconjugate journal2014
Changes in fucosylation of human seminal IgG and secretory component of IgA in leukocytospermic patients.
Article in Glycoconjugate journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Developing glycoproteomics reveals the role of posttranslational glycosylation in the physiological and pathological processes of male reproduction.iMetaOmics · 2024Article
- The Alterations of Serum IgG Fucosylation as a Potential Additional New Diagnostic Marker in Advanced Endometriosis.Journal of inflammation research · 2022Article
- Substrate specificity of FUT8 and chemoenzymatic synthesis of core-fucosylated asymmetric N-glycans.Organic & biomolecular chemistry · 2016Article
- Changes in glycosylation of human blood plasma chitotriosidase in patients with type 2 diabetes.Glycoconjugate journal · 2016Article
- Terminal Mannose Residues in Seminal Plasma Glycoproteins of Infertile Men Compared to Fertile Donors.International journal of molecular sciences · 2015Article
- The analysis of sialylation, N-glycan branching, and expression of O-glycans in seminal plasma of infertile men.Disease markers · 2015Article
- Glycoprotein fucosylation is increased in seminal plasma of subfertile men.Asian journal of andrologyArticle
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Authors and funding
4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Our study compares the status of human seminal plasma immunoglobulin G (IgG) and IgA secretory component (SC) fucosylation between infertile leukocytospermic and normal, fertile normozoospermic patients. The seminal IgG and SC are decorated with AAL-reactive core fucose, and antennary UEA- and LTA-reactive fucose of Lewis(y) and Lewis(x) structures, respectively. However, a correlation between IgG core fucosylation and IgG concentration (r = -0.52; p < 0.0003) was observed. The IgG present in leukocytospermic samples is characterized by lower expression of core fucose than in the normal group (0.82 ± 0.3 AU and 1.2 ± 0.3 AU, respectively; p < 0.002). In seminal plasma the SC is present in two forms: 78-kDa and 63-kDa. The present study has also shown a higher AAL and LTA specific reactivity of glycans expressed in 63-kDa SC, in comparison to 78-kDa SC, in the normal group. In leukocytospermia, the values of specific lectin reactivity for core fucose, fucose α(1-2)- and α(1-3)- linked, were similar for both SC bands. Moreover, the present study has shown that in leukocytospermic samples the mean concentrations of IgG and S-IgA are twice as high (131.68 ± 102.6 mg/l and 36 ± 27 mg/l, respectively) as in the normal group (67.68 ± 29.2 mg/l; p < 0.02, and 19 ± 18 mg/l, p < 0.019, respectively). The analysis of IgG and SC fucosylation status and the determination of IgG and S-IgA concentrations in seminal plasma might constitute a valuable diagnosis tools for the evaluation of male infertility associated with leukocytospermia with accompanying inflammation.
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