ArticleMolecular & cellular proteomics : MCP2012
Tumor biomarker glycoproteins in the seminal plasma of healthy human males are endogenous ligands for DC-SIGN.
Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Amniotic fluid glycoproteins as potential ligands for macrophage galactose-type C-type lectin and their possible implications for immunoregulation during pregnancy.Scientific reports · 2025Article
- Article
- Ligand Recognition by the Macrophage Galactose-Type C-Type Lectin: Self or Non-Self?-A Way to Trick the Host's Immune System.International journal of molecular sciences · 2023Review
- Seminal Plasma Glycoproteins as Potential Ligands of Lectins Engaged in Immunity Regulation.International journal of environmental research and public health · 2022Review
- The possible association of clusterin fucosylation changes with male fertility disorders.Scientific reports · 2021Article
- Glycoproteins Presenting Galactose andInternational journal of molecular sciences · 2021Article
- Unusual N-type glycosylation of salivary prolactin-inducible protein (PIP): multiple LewisGlycoconjugate journal · 2018Article
- Reversed-phase separation methods for glycan analysis.Analytical and bioanalytical chemistry · 2017Review
- Functional glycosylation in the human and mammalian uterus.Fertility research and practice · 2015Review
- Investigation of galectin-3 function in the reproductive tract by identification of binding ligands in human seminal plasma.American journal of reproductive immunology (New York, N.Y. : 1989) · 2014Article
- The role of glycans in immune evasion: the human fetoembryonic defence system hypothesis revisited.Molecular human reproduction · 2014Review
- Attenuation of fibroblast growth factor signaling by poly-N-acetyllactosamine type glycans.FEBS letters · 2013Article
- Site-specific glycoforms of haptoglobin in liver cirrhosis and hepatocellular carcinoma.Molecular & cellular proteomics : MCP · 2013Article
- Manifestations of immune tolerance in the human female reproductive tract.Frontiers in immunology · 2013Article
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- Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
Abstract
DC-SIGN is an immune C-type lectin that is expressed on both immature and mature dendritic cells associated with peripheral and lymphoid tissues in humans. It is a pattern recognition receptor that binds to several pathogens including HIV-1, Ebola virus, Mycobacterium tuberculosis, Candida albicans, Helicobacter pylori, and Schistosoma mansoni. Evidence is now mounting that DC-SIGN also recognizes endogenous glycoproteins, and that such interactions play a major role in maintaining immune homeostasis in humans and mice. Autoantigens (neoantigens) are produced for the first time in the human testes and other organs of the male urogenital tract under androgenic stimulus during puberty. Such antigens trigger autoimmune orchitis if the immune response is not tightly regulated within this system. Endogenous ligands for DC-SIGN could play a role in modulating such responses. Human seminal plasma glycoproteins express a high level of terminal Lewis(x) and Lewis(y) carbohydrate antigens. These epitopes react specifically with the lectin domains of DC-SIGN. However, because the expression of these sequences is necessary but not sufficient for interaction with DC-SIGN, this study was undertaken to determine if any seminal plasma glycoproteins are also endogenous ligands for DC-SIGN. Glycoproteins bearing terminal Lewis(x) and Lewis(y) sequences were initially isolated by lectin affinity chromatography. Protein sequencing established that three tumor biomarker glycoproteins (clusterin, galectin-3 binding glycoprotein, prostatic acid phosphatase) and protein C inhibitor were purified by using this affinity method. The binding of DC-SIGN to these seminal plasma glycoproteins was demonstrated in both Western blot and immunoprecipitation studies. These findings have confirmed that human seminal plasma contains endogenous glycoprotein ligands for DC-SIGN that could play a role in maintaining immune homeostasis both in the male urogenital tract and the vagina after coitus.
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