Investigation of N-Acetyllactosamine and N,N-Diacetyllactosamine Residues of Seminal Plasma Prolactin-Induced Protein as Ligands Recognized by Galectin-3
Prolactin induced-protein (PIP) has been found to be rich in immunomodulatory epitopes, including N-acetyllactosamine (LacNAc) and N,N-diacetyllactosamine (LacdiNAc) residues, which may constitute ligands for galecin-3 (Gal-3). In the current study, we aimed to investigate the reactivity of galactos...
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Published in | International journal of molecular sciences Vol. 25; no. 24; p. 13432 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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ISSN | 1422-0067 1661-6596 1422-0067 |
DOI | 10.3390/ijms252413432 |
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Abstract | Prolactin induced-protein (PIP) has been found to be rich in immunomodulatory epitopes, including N-acetyllactosamine (LacNAc) and N,N-diacetyllactosamine (LacdiNAc) residues, which may constitute ligands for galecin-3 (Gal-3). In the current study, we aimed to investigate the reactivity of galactose- and N-acetylgalactosamine-specific lectins with human seminal plasma PIP. Subsequently, we examined the direct interaction between seminal plasma PIP and galectin-3, and next analyzed whether there are any differences in the interaction associated with impaired semen parameters. The reactivity of terminal galactose-presenting glycans in seminal plasma PIP with Ricinus communis agglutinin I in the asthenozoospermic group was significantly higher compared to the normozoospermic fertile subjects. Investigating the reactivity of Wisteria floribunda lectin with PIP glycans, we found likewise significantly higher relative reactivity in the normozoospermic infertile as well as the oligoasthenozoopermic group compared to the control group. These results are related to the expression of LacdiNAc epitopes in the oligosaccharide chain of PIP. Finally, we observed that PIP reactivity with Wisteria floribunda lectin correlates positively with the interaction between galectin-3 and PIP in the seminal plasma. This can suggest that LacdiNAc residues are engaged in the interaction between PIP and galectin-3. |
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AbstractList | Prolactin induced-protein (PIP) has been found to be rich in immunomodulatory epitopes, including
-acetyllactosamine (LacNAc) and
,
-diacetyllactosamine (LacdiNAc) residues, which may constitute ligands for galecin-3 (Gal-3). In the current study, we aimed to investigate the reactivity of galactose- and
-acetylgalactosamine-specific lectins with human seminal plasma PIP. Subsequently, we examined the direct interaction between seminal plasma PIP and galectin-3, and next analyzed whether there are any differences in the interaction associated with impaired semen parameters. The reactivity of terminal galactose-presenting glycans in seminal plasma PIP with
agglutinin I in the asthenozoospermic group was significantly higher compared to the normozoospermic fertile subjects. Investigating the reactivity of
lectin with PIP glycans, we found likewise significantly higher relative reactivity in the normozoospermic infertile as well as the oligoasthenozoopermic group compared to the control group. These results are related to the expression of LacdiNAc epitopes in the oligosaccharide chain of PIP. Finally, we observed that PIP reactivity with
lectin correlates positively with the interaction between galectin-3 and PIP in the seminal plasma. This can suggest that LacdiNAc residues are engaged in the interaction between PIP and galectin-3. Prolactin induced-protein (PIP) has been found to be rich in immunomodulatory epitopes, including N-acetyllactosamine (LacNAc) and N,N-diacetyllactosamine (LacdiNAc) residues, which may constitute ligands for galecin-3 (Gal-3). In the current study, we aimed to investigate the reactivity of galactose- and N-acetylgalactosamine-specific lectins with human seminal plasma PIP. Subsequently, we examined the direct interaction between seminal plasma PIP and galectin-3, and next analyzed whether there are any differences in the interaction associated with impaired semen parameters. The reactivity of terminal galactose-presenting glycans in seminal plasma PIP with Ricinus communis agglutinin I in the asthenozoospermic group was significantly higher compared to the normozoospermic fertile subjects. Investigating the reactivity of Wisteria floribunda lectin with PIP glycans, we found likewise significantly higher relative reactivity in the normozoospermic infertile as well as the oligoasthenozoopermic group compared to the control group. These results are related to the expression of LacdiNAc epitopes in the oligosaccharide chain of PIP. Finally, we observed that PIP reactivity with Wisteria floribunda lectin correlates positively with the interaction between galectin-3 and PIP in the seminal plasma. This can suggest that LacdiNAc residues are engaged in the interaction between PIP and galectin-3. Prolactin induced-protein (PIP) has been found to be rich in immunomodulatory epitopes, including N-acetyllactosamine (LacNAc) and N,N-diacetyllactosamine (LacdiNAc) residues, which may constitute ligands for galecin-3 (Gal-3). In the current study, we aimed to investigate the reactivity of galactose- and N-acetylgalactosamine-specific lectins with human seminal plasma PIP. Subsequently, we examined the direct interaction between seminal plasma PIP and galectin-3, and next analyzed whether there are any differences in the interaction associated with impaired semen parameters. The reactivity of terminal galactose-presenting glycans in seminal plasma PIP with Ricinus communis agglutinin I in the asthenozoospermic group was significantly higher compared to the normozoospermic fertile subjects. Investigating the reactivity of Wisteria floribunda lectin with PIP glycans, we found likewise significantly higher relative reactivity in the normozoospermic infertile as well as the oligoasthenozoopermic group compared to the control group. These results are related to the expression of LacdiNAc epitopes in the oligosaccharide chain of PIP. Finally, we observed that PIP reactivity with Wisteria floribunda lectin correlates positively with the interaction between galectin-3 and PIP in the seminal plasma. This can suggest that LacdiNAc residues are engaged in the interaction between PIP and galectin-3.Prolactin induced-protein (PIP) has been found to be rich in immunomodulatory epitopes, including N-acetyllactosamine (LacNAc) and N,N-diacetyllactosamine (LacdiNAc) residues, which may constitute ligands for galecin-3 (Gal-3). In the current study, we aimed to investigate the reactivity of galactose- and N-acetylgalactosamine-specific lectins with human seminal plasma PIP. Subsequently, we examined the direct interaction between seminal plasma PIP and galectin-3, and next analyzed whether there are any differences in the interaction associated with impaired semen parameters. The reactivity of terminal galactose-presenting glycans in seminal plasma PIP with Ricinus communis agglutinin I in the asthenozoospermic group was significantly higher compared to the normozoospermic fertile subjects. Investigating the reactivity of Wisteria floribunda lectin with PIP glycans, we found likewise significantly higher relative reactivity in the normozoospermic infertile as well as the oligoasthenozoopermic group compared to the control group. These results are related to the expression of LacdiNAc epitopes in the oligosaccharide chain of PIP. Finally, we observed that PIP reactivity with Wisteria floribunda lectin correlates positively with the interaction between galectin-3 and PIP in the seminal plasma. This can suggest that LacdiNAc residues are engaged in the interaction between PIP and galectin-3. |
Audience | Academic |
Author | Trzęsicka, Katarzyna Drzyzga, Damian Kałuża, Anna Ferens-Sieczkowska, Mirosława |
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Cites_doi | 10.3390/biom12020195 10.1155/2019/5397804 10.1021/bi034038a 10.1186/s12958-018-0334-1 10.3109/1354750X.2012.699555 10.1002/pros.21287 10.1002/chem.202100800 10.1021/acs.jproteome.5b01069 10.1007/s00018-008-8463-x 10.1016/j.ijbiomac.2011.12.015 10.1155/2014/981627 10.1002/adsc.201700331 10.1155/2011/798072 10.3390/ijms22147331 10.4236/oji.2013.34026 10.1021/acschembio.1c00689 10.1093/molehr/gaz030 10.1002/mrd.22500 10.1002/jssc.200700686 10.1007/s10719-009-9262-9 10.4049/jimmunol.173.3.1902 10.1111/aji.12273 10.1016/S0165-0378(03)00084-6 10.1021/bi051144z 10.1074/jbc.M115.651497 10.1016/j.molcatb.2013.12.018 10.1038/s41577-022-00829-7 10.1111/j.2047-2927.2013.00099.x 10.1074/jbc.C112.358002 10.3390/ijms19020372 10.3389/fimmu.2019.01166 10.1016/j.mcpro.2022.100214 10.1093/humrep/den024 10.1007/s00281-020-00801-4 10.3389/fimmu.2012.00199 10.3390/biom5031671 |
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Snippet | Prolactin induced-protein (PIP) has been found to be rich in immunomodulatory epitopes, including N-acetyllactosamine (LacNAc) and N,N-diacetyllactosamine... Prolactin induced-protein (PIP) has been found to be rich in immunomodulatory epitopes, including -acetyllactosamine (LacNAc) and , -diacetyllactosamine... |
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SubjectTerms | Adult Amino Sugars - metabolism Analysis Antigenic determinants Blood Proteins Carbohydrates Galactose Galectin 3 - metabolism Galectins Glycodelin Glycoproteins Glycoproteins - metabolism Humans Immunomodulators Infertility Inflammation Investigations Lectins Ligands Male Membrane Transport Proteins Plant Lectins - chemistry Plant Lectins - metabolism Plasma Polysaccharides Polysaccharides - chemistry Polysaccharides - metabolism Preferences Prolactin Protein Binding Proteins Semen - chemistry Semen - metabolism Sperm |
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Title | Investigation of N-Acetyllactosamine and N,N-Diacetyllactosamine Residues of Seminal Plasma Prolactin-Induced Protein as Ligands Recognized by Galectin-3 |
URI | https://www.ncbi.nlm.nih.gov/pubmed/39769197 https://www.proquest.com/docview/3149647443 https://www.proquest.com/docview/3160920617 |
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