期刊
GLYCOBIOLOGY
卷 30, 期 11, 页码 895-909出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwaa034
关键词
galectin; glycosylation; pregnancy specific glycoproteins
资金
- National Institutes of Health [R01GM070589, R21AI120918]
- Collaborative Health Initiative Research Program at USUHS [401738]
- National Institutes of Health/National Cancer Institute Alliance of Glycobiologists for Cancer Research: Biological Tumor Glycomics Laboratory [U01 CA225644]
- National Institutes of Health/National Institute of Allergy and Infectious Diseases [R21 AI146368]
- Mizutani Foundation for Glycoscience Research [17-0093]
- Biotechnology and Biological Sciences Research Council [BB/F008309/1]
- Deutsche Forschungsgemeinschaft (DFG) through the Heisenberg Program [BL1115/3-1, BL1115/7-1, BL1115/4-1]
- National Science Foundation [IOS-1656720, IOS-1050518]
- BBSRC [BB/F008309/1, BB/K016164/1] Funding Source: UKRI
Pregnancy-specific beta 1 glycoprotein (PSG1) is secreted from trophoblast cells of the human placenta in increasing concentrations as pregnancy progresses, becoming one of the most abundant proteins in maternal serum in the third trimester. PSG1 has seven potential N-linked glycosylation sites across its four domains. We carried out glycomic and glycoproteomic studies to characterize the glycan composition of PSG1 purified from serum of pregnant women and identified the presence of complex N-glycans containing poly LacNAc epitopes with alpha 2,3 sialyation at four sites. Using different techniques, we explored whether PSG1 can bind to galectin-1 (Gal-1) as these two proteins were previously shown to participate in processes required for a successful pregnancy. We confirmed that PSG1 binds to Gal-1 in a carbohydrate-dependent manner with an affinity of the interaction of 0.13 mu M. In addition, we determined that out of the three N-glycosylation-carrying domains, only the N and A2 domains of recombinant PSG1 interact with Gal-1. Lastly, we observed that the interaction between PSG1 and Gal-1 protects this lectin from oxidative inactivation and that PSG1 competes the ability of Gal-1 to bind to some but not all of its glycoprotein ligands.
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