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Glycan characterization of pregnancy-specific glycoprotein 1 and its identification as a novel Galectin-1 ligand

Item Type:Article
Title:Glycan characterization of pregnancy-specific glycoprotein 1 and its identification as a novel Galectin-1 ligand
Creators Name:Mendoza, M. and Lu, D. and Ballesteros, A. and Blois, S.M. and Abernathy, K. and Feng, C. and Dimitroff, C.J. and Zmuda, J. and Panico, M. and Dell, A. and Vasta, G.R. and Haslam, S.M. and Dveksler, G.
Abstract: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 α2,3 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 μM. 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.
Keywords:Galectin, Glycosylation, Pregnancy Specific Glycoproteins
Publisher:Oxford University Press
Page Range:895-909
Date:November 2020
Official Publication:https://doi.org/10.1093/glycob/cwaa034
External Fulltext:View full text on PubMed Central
PubMed:View item in PubMed

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