Imperial College London
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ProfessorAnneDell

Faculty of Natural Sciences, Department of Life Sciences

Professor of Carbohydrate Bichemistry
 
 
 
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Contact

 

a.dell

 
 
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Location

 

101BSir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Mendoza:2020:glycob/cwaa034,
author = {Mendoza, M and Lu, D and Ballesteros, A and Blois, SM and Abernathy, K and Feng, C and Dimitroff, CJ and Zmuda, J and Panico, M and Dell, A and Vasta, GR and Haslam, SM and Dveksler, G},
doi = {glycob/cwaa034},
journal = {Glycobiology},
pages = {895--909},
title = {Glycan characterization of pregnancy-specific glycoprotein 1 and its identification as a novel Galectin-1 ligand},
url = {http://dx.doi.org/10.1093/glycob/cwaa034},
volume = {30},
year = {2020}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - 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.
AU  - Mendoza,M
AU  - Lu,D
AU  - Ballesteros,A
AU  - Blois,SM
AU  - Abernathy,K
AU  - Feng,C
AU  - Dimitroff,CJ
AU  - Zmuda,J
AU  - Panico,M
AU  - Dell,A
AU  - Vasta,GR
AU  - Haslam,SM
AU  - Dveksler,G
DO  - glycob/cwaa034
EP  - 909
PY  - 2020///
SN  - 0959-6658
SP  - 895
TI  - Glycan characterization of pregnancy-specific glycoprotein 1 and its identification as a novel Galectin-1 ligand
T2  - Glycobiology
UR  - http://dx.doi.org/10.1093/glycob/cwaa034
UR  - https://www.ncbi.nlm.nih.gov/pubmed/32280962
UR  - https://academic.oup.com/glycob/article/doi/10.1093/glycob/cwaa034/5818751
UR  - http://hdl.handle.net/10044/1/78168
VL  - 30
ER  -
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