Glycan characterization of pregnancy-specific glycoprotein 1 and its identification as a novel Galectin-1 ligand
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Glycan characterization of pregnancy-specific glycoprotein 1 and its identification as a novel Galectin-1 ligand. / Mendoza, Mirian; Lu, Dongli; Ballesteros, Angela; Blois, Sandra M; Abernathy, Kelsey; Feng, Chiguang; Dimitroff, Charles J; Zmuda, Jonathan; Panico, Maria; Dell, Anne; Vasta, Gerardo R; Haslam, Stuart M; Dveksler, Gabriela.
In: GLYCOBIOLOGY, Vol. 30, No. 11, 21.10.2020, p. 895-909.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Glycan characterization of pregnancy-specific glycoprotein 1 and its identification as a novel Galectin-1 ligand
AU - Mendoza, Mirian
AU - Lu, Dongli
AU - Ballesteros, Angela
AU - Blois, Sandra M
AU - Abernathy, Kelsey
AU - Feng, Chiguang
AU - Dimitroff, Charles J
AU - Zmuda, Jonathan
AU - Panico, Maria
AU - Dell, Anne
AU - Vasta, Gerardo R
AU - Haslam, Stuart M
AU - Dveksler, Gabriela
N1 - Published by Oxford University Press 2020. This work is written by (a) US Government employee(s) and is in the public domain in the US.
PY - 2020/10/21
Y1 - 2020/10/21
N2 - 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.
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.
U2 - 10.1093/glycob/cwaa034
DO - 10.1093/glycob/cwaa034
M3 - SCORING: Journal article
C2 - 32280962
VL - 30
SP - 895
EP - 909
JO - GLYCOBIOLOGY
JF - GLYCOBIOLOGY
SN - 0959-6658
IS - 11
ER -