Imperial College London
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DrPeiLai

Faculty of Medicine, Department of Metabolism, Digestion and Reproduction

Research Associate
 
 
 
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Contact

 

p.lai

 
 
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Location

 

Chelsea and Westminster HospitalChelsea and Westminster Campus

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Summary

 

Publications

Citation

BibTex format

@article{Huang:2023:10.1042/BST20221406,
author = {Huang, Z and Lai, PF and Cocker, ATH and Haslam, SM and Dell, A and Brady, HJM and Johnson, MR},
doi = {10.1042/BST20221406},
journal = {Biochemical Society Transactions},
pages = {639--653},
title = {Roles of N-linked glycosylation and glycan-binding proteins in placentation: trophoblast infiltration, immunomodulation, angiogenesis, and pathophysiology},
url = {http://dx.doi.org/10.1042/BST20221406},
volume = {51},
year = {2023}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Protein N-linked glycosylation is a structurally diverse post-translational modification that stores biological information in a larger order of magnitude than other post-translational modifications such as phosphorylation, ubiquitination and acetylation. This gives N-glycosylated proteins a diverse range of properties and allows glyco-codes (glycan-related information) to be deciphered by glycan-binding proteins (GBPs). The intervillous space of the placenta is richly populated with membrane-bound and secreted glycoproteins. Evidence exists to suggest that altering the structural nature of their N-glycans can impact several trophoblast functions, which include those related to interactions with decidual cells. This review summarizes trophoblast-related activities influenced by N-glycan-GBP recognition, exploring how different subtypes of trophoblasts actively adapt to characteristics of the decidualized endometrium through cell-specific expression of N-glycosylated proteins, and how these cells receive decidua-derived signals via N-glycan-GBP interactions. We highlight work on how changes in N-glycosylation relates to the success of trophoblast infiltration, interactions of immunomodulators, and uterine angiogenesis. We also discuss studies that suggest aberrant N-glycosylation of trophoblasts may contribute to the pathogenesis of pregnancy complications (e.g. pre-eclampsia, early spontaneous miscarriages and hydatidiform mole). We propose that a more in-depth understanding of how N-glycosylation shapes trophoblast phenotype during early pregnancy has the potential to improve our approach to predicting, diagnosing and alleviating poor maternal/fetal outcomes associated with placental dysfunction.
AU  - Huang,Z
AU  - Lai,PF
AU  - Cocker,ATH
AU  - Haslam,SM
AU  - Dell,A
AU  - Brady,HJM
AU  - Johnson,MR
DO  - 10.1042/BST20221406
EP  - 653
PY  - 2023///
SN  - 0300-5127
SP  - 639
TI  - Roles of N-linked glycosylation and glycan-binding proteins in placentation: trophoblast infiltration, immunomodulation, angiogenesis, and pathophysiology
T2  - Biochemical Society Transactions
UR  - http://dx.doi.org/10.1042/BST20221406
UR  - https://www.ncbi.nlm.nih.gov/pubmed/36929183
UR  - http://hdl.handle.net/10044/1/104325
VL  - 51
ER  -
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