Imperial College London
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Dr Poh-Choo Pang

Faculty of Natural Sciences, Department of Life Sciences

Visiting Researcher
 
 
 
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Contact

 

p.pang05 Website

 
 
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Location

 

Room 3158 Prince's GateSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Lee:2009:10.1074/jbc.M807960200,
author = {Lee, C and Pang, P and Yeung, WSB and Tissot, B and Panico, M and Lao, TTH and Chu, IK and Lee, K and Chung, M and Lam, KKW and Koistinen, R and Koistinen, H and Seppälä, M and Morris, HR and Dell, A and Chiu, PCN},
doi = {10.1074/jbc.M807960200},
journal = {Journal of Biological Chemistry},
pages = {15084--15096},
title = {Effects of Differential Glycosylation of Glycodelins on Lymphocyte Survival},
url = {http://dx.doi.org/10.1074/jbc.M807960200},
volume = {284},
year = {2009}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Glycodelin is a human glycoprotein with four reported glycoforms, namely glycodelin-A (GdA), glycodelin-F (GdF), glycodelin-C (GdC), and glycodelin-S (GdS). These glycoforms have the same protein core and appear to differ in their N-glycosylation. The glycosylation of GdA is completely different from that of GdS. GdA inhibits proliferation and induces cell death of T cells. However, the glycosylation and immunomodulating activities of GdF and GdC are not known. This study aimed to use ultra-high sensitivity mass spectrometry to compare the glycomes of GdA, GdC, and GdF and to study the relationship between the immunological activity and glycosylation pattern among glycodelin glycoforms. Using MALDI-TOF strategies, the glycoforms were shown to contain an enormous diversity of bi-, tri-, and tetra-antennary complex-type glycans carrying Galβ1–4GlcNAc (lacNAc) and/or GalNAcβ1–4GlcNAc (lacdiNAc) antennae backbones with varying levels of fucose and sialic acid substitution. Interestingly, they all carried a family of Sda (NeuAcα2–3(GalNAcβ1–4)Gal)-containing glycans, which were not identified in the earlier study because of less sensitive methodologies used. Among the three glycodelins, GdA is the most heavily sialylated. Virtually all the sialic acid on GdC is located on the Sda antennae. With the exception of the Sda epitope, the GdC N-glycome appears to be the asialylated counterpart of the GdA/GdF glycomes. Sialidase activity, which may be responsible for transforming GdA/GdF to GdC, was detected in cumulus cells. Both GdA and GdF inhibited the proliferation, induced cell death, and suppressed interleukin-2 secretion of Jurkat cells and peripheral blood mononuclear cells. In contrast, no immunosuppressive effect was observed for GdS and GdC.
AU  - Lee,C
AU  - Pang,P
AU  - Yeung,WSB
AU  - Tissot,B
AU  - Panico,M
AU  - Lao,TTH
AU  - Chu,IK
AU  - Lee,K
AU  - Chung,M
AU  - Lam,KKW
AU  - Koistinen,R
AU  - Koistinen,H
AU  - Seppälä,M
AU  - Morris,HR
AU  - Dell,A
AU  - Chiu,PCN
DO  - 10.1074/jbc.M807960200
EP  - 15096
PY  - 2009///
SP  - 15084
TI  - Effects of Differential Glycosylation of Glycodelins on Lymphocyte Survival
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1074/jbc.M807960200
UR  - http://www.jbc.org/content/284/22/15084.abstract
UR  - http://hdl.handle.net/10044/1/15582
VL  - 284
ER  -
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