Imperial College London
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ProfessorStuartHaslam

Faculty of Natural Sciences, Department of Life Sciences

Professor in Structural Glycobiology
 
 
 
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Contact

 

+44 (0)20 7594 5222s.haslam

 
 
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Location

 

101ASir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Hautala:2020:10.1038/s41374-020-0411-x,
author = {Hautala, LC and Pang, P-C and Antonopoulos, A and Pasanen, A and Lee, C-L and Chiu, PCN and Yeung, WSB and Loukovaara, M and Butzow, R and Haslam, SM and Dell, A and Koistinen, H},
doi = {10.1038/s41374-020-0411-x},
journal = {Laboratory Investigation},
pages = {1014--1025},
title = {Altered glycosylation of glycodelin in endometrial carcinoma},
url = {http://dx.doi.org/10.1038/s41374-020-0411-x},
volume = {100},
year = {2020}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Glycodelin is a major glycoprotein expressed in reproductive tissues, like secretory and decidualized endometrium. It has several reproduction related functions that are dependent on specific glycosylation, but it has also been found to drive differentiation of endometrial carcinoma cells toward a less malignant phenotype. Here we aimed to elucidate whether the glycosylation and function of glycodelin is altered in endometrial carcinoma as compared with a normal endometrium. We carried out glycan structure analysis of glycodelin expressed in HEC-1B human endometrial carcinoma cells (HEC-1B Gd) by mass spectrometry glycomics strategies. Glycans of HEC-1B Gd were found to comprise a typical mixture of high-mannose, hybrid, and complex-type N-glycans, often containing undecorated LacNAc (Galβ1–4GlcNAc) antennae. However, several differences, as compared with previously reported glycan structures of normal human decidualized endometrium-derived glycodelin isoform, glycodelin-A (GdA), were also found. These included a lower level of sialylation and more abundant poly-LacNAc antennae, some of which are fucosylated. This allowed us to select lectins that showed different binding to these classes of glycodelin. Despite the differences in glycosylation between HEC-1B Gd and GdA, both showed similar inhibitory activity on trophoblast cell invasion and peripheral blood mononuclear cell proliferation. For the detection of cancer associated glycodelin, we established a novel in situ proximity-ligation based histochemical staining method using a specific glycodelin antibody and UEAI lectin. We found that the UEAI reactive glycodelin was abundant in endometrial carcinoma, but virtually absent in normal endometrial tissue even when glycodelin was strongly expressed. In conclusion, we established a histochemical staining method for the detection of endometrial carcinoma-associated glycodelin and showed that this specific glycodelin is exclusively expressed in cancer, not
AU  - Hautala,LC
AU  - Pang,P-C
AU  - Antonopoulos,A
AU  - Pasanen,A
AU  - Lee,C-L
AU  - Chiu,PCN
AU  - Yeung,WSB
AU  - Loukovaara,M
AU  - Butzow,R
AU  - Haslam,SM
AU  - Dell,A
AU  - Koistinen,H
DO  - 10.1038/s41374-020-0411-x
EP  - 1025
PY  - 2020///
SN  - 0023-6837
SP  - 1014
TI  - Altered glycosylation of glycodelin in endometrial carcinoma
T2  - Laboratory Investigation
UR  - http://dx.doi.org/10.1038/s41374-020-0411-x
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000521525000001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/78020
VL  - 100
ER  -
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