MGAT4A/Galectin9‐Driven N‐Glycosylation Aberration as a Promoting Mechanism for Poor Prognosis of Endometrial Cancer with TP53 Mutation

Abstract Emerging evidence recognizes aberrant glycosylation as the malignant characteristics of cancer cells, but little is known about glycogenes’ roles in endometrial carcinoma (EC), especially the most aggressive subtype carrying TP53 mutations. Using unsupervised hierarchical clustering, an 11‐...

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Main Authors: Zhen Zhu, Jingya Sun, Weiqing Xu, Qinghe Zeng, Hanyi Feng, Lijuan Zang, Yinyan He, Xiao He, Na Sheng, Xuelian Ren, Guobin Liu, He Huang, Ruimin Huang, Jun Yan
Format: Article
Language:English
Published: Wiley 2024-12-01
Series:Advanced Science
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Online Access:https://doi.org/10.1002/advs.202409764
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author Zhen Zhu
Jingya Sun
Weiqing Xu
Qinghe Zeng
Hanyi Feng
Lijuan Zang
Yinyan He
Xiao He
Na Sheng
Xuelian Ren
Guobin Liu
He Huang
Ruimin Huang
Jun Yan
author_facet Zhen Zhu
Jingya Sun
Weiqing Xu
Qinghe Zeng
Hanyi Feng
Lijuan Zang
Yinyan He
Xiao He
Na Sheng
Xuelian Ren
Guobin Liu
He Huang
Ruimin Huang
Jun Yan
author_sort Zhen Zhu
collection DOAJ
description Abstract Emerging evidence recognizes aberrant glycosylation as the malignant characteristics of cancer cells, but little is known about glycogenes’ roles in endometrial carcinoma (EC), especially the most aggressive subtype carrying TP53 mutations. Using unsupervised hierarchical clustering, an 11‐glycogene cluster is identified to distinguish an EC subtype associated with frequent TP53 mutation and worse prognosis. Among them, MGAT4A (alpha‐1,3‐mannosyl‐glycoprotein 4‐β‐N‐acetylglucosaminyltransferase A) emerges as the most consistently overexpressed glycogene, contributing to EC aggressiveness. In the presence of galectin‐9, MGAT4A increases EC cell proliferation and invasion via promoting glucose metabolism. N‐glycoproteomics further revealed GLUT1, a glucose transporter, as a glycoprotein modified by MGAT4A. Binding of galectin‐9 to the MGAT4A‐branched N‐glycan on GLUT1 enhances its cell membrane distribution, leading to glucose uptake increase. In addition, oncogenic mutations of TP53 gene in EC cells upregulate MGAT4A expression by disrupting the regulatory oversight exerted by wild‐type p53 on tumor‐suppressive miRNAs, including miR‐34a and miR‐449a/b. The findings highlight a new molecular mechanism involving MGAT4A‐regulated N‐glycosylation on the key regulator of glucose metabolism in p53 mutants‐driven EC aggressiveness, which may provide a strategic avenue to combat advanced EC.
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spelling doaj-art-e7345274041041919a74dae11f25bace2025-08-20T02:55:53ZengWileyAdvanced Science2198-38442024-12-011148n/an/a10.1002/advs.202409764MGAT4A/Galectin9‐Driven N‐Glycosylation Aberration as a Promoting Mechanism for Poor Prognosis of Endometrial Cancer with TP53 MutationZhen Zhu0Jingya Sun1Weiqing Xu2Qinghe Zeng3Hanyi Feng4Lijuan Zang5Yinyan He6Xiao He7Na Sheng8Xuelian Ren9Guobin Liu10He Huang11Ruimin Huang12Jun Yan13Center for Medical Research and Innovation Shanghai Pudong Hospital Fudan University Pudong Medical Center; Laboratory Animal Center Fudan University Shanghai 200032 ChinaCenter for Drug Safety Evaluation and Research Shanghai Institute of Materia Medica Chinese Academy of Sciences Shanghai 201203 ChinaDepartment of Pathology Shanghai General Hospital Shanghai Jiao Tong University School of Medicine Shanghai 200080 ChinaCenter for Drug Safety Evaluation and Research Shanghai Institute of Materia Medica Chinese Academy of Sciences Shanghai 201203 ChinaCenter for Drug Safety Evaluation and Research Shanghai Institute of Materia Medica Chinese Academy of Sciences Shanghai 201203 ChinaDepartment of Pathology Shanghai General Hospital Shanghai Jiao Tong University School of Medicine Shanghai 200080 ChinaDepartment of Obstetrics and Gynecology Shanghai General Hospital Shanghai Jiao Tong University School of Medicine Shanghai 200080 ChinaCenter for Drug Safety Evaluation and Research Shanghai Institute of Materia Medica Chinese Academy of Sciences Shanghai 201203 ChinaModel Animal Research Center of Nanjing University Nanjing 210061 ChinaState Key Laboratory of Chemical Biology Shanghai Institute of Materia Medica Chinese Academy of Sciences Shanghai 201203 ChinaState Key Laboratory of Chemical Biology Shanghai Institute of Materia Medica Chinese Academy of Sciences Shanghai 201203 ChinaState Key Laboratory of Chemical Biology Shanghai Institute of Materia Medica Chinese Academy of Sciences Shanghai 201203 ChinaCenter for Drug Safety Evaluation and Research Shanghai Institute of Materia Medica Chinese Academy of Sciences Shanghai 201203 ChinaCenter for Medical Research and Innovation Shanghai Pudong Hospital Fudan University Pudong Medical Center; Laboratory Animal Center Fudan University Shanghai 200032 ChinaAbstract Emerging evidence recognizes aberrant glycosylation as the malignant characteristics of cancer cells, but little is known about glycogenes’ roles in endometrial carcinoma (EC), especially the most aggressive subtype carrying TP53 mutations. Using unsupervised hierarchical clustering, an 11‐glycogene cluster is identified to distinguish an EC subtype associated with frequent TP53 mutation and worse prognosis. Among them, MGAT4A (alpha‐1,3‐mannosyl‐glycoprotein 4‐β‐N‐acetylglucosaminyltransferase A) emerges as the most consistently overexpressed glycogene, contributing to EC aggressiveness. In the presence of galectin‐9, MGAT4A increases EC cell proliferation and invasion via promoting glucose metabolism. N‐glycoproteomics further revealed GLUT1, a glucose transporter, as a glycoprotein modified by MGAT4A. Binding of galectin‐9 to the MGAT4A‐branched N‐glycan on GLUT1 enhances its cell membrane distribution, leading to glucose uptake increase. In addition, oncogenic mutations of TP53 gene in EC cells upregulate MGAT4A expression by disrupting the regulatory oversight exerted by wild‐type p53 on tumor‐suppressive miRNAs, including miR‐34a and miR‐449a/b. The findings highlight a new molecular mechanism involving MGAT4A‐regulated N‐glycosylation on the key regulator of glucose metabolism in p53 mutants‐driven EC aggressiveness, which may provide a strategic avenue to combat advanced EC.https://doi.org/10.1002/advs.202409764endometrial cancerglucose metabolismMGAT4AN‐glycosylationTP53 mutation
spellingShingle Zhen Zhu
Jingya Sun
Weiqing Xu
Qinghe Zeng
Hanyi Feng
Lijuan Zang
Yinyan He
Xiao He
Na Sheng
Xuelian Ren
Guobin Liu
He Huang
Ruimin Huang
Jun Yan
MGAT4A/Galectin9‐Driven N‐Glycosylation Aberration as a Promoting Mechanism for Poor Prognosis of Endometrial Cancer with TP53 Mutation
Advanced Science
endometrial cancer
glucose metabolism
MGAT4A
N‐glycosylation
TP53 mutation
title MGAT4A/Galectin9‐Driven N‐Glycosylation Aberration as a Promoting Mechanism for Poor Prognosis of Endometrial Cancer with TP53 Mutation
title_full MGAT4A/Galectin9‐Driven N‐Glycosylation Aberration as a Promoting Mechanism for Poor Prognosis of Endometrial Cancer with TP53 Mutation
title_fullStr MGAT4A/Galectin9‐Driven N‐Glycosylation Aberration as a Promoting Mechanism for Poor Prognosis of Endometrial Cancer with TP53 Mutation
title_full_unstemmed MGAT4A/Galectin9‐Driven N‐Glycosylation Aberration as a Promoting Mechanism for Poor Prognosis of Endometrial Cancer with TP53 Mutation
title_short MGAT4A/Galectin9‐Driven N‐Glycosylation Aberration as a Promoting Mechanism for Poor Prognosis of Endometrial Cancer with TP53 Mutation
title_sort mgat4a galectin9 driven n glycosylation aberration as a promoting mechanism for poor prognosis of endometrial cancer with tp53 mutation
topic endometrial cancer
glucose metabolism
MGAT4A
N‐glycosylation
TP53 mutation
url https://doi.org/10.1002/advs.202409764
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