Silencing the Nucleocytoplasmic O-GlcNAc ...
Document type :
Article dans une revue scientifique
DOI :
PMID :
Permalink :
Title :
Silencing the Nucleocytoplasmic O-GlcNAc Transferase Reduces Proliferation, Adhesion, and Migration of Cancer and Fetal Human Colon Cell Lines
Author(s) :
Steenackers, Agata [Auteur]
Olivier-Van Stichelen, Stéphanie [Auteur]
Baldini, Steffi F. [Auteur]
Dehennaut, Vanessa [Auteur]
Toillon, Robert-Alain [Auteur]
Le Bourhis, Xuefen [Auteur]
Plasticité Cellulaire et Cancer - U908 [CPAC]
El Yazidi-Belkoura, Ikram [Auteur]
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Olivier-Van Stichelen, Stéphanie [Auteur]
Baldini, Steffi F. [Auteur]
Dehennaut, Vanessa [Auteur]
Toillon, Robert-Alain [Auteur]
Le Bourhis, Xuefen [Auteur]
Plasticité Cellulaire et Cancer - U908 [CPAC]
El Yazidi-Belkoura, Ikram [Auteur]
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Journal title :
Frontiers in endocrinology
Abbreviated title :
Front Endocrinol (Lausanne)
Volume number :
7
Pages :
46
Publication date :
2016
ISSN :
1664-2392
English keyword(s) :
O-GlcNAcylation
siRNA
colorectal cancer
O-linked N-acetylglucosamine transferase
colon cell lines
siRNA
colorectal cancer
O-linked N-acetylglucosamine transferase
colon cell lines
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
The post-translational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is regulated by a unique couple of enzymes. O-GlcNAc transferase (OGT) transfers the GlcNAc residue from UDP-GlcNAc, the final ...
Show more >The post-translational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is regulated by a unique couple of enzymes. O-GlcNAc transferase (OGT) transfers the GlcNAc residue from UDP-GlcNAc, the final product of the hexosamine biosynthetic pathway (HBP), whereas O-GlcNAcase (OGA) removes it. This study and others show that OGT and O-GlcNAcylation levels are increased in cancer cell lines. In that context, we studied the effect of OGT silencing in the colon cancer cell lines HT29 and HCT116 and the primary colon cell line CCD841CoN. Herein, we report that OGT silencing diminished proliferation, in vitro cell survival and adhesion of primary and cancer cell lines. SiOGT dramatically decreased HT29 and CCD841CoN migration, CCD841CoN harboring high capabilities of migration in Boyden chamber system when compared to HT29 and HCT116. The expression levels of actin and tubulin were unaffected by OGT knockdown but siOGT seemed to disorganize microfilament, microtubule, and vinculin networks in CCD841CoN. While cancer cell lines harbor higher levels of OGT and O-GlcNAcylation to fulfill their proliferative and migratory properties, in agreement with their higher consumption of HBP main substrates glucose and glutamine, our data demonstrate that OGT expression is not only necessary for the biological properties of cancer cell lines but also for normal cells.Show less >
Show more >The post-translational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is regulated by a unique couple of enzymes. O-GlcNAc transferase (OGT) transfers the GlcNAc residue from UDP-GlcNAc, the final product of the hexosamine biosynthetic pathway (HBP), whereas O-GlcNAcase (OGA) removes it. This study and others show that OGT and O-GlcNAcylation levels are increased in cancer cell lines. In that context, we studied the effect of OGT silencing in the colon cancer cell lines HT29 and HCT116 and the primary colon cell line CCD841CoN. Herein, we report that OGT silencing diminished proliferation, in vitro cell survival and adhesion of primary and cancer cell lines. SiOGT dramatically decreased HT29 and CCD841CoN migration, CCD841CoN harboring high capabilities of migration in Boyden chamber system when compared to HT29 and HCT116. The expression levels of actin and tubulin were unaffected by OGT knockdown but siOGT seemed to disorganize microfilament, microtubule, and vinculin networks in CCD841CoN. While cancer cell lines harbor higher levels of OGT and O-GlcNAcylation to fulfill their proliferative and migratory properties, in agreement with their higher consumption of HBP main substrates glucose and glutamine, our data demonstrate that OGT expression is not only necessary for the biological properties of cancer cell lines but also for normal cells.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Collections :
Research team(s) :
O-GlcNAcylation, signalisation cellulaire et cycle cellulaire
Submission date :
2020-02-12T15:11:47Z
2021-06-14T06:33:22Z
2021-06-14T06:33:22Z