OGT Controls the Expression and the Glycosylation of E‐cadherin, and Affects Glycosphingolipid Structures in Human Colon Cell Lines

Autor: Katarina Madunić, Céline Schulz, Tony Lefebvre, Manfred Wuhrer, Charlotte Clarisse, Anne-Sophie Vercoutter-Edouart, Marlène Mortuaire, James Biwi, Radoslaw P. Kozak, Daniel I. R. Spencer, Yann Guérardel, Christophe Biot
Přispěvatelé: Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Culham Science Centre [Abingdon], LeidenUniversity Medical Centre, LeidenUniversity Medical Center, CNRS UMR 8576, UGSF, Université de Lille, Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), CNRS, UMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Leiden University Medical Center (LUMC), Universiteit Leiden, CNRS, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF], Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Rok vydání: 2019
Předmět:
Epithelial-Mesenchymal Transition
Glycosylation
[SDV]Life Sciences [q-bio]
[SDV.CAN]Life Sciences [q-bio]/Cancer
[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]
Biology
N-Acetylglucosaminyltransferases
Biochemistry
glycomics
03 medical and health sciences
chemistry.chemical_compound
O-GlcNAcylation
Downregulation and upregulation
Polysaccharides
Humans
Gene silencing
Gene Silencing
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
Molecular Biology
ComputingMilieux_MISCELLANEOUS
Fucosylation
030304 developmental biology
0303 health sciences
glycosphingolipids
Globoside
Cadherin
colon cancer
E-cadherin
030302 biochemistry & molecular biology
Glycosphingolipid
Cadherins
HCT116 Cells
digestive system diseases
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
Cell biology
Gene Expression Regulation
Neoplastic
carbohydrates (lipids)
chemistry
Cell culture
lipids (amino acids
peptides
and proteins)
Colorectal Neoplasms
HT29 Cells
Zdroj: Proteomics
Proteomics, Wiley-VCH Verlag, 2019, pp.1800452. ⟨10.1002/pmic.201800452⟩
Proteomics, 2019, pp.1800452. ⟨10.1002/pmic.201800452⟩
Proteomics, 19(21-22)
ISSN: 1615-9861
1615-9853
DOI: 10.1002/pmic.201800452
Popis: Colorectal cancer (CRC) affects both women and men living in societies with a high sedentary lifestyle. Amongstthe phenotypic changes exhibited by tumor cells, a widerange of glycosylationshas been reported for colon cancer-derived cell lines and CRC tissues. These aberrant modifications affect different aspectsof glycosylation, including an increase in core fucosylation and GlcNAc branching on N-glycans, alteration of O-glycans, upregulated sialylation and O-GlcNAcylation. Although O-GlcNAcylation and complex glycosylations differ in many aspects, sparse evidences report on the interference of O-GlcNAcylation with complex glycosylation. Nevertheless, this relationship is still a matter of debate. Combining different approaches onthree human colon cell lines (HT29, HCT116 and CCD841CoN), we herein report that silencing O-GlcNAc transferase (OGT, the sole enzyme driving O-GlcNAcylation), only slightly affectsoverall N-and O-glycosylation patterns. Interestingly, silencingof OGT in HT29 cells upregulates E-cadherin (a major actor of epithelial-to-mesenchymal transition) and changes its glycosylation.On the other hand, OGT silencing perturbs biosynthesis ofglycosphingolipids resulting ina decreaseingangliosidesandan increase in globosides.Together, these results provide novel insights regarding the selective regulation of complex glycosylations by O-GlcNAcylation in colon cancer cells. 19;21-22
Databáze: OpenAIRE
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