OGT Controls the Expression and the Glycosylation of E‐cadherin, and Affects Glycosphingolipid Structures in Human Colon Cell Lines. Issue 21 (20th August 2019)
- Record Type:
- Journal Article
- Title:
- OGT Controls the Expression and the Glycosylation of E‐cadherin, and Affects Glycosphingolipid Structures in Human Colon Cell Lines. Issue 21 (20th August 2019)
- Main Title:
- OGT Controls the Expression and the Glycosylation of E‐cadherin, and Affects Glycosphingolipid Structures in Human Colon Cell Lines
- Authors:
- Biwi, James
Clarisse, Charlotte
Biot, Christophe
Kozak, Radoslaw Pawel
Madunic, Katarina
Mortuaire, Marlène
Wuhrer, Manfred
Spencer, Daniel Ian Richard
Schulz, Céline
Guerardel, Yann
Lefebvre, Tony
Vercoutter‐Edouart, Anne‐Sophie - Other Names:
- Hondermarck Hubert guestEditor.
- Abstract:
- Abstract: Colorectal cancer (CRC) affects both women and men living in societies with a high sedentary lifestyle. Amongst the phenotypic changes exhibited by tumor cells, a wide range of glycosylation has been reported for colon cancer‐derived cell lines and CRC tissues. These aberrant modifications affect different aspects of 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 on three human colon cell lines (HT29, HCT116 and CCD841CoN), it is herein reported that silencing O ‐GlcNAc transferase (OGT, the sole enzyme driving O ‐GlcNAcylation), only slightly affects overall N ‐ and O ‐glycosylation patterns. Interestingly, silencing of 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 of glycosphingolipids resulting in a decrease in gangliosides and an increase in globosides. Together, these results provide novel insights regarding the selective regulation of complex glycosylations by O ‐GlcNAcylation in colon cancer cells.
- Is Part Of:
- Proteomics. Volume 19:Issue 21/22(2019)
- Journal:
- Proteomics
- Issue:
- Volume 19:Issue 21/22(2019)
- Issue Display:
- Volume 19, Issue 21/22 (2019)
- Year:
- 2019
- Volume:
- 19
- Issue:
- 21/22
- Issue Sort Value:
- 2019-0019-NaN-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2019-08-20
- Subjects:
- colon cancer -- E‐cadherin -- glycomics -- glycosphingolipids -- O‐GlcNAcylation
Proteins -- Separation -- Periodicals
Bioinformatics -- Periodicals
Proteomics -- Periodicals
Genomes -- Periodicals
Molecular genetics -- Periodicals
572.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1615-9861 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/pmic.201800452 ↗
- Languages:
- English
- ISSNs:
- 1615-9853
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.178000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 12361.xml