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Aberrant Glycosylation of E-cadherin Enhances Cell-Cell Binding to Suppress Metastasis
Open accessAbstract
Introduction of the beta1-4 N-acetylglucosaminyltransferase (GnT-III) gene was reported to suppress metastasis in highly metastatic B16-hm murine melanoma cells (Yoshimura, M., Nishikawa, A. , Ihara, Y., Taniguchi, S., and Taniguchi, N.(1995) Proc. Natl. Acad. Sci. U. S. A. 92, 8754-8758). In this study, the effect of GnT-III gene transfer on E-cadherin was studied, since E-cadherin acts as a suppressor of metastasis. E-cadherin expression at cell-cell contacts of B16-hm cells expressing high GnT-III activity was greater than controls without affecting transcription. Lectin blotting showed that E-cadherin from GnT-III transfectants was glycosylated by ectopically expressed GnT-III. The glycosylated E-cadherin exhibited the delayed turnover and the decreased release from cell surface, as compared with the native E-cadherin, resulting in the elevated expression at the cell-cell border of GnT-III transfectants. Furthermore, cell-cell aggregation was enhanced in GnT-III transfectants, indicating that the glycosylated E-cadherin is biologically functional. These results suggest that the glycosylated E-cadherin contributes to the suppression of metastasis by the introduction of GnT-III gene into melanoma cells.
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E-cadherin may be a target molecule for the glycan modulating effect of bissecting GlcNAc.
“and E-cadherin may be a target molecule for this glycan modulating effect (612 -613).”
From Biological roles of glycans (2017) · cites this paper as [613]
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References 24 · Cited by 209
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Metadata
- Authors
- Yoshimura, M., Ihara, Y., Matsuzawa, Y., & Taniguchi, N.
- Affiliations
- The University of Osaka (JP)
- Corresponding author
- Taniguchi, Naoyuki
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-06
- Volume
- 271
- Issue
- 23
- Pages
- 13811-13815
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2048065251
- Cited by
- 209
- References
- 24
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 6 · 2023: 2 · 2022: 4 · 2021: 6 · 2020: 7 · 2019: 7 · 2018: 7 · 2017: 2 · 2016: 10 · 2015: 7 · 2014: 9 · 2013: 5 · 2012: 7
- FWCI
- 3.03
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Keywords
- E-cadherin, aberrant glycosylation, N-acetylglucosaminyltransferase III, metastasis suppression, melanoma, cell-cell adhesion, cell-cell aggregation, protein turnover, gene transfer, cell-cell contact
- MeSH terms
- Animals, Cell Aggregation, Glycosylation, Melanoma, Experimental, Transfection, Tumor Cells, Cultured, Cadherins, N-Acetylglucosaminyltransferases, Mice
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