Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis.

Abstract

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.

• Authors: M Yoshimura, Y Ihara, Y Matsuzawa, N Taniguchi
• Journal: The Journal of biological chemistry (J Biol Chem) Vol. 271 Issue 23 Pg. 13811-5 (Jun 07 1996) ISSN: 0021-9258 [Print] United States
• PMID: 8662832 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Cadherins
• N-Acetylglucosaminyltransferases
• beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase

Topics

• Animals
• Cadherins (chemistry, metabolism)
• Cell Aggregation (physiology)
• Glycosylation
• Melanoma, Experimental (genetics, metabolism, secondary)
• Mice
• N-Acetylglucosaminyltransferases (genetics, metabolism)
• Transfection
• Tumor Cells, Cultured