Journal
PROTEOMICS
Volume 8, Issue 16, Pages 3221-3228Publisher
WILEY
DOI: 10.1002/pmic.200800038
Keywords
cell adhesion; E-cadherin; glycosylation; GnT-III; regulation
Funding
- Core Research for Evolutional Science and Technology (CREST)
- Japan Science and Technology Agency (JST)
- Ministry of Education, Culture, Sports, Science and Technology of Japan
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Recently, our research group investigated the effects of cell-cell interactions on N-linked oligosaccharides (N-glycans). We found that N-acetylglucosaminyltransferase III (GnT-III) activity, and thus, the enzyme product-bisected N-glycans were induced in cells cultured under dense condition in an E-cadherin-dependent manner [26]. To further explore the underlying molecular mechanism, we examined the effects of a-catenin, which is a component of the E-cadherin-catenin complex that can bind to actin cytoskeleton, on the regulation of GnT-III expression in the human colon carcinoma DLD-1 cells. GnT-III activity was not substantially increased in cells cultured under dense conditions, compared with those cultured under sparse conditions. However, restoration of of.-catenin gene to DLD-1 cells resulted in a significant increase in GnT-III activity and in production of the bisected N-glycans, which were detected by E-4-PHA, suggesting that the E-cadherin-catenin complex is required for the induction. Moreover, treatment with cytochalasin D, an inhibitor of F-actin polymerization, completely blocked the upregulation of GnT-III expression in the dense culture. Taken together, these results strongly suggest that GnT-III expression is tightly regulated by cell-cell adhesion via the E-cadherin-catenin complex and actin cytoskeleton formation.
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