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J. Biol. Chem., Vol. 281, Issue 19, 13038-13046, May 12, 2006

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Cell-Cell Interaction-dependent Regulation of N-Acetylglucosaminyltransferase III and the Bisected N-Glycans in GE11 Epithelial Cells

INVOLVEMENT OF E-CADHERIN-MEDIATED CELL ADHESION^*

Junko Iijima¹, Yanyang Zhao¹, Tomoya Isaji, Akihiko Kameyama^¶, Shuuichi Nakaya^¶, Xiangchun Wang, Hideyuki Ihara, Xinyao Cheng, Takatoshi Nakagawa^||, Eiji Miyoshi, Akihiro Kondo^||, Hisashi Narimatsu^¶, Naoyuki Taniguchi², and Jianguo Gu³

From the Departments of Biochemistry and ^||Glycotherapeutics, Osaka University Graduate School of Medicine, Osaka 565-0871, Japan, the Division of Regulatory Glycobiology, Tohoku Pharmaceutical University, Sendai, Miyagi 981-8558, Japan, and the ^¶Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8568, Japan

Changes in oligosaccharide structures are associated with numerous physiological and pathological events. In this study, the effects of cell-cell interactions on N-linked oligosaccharides (N-glycans) were investigated in GE11 epithelial cells. N-glycans were purified from whole cell lysates by hydrazinolysis and then detected by high performance liquid chromatography and mass spectrometry. Interestingly, the population of the bisecting GlcNAc-containing N-glycans, the formation of which is catalyzed by N-acetylglucosaminyltransferase III (GnT-III), was substantially increased in cells cultured under dense conditions compared with those cultured under sparse conditions. The expression levels and activities of GnT-III but not other glycosyltransferases, such as GnT-V and 1,6-fucosyltransferase, were also consistently increased in these cells. However, this was not observed in mouse embryonic fibroblasts or MDA-MB231 cells, in which E-cadherin is deficient. In contrast, perturbation of E-cadherin-mediated adhesion by treatment with EDTA or a neutralizing anti-E-cadherin antibody abolished the up-regulation of expression of GnT-III. Furthermore, we observed the significant increase in GnT-III activity under dense growth conditions after restoration of the expression of E-cadherin in MDA-MB231 cells. Our data together indicate that a E-cadherin-dependent pathway plays a critical role in regulation of GnT-III expression. Given the importance of GnT-III and the dynamic regulation of cell-cell interaction during tissue development and homeostasis, the changes in GnT-III expression presumably contribute to intracellular signaling transduction during such processes.

Received for publication, March 1, 2006

^* This work was partly supported by the 21st Century Center of Excellence program from the Ministry of Education, Culture, Sports, Science, and Technology of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work.

² To whom correspondence may be addressed: Dept. of Biochemistry, Osaka University Graduate School of Medicine, B1, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan. E-mail: proftani{at}biochem.med.osaka-u.ac.jp. ³ To whom correspondence may be addressed: Division of Regulatory Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsusima, Aobaku, Sendai, Miyagi 981-8558, Japan. Tel.: 81-2-727-0216; Fax: 81-2-727-0078; E-mail: jgu{at}tohoku-pharm.ac.jp.

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