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Glycobiology Advance Access published online on March 10, 2006

Glycobiology, doi:10.1093/glycob/cwj100
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Published by Oxford University Press 2006. All rights reserved. The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org
Received January 13, 2006
Revised February 27, 2006
Accepted March 2, 2006

Article

{beta}1,4-N-Acetylglucosaminyltransferase III potentiates {beta}1 integrin-mediated neuritogenesis induced by serum deprivation in Neuro2a cells

Masaki Shigeta 1, Yukinao Shibukawa 1, Hideyuki Ihara 1, Eiji Miyoshi 1, Naoyuki Taniguchi 1 *, and Jianguo Gu 2 *

1 Department of Biochemistry, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan
2 Department of Biochemistry, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan; Division of Regulatory Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsusima, Aobaku, Sendai, Miyagi 981-8558, Japan

* To whom correspondence should be addressed.
Naoyuki Taniguchi, E-mail: proftani{at}biochem.med.osaka-u.ac.jp
Jianguo Gu, E-mail: jgu{at}biochem.med.osaka-u.ac.jp


   Abstract

Aspects of the biological significance of the bisecting N-acetylglucosamine (GlcNAc) structure on N-glycans introduced by {beta}1,4-N-acetylglucosaminyltransferase III (GnT-III) in Neuro2a cell differentiation is demonstrated. The overexpression of GnT-III in the cells led to the induction of axon-like processes with numerous neurites and swellings, in which {beta}1 integrin was localized, under conditions of serum starvation. This enhancement in neuritogenesis was suppressed by either the addition of a bisecting GlcNAc-containing N-glycan or E4-PHA, which preferentially recognizes the bisecting GlcNAc. GnT-III-promoted neuritogenesis was also significantly perturbed by treatment with a functional blocking anti-{beta}1 integrin antibody. In fact, {beta}1 integrin was found to be one of target proteins of GnT-III, as confirmed by a pull down assay with E4-PHA. These data suggest that N-glycans with a bisecting GlcNAc on target molecules, such as {beta}1 integrin, play important roles in the regulation of neuritogenesis.

Keywords: bisecting GlcNAc/glycosyltransferase/GnT-III/integrin/neurite formation.
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