Glycobiology Advance Access published online on March 10, 2006
Glycobiology, doi:10.1093/glycob/cwj100
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1 Department of Biochemistry, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan
* To whom correspondence should be addressed. Aspects of the biological significance of the bisecting N-acetylglucosamine (GlcNAc) structure on N-glycans introduced by
Received January 13, 2006
Revised February 27, 2006
Accepted March 2, 2006
Article
Masaki Shigeta 1,
Yukinao Shibukawa 1,
Hideyuki Ihara 1,
Eiji Miyoshi 1,
Naoyuki Taniguchi 1 *,
and
Jianguo Gu 2 *
1,4-N-Acetylglucosaminyltransferase III potentiates
1 integrin-mediated neuritogenesis induced by serum deprivation in Neuro2a cells
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
Naoyuki Taniguchi, E-mail: proftani{at}biochem.med.osaka-u.ac.jp
Jianguo Gu, E-mail: jgu{at}biochem.med.osaka-u.ac.jp
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Abstract
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
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-
1 integrin antibody. In fact,
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
1 integrin, play important roles in the regulation of neuritogenesis.![]()
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