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Glycobiology Advance Access originally published online on March 10, 2006
Glycobiology 2006 16(6):564-571; doi:10.1093/glycob/cwj100
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ß1,4-N-Acetylglucosaminyltransferase III potentiates ß1 integrin-mediated neuritogenesis induced by serum deprivation in Neuro2a cells

Masaki Shigeta2, Yukinao Shibukawa2, Hideyuki Ihara2, Eiji Miyoshi2, Naoyuki Taniguchi1,2 and Jianguo Gu1,2,3

2 Department of Biochemistry, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan; and 3 Division of Regulatory Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsusima, Aobaku, Sendai, Miyagi 981-8558, Japan

1 To whom correspondence should be addressed; e-mail: jgu{at}biochem.med.osaka-u.ac.jp or proftani{at}biochem.med.osaka-u.ac.jp

Received on January 13, 2006; revised on February 27, 2006; accepted on March 2, 2006

Aspects of the biological significance of the bisecting N-acetylglucosamine (GlcNAc) structure on N-glycans introduced by ß1,4-N-acetylglucosaminyltransferase III (GnT-III) in Neuro2a cell differentiation are demonstrated. The overexpression of GnT-III in the cells led to the induction of axon-like processes with numerous neurites and swellings, in which ß1 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 erythroagglutinating phytohemagglutinin (E4-PHA), which preferentially recognizes the bisecting GlcNAc. GnT-III-promoted neuritogenesis was also significantly perturbed by treatment with a functional blocking anti-ß1 integrin antibody. In fact, ß1 integrin was found to be one of the 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 ß1 integrin, play important roles in the regulation of neuritogenesis.

Key words: bisecting GlcNAc / glycosyltransferase / GnT-III / integrin / neurite formation


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