Journal
GLYCOBIOLOGY
Volume 16, Issue 6, Pages 564-571Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwj100
Keywords
bisecting GlcNAc; glycosyltransferase; GnT-III; integrin; neurite formation
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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 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 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 erythroagglutinating phytohemagglutinin (E-4-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 the target proteins of GnT-III, as confirmed by a pull-down assay with E-4-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.
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