Glycobiology Advance Access originally published online on December 15, 2006
Glycobiology 2007 17(3):261-276; doi:10.1093/glycob/cwl076
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Developmental changes in the expression of glycogenes and the content of N-glycans in the mouse cerebral cortex
2 Department of Physiological Sciences, The Graduate University for Advanced Studies (SOKENDAI), Okazaki, Aichi 444-8585, Japan
3 Division of Neurobiology and Bioinformatics, National Institute for Physiological Sciences, Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi 444-8787, Japan
4 Department of Functional Glycomics, Life Science Research Center, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan
5 Department of Chemistry, Graduate School of Science, Osaka University, Osaka 560-0043, Japan
1 To whom correspondence should be addressed; Tel: +81-564-595245; Fax: +81-564-595247; e-mail: ikenaka{at}nips.ac.jp
Received on May 10, 2006; revised on November 23, 2006; accepted on December 1, 2006
Biosynthesis of N-glycans varies significantly among tissues and is strictly regulated spatially and temporally within the tissue. The strict molecular mechanisms that are responsible for control of N-glycan synthesis remain largely unknown. We developed complementary deoxyribonucleic acid (cDNA) macroarray system and analyzed gene expression levels of more than 140 glycosyltransferases and glycosidases in the cerebral cortex from developing and adult mice. We also analyzed the relative amounts of major N-glycans present in the cerebral cortex and examined how the synthesis of N-glycans might be regulated through the expression of these genes. We demonstrated that the content of N-linked oligosaccharides dramatically changed during the course of brain development. Some of these changes could not be explained by alterations in the expression of the corresponding genes. For example, the amount of core fucosylated sugar chains in the early embryonic brain and the expression level of fucosyltransferase VIII, the only gene known to be responsible for core fucosylation, did not change proportionately. This result suggests that post-transcriptional regulation of this gene plays an important role in regulating its enzymatic activity. On the other hand, the amount of ß1,3-galactose residue-containing sugar chains increased postnatally following an increase in the level of ß1,3-galactosyltransferase messenger ribonucleic acid (mRNA). Furthermore, the amount of sugar chains with an outer fucose residue, containing LewisX-BA-2, correlated well with the expression of fusocyltransferase IX mRNA. These findings add to our understanding of the molecular mechanisms responsible for the regulation of N-glycan biosynthesis in the cerebral cortex.
Key words: cDNA macroarray / two-dimensional HPLC / N-linked sugar chain / pyridylamination / glycogene
* These authors contributed equally to this work.
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