Cover Picture: Effect of Ganglioside GM3 Synthase Gene Knockout on the Glycoprotein N-Glycan Profile of Mouse Embryonic Fibroblast (ChemBioChem 1/2013)

Authors

  • Noriko Nagahori,

    1. Graduate School of Advanced Life Science, and Frontier Research Center for the Post-Genome Science and Technology, Hokkaido University, N21, W11, Sapporo 001-0021 (Japan)
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  • Tadashi Yamashita,

    1. Graduate School of Advanced Life Science, and Frontier Research Center for the Post-Genome Science and Technology, Hokkaido University, N21, W11, Sapporo 001-0021 (Japan)
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  • Maho Amano,

    1. Graduate School of Advanced Life Science, and Frontier Research Center for the Post-Genome Science and Technology, Hokkaido University, N21, W11, Sapporo 001-0021 (Japan)
    2. Medicinal Chemistry Pharmaceuticals, Co. Ltd. N21, W12, Sapporo 001-0021 (Japan)
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  • Shin-Ichiro Nishimura

    Corresponding author
    1. Graduate School of Advanced Life Science, and Frontier Research Center for the Post-Genome Science and Technology, Hokkaido University, N21, W11, Sapporo 001-0021 (Japan)
    2. Medicinal Chemistry Pharmaceuticals, Co. Ltd. N21, W12, Sapporo 001-0021 (Japan)
    • Graduate School of Advanced Life Science, and Frontier Research Center for the Post-Genome Science and Technology, Hokkaido University, N21, W11, Sapporo 001-0021 (Japan)
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Abstract

original image

The cover picture shows that gene knockout of the enzymes responsible for glycosphingolipid (GSL) synthesis significantly influences the biosynthesis of glycoprotein N-glycans. On p. 73 ff., S.-I. Nishimura et al. describe how they have established a general and comprehensive glycomics protocol of cellular GLSs and N-glycans of glycoproteins. To test the feasibility of a glycoblotting-based protocol, whole glycans released both from GLSs and glycoproteins were profiled concurrently by using the GM3 synthase-deficient mouse embryonic fibroblast GM3(−/−). GM3(−/−) cells did not synthesize GM3 or any downstream product of GM3 synthase. Instead, expression levels of o-series gangliosides involving GM1b and GD1-α were increased dramatically whereas a-/b-series gangliosides were predominantly detected in wild-type cells. It was also discovered that glycoprotein N-glycan profiles of GM3(−/−) cells are significantly different from those of WT cells, though GM3 synthase is responsible only for GSL synthesis and is not associated with glycoprotein N-glycan biosynthesis.

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