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Cover Picture: Effect of Ganglioside GM3 Synthase Gene Knockout on the Glycoprotein N ‐Glycan Profile of Mouse Embryonic Fibroblast (ChemBioChem 1/2013)
Author(s) -
Nagahori Noriko,
Yamashita Tadashi,
Amano Maho,
Nishimura ShinIchiro
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201290078
Subject(s) - glycomics , glycan , glycoprotein , sphingolipid , ganglioside , biochemistry , glycosphingolipid , glycosyltransferase , biology , biosynthesis , ceramide , atp synthase , microbiology and biotechnology , chemistry , gene , apoptosis
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.