日本質量分析学会 第66回質量分析総合討論会

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ポスター発表

第3日 5月17日(木)  ポスター会場

Fut9ノックアウトマウスを用いた脳におけるルイスxキャリアタンパク質の網羅的な解析

(産総研)
o野呂絵里花栂谷内晶富岡あづさ助川昌子藤田弥佳梶裕之成松久

Alpha 1,3-fucosyltransferase 9 (Fut9) transfers a fucose residue to non-reducing end of glycans on glycolipids and glycoproteins to form Lewis x. Fut9 is expressed specifically in the stomach, kidney, brain, and leukocytes in mouse. Furthermore, we found that knock out of the gene caused some phenotypes such as immune enhancement of gastric mucosa, abnormal emotional behavior (Kudo et al., Glycobiology., 2007), and abnormal leukocytes rolling. To elucidate the mechanism, we first identified many glycoproteins carrying Lewis x from kidney utilizing a newly developed glycoproteome technology (Glyco-RIDGE method, Noro et al., J Proteome Res., 2015).
By the same approach, we analyzed site-specific glycome for mouse brain glycoproteins. We analyzed the site-specific glycome (glycan composition) of brain glycoproteins by Glyco-RIDGE method to identify Lewis x-carrying glycoproteins in brain. Then, we selected glycoproteins possessing multiple fucoses on a single N-glycan. Similar to the kidney glycoproteins, fucoses except one, which was presumed to be a core-fucose, were disappeared in Fut9 KO mice. Therefore, the lost fucose(s) were suggested to be Lewis x-composing fucose attached by Fut9. Thus, we could identify many Lewis x-carrying glycoproteins in brain.