Diversity of N-acetylglucosamine-6-O-sulfotransferases:: Molecular cloning of a novel enzyme with different distribution and specificities

被引:33
作者
Uchimura, K
Fasakhany, F
Kadomatsu, K
Matsukawa, T
Yamakawa, T
Kurosawa, N
Muramatsu, T
机构
[1] Nagoya Univ, Dept Biochem, Sch Med, Showa Ku, Nagoya, Aichi 4668550, Japan
[2] Nagoya Univ, Dept Internal Med 3, Sch Med, Showa Ku, Nagoya, Aichi 4668550, Japan
基金
日本学术振兴会;
关键词
carbohydrate; gene family; molecular cloning; L-selectin ligand; sulfotransferase;
D O I
10.1006/bbrc.2000.3141
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
N-Acetylglucosamine-6-O-sulfotransferase (GlcNAc6ST) transfers sulfate to the C-6 position of non-reducing N-acetylglucosamine (GlcNAc) residues. We cloned human and mouse cDNAs encoding a novel GlcNAc6ST, designated as GlcNAc6ST-4, which showed sequence identities of 26 to 41% to other GlcNAc6STs. Human organs with strong expression of the enzyme mRNA were the heart, spleen, and ovary, while in the mouse strong expression was detected in the kidney. The enzyme expressed in CHO cells preferentially acted on mannose-linked GlcNAc, while a core 2 mucin-type oligosaccharide and an N-acetyllactosamine oligomer also served as accepters, The distribution and the specificity of GlcNAc6ST are different from those of GlcNAc6STs identified previously. (C) 2000 Academic Press.
引用
收藏
页码:291 / 296
页数:6
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