α1,3‐Fucosyltransferase 9 (FUT9; Fuc‐TIX) preferentially fucosylates the distal GlcNAc residue of polylactosamine chain while the other four α1,3FUT members preferentially fucosylate the inner GlcNAc residue

FEBS Letters

Ito, Masato¹  Narimatsu, Hisashi²  Tawada, Akira³  Iwasaki, Hiroko²  Kaneko, Mika²  Nishihara, Shoko² 

[1] Department of Bioengineering, Faculty of Engineering, Soka University, 1-236 Tangi-cho, Hachioji-shi, Tokyo 192-8577, Japan;Division of Cell Biology, Institute of Life Science, Soka University, 1-236, Tangi-cho, Hachioji-shi, Tokyo 192-8577, Japan;Tokyo Research Institute, Seikagaku Corporation, 3-1253 Tatsuno Higashiyamato-shi, Tokyo 207-0021, Japan

关键词: Fucosyltransferase 9;    Polylactosamine;    Lewis x;    Stage-specific embryonal antigen-1;    CD15;    2AB;    2-aminobenzamide;    CNS;    central nervous system;    FUT;    fucosyltransferase;    GlcNAc;    N-acetylglucosamine;    gu;    glucose unit;    KS;    keratan sulfate;    Lex;    Lewis x;    LN;    N-acetyllactosamine;    Galβ1-4GlcNAc;    PBL;    peripheral blood leukocyte;    SSEA-1;    stage-specific embryonal antigen-1;   

DOI  :  10.1016/S0014-5793(99)01549-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We analyzed the substrate specificity of six human α1,3-fucosyltransferases (α1,3FUTs) for the 2-aminobenzamide (2AB)-labelled polylactosamine acceptor, Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAc-2AB (3LN-2AB). FUT9 preferentially fucosylated the distal GlcNAc residue of the polylactosamine chain while the other four α1,3FUT members, FUT3, FUT4, FUT5 and FUT6, preferentially fucosylated the inner GlcNAc residue. This indicated that FUT9 exhibits more efficient activity for the synthesis of Lewis x carbohydrate epitope (Le^x; CD15; stage-specific embryonal antigen-1 (SSEA-1)). In contrast, the other four members synthesize more effectively the internal Le^x epitope. FUT7 could not transfer a fucose to an acceptor which is non-sialylated.

【 授权许可】

Unknown