Identification and characterization of N‐acetylglucosamine‐6‐O‐sulfate‐specific β1,4‐galactosyltransferase in human colorectal mucosa

FEBS Letters

Nagata, Koji¹  Yamashita, Katsuko²  Seko, Akira²  Yonezawa, Suguru¹  Hara-Kuge, Sayuri² 

[1] Second Department of Pathology, Kagoshima University School of Medicine, Sakuragaoka 8-35-1, Kagoshima 890-8520, Japan;Department of Biochemistry, Sasaki Institute, Kanda-Surugadai 2-2, Chiyoda-ku, Tokyo 101-0062, Japan

关键词: Galactosyltransferase;    Colorectal mucosa;    Sulfated glycan;    Selectin;    Sialyl Lewis X;    GalT;    galactosyltransferase;    GL;    GlcNAcβ1→3Galβ1→4Glc;    GP;    GlcNAcβ1→2Manα1→3(GlcNAcβ1→2Manα1→6)Manβ1→4GlcNAcβ1→4GlcNAc;    NEM;    N-ethylmaleimide;    RCA;    Ricinus communis agglutinin;    6S-GN;    GlcNAc-6-O-sulfate;    6S-GP;    SO− 3→6GlcNAcβ1→2Manα1→3(Manα1→6)Manβ1→4GlcNAcβ1→4 (Fucα1→6)GlcNAc;    SulT;    sulfotransferase;    TAPS;    N-tris(hydroxymethyl)-methyl-3-aminopropanesulfonic acid;    UDP-hexanolamine;    uridine 5′-diphosphohexanolamine;   

DOI  :  10.1016/S0014-5793(98)01458-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

6-Sulfo-sialyl Lewis X structure is attributable to recognition between lymphocytes and high endothelial venules. However, the biosynthetic pathway still remains unclear. We found that a β-galactosyltransferase (βGalT) in human colorectal mucosa preferentially acts on GlcNAc-6-O-sulfate (6S-GN). 6S-GN:β4GalT was partially purified by UDP-hexanolamine-Sepharose and asialo-agalacto-ovomucin-Sepharose chromatographies. The optimum pH of this enzyme was found to be 6.5–7.5 and the Michaelis constants for 6S-GN and UDP-Gal were 0.43 mM and 16 μM, respectively. The enzymatic activity was dependent on divalent cations and the substrate specificity was not affected by α-lactalbumin. This is the first demonstration of the occurrence of 6S-GN:β4GalT.

【 授权许可】

Unknown