Enzymatic activity of a developmentally regulated member of the sialyltransferase family (STX): evidence for α2,8‐sialyltransferase activity toward N‐linked oligosaccharides

FEBS Letters

Tsuji, Shuichi¹  Kurosawa, Nobuyuki¹  Lee, Young-Choon¹  Kojima, Naoya¹  Yoshida, Yukiko¹ 

[1] Molecular Glycobiology, Frontier Research Program, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01, Japan

关键词: Sialyltransferase;    Glycoprotein;    N-linked oligosaccharide;    Glycosyltransfease gene;    Polysialic acid;    Neural cell adhesion molecule;    N-CAM;    neural cell adhesion molecule;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(95)00059-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have detected sialyltransferase activity of recombinant mouse STX, which was cloned from rat brain as a new member of the sialyltransferase family, but sialyltransferase activity of which had not been detected previously [Livingston and Paulson, J. Biol. Chem. (1993) 268, 11504–11507]. The activity of mouse STX was specific toward sialylated glycoproteins. N-Glycanase treatment and linkage-specific sialidase treatment of glycoproteins revealed that STX transfers sialic acids through α2,8-linkages to only N-linked oligosaccharides of glycoproteins. However, polymerase activity for polysialic acid synthesis was not detected for this sialyltransferase. Since this α2,8-sialyltransferase gene is highly restricted in fetal and newborn brain, it may be involved in the polysialylation of glycoproteins, especially of N-CAM.

【 授权许可】

Unknown