Binding partners for the myelin‐associated glycoprotein of N2A neuroblastoma cells

FEBS Letters

Kelm, Sørge¹  Schauer, Roland¹  Strenge, Karen¹ 

[1]Institute of Biochemistry, University of Kiel, Olshausenstrasse 40, 24098 Kiel, Germany

关键词: Myelin-associated glycoprotein;    Siglec;    Sialic acid;    Cell-cell interaction;    a2;    3SL;    a2;    3-sialyllactose;    benzyl-GalNAc;    benzyl-N-acetyl-a-D-galactosamine;    Con A;    concanavalin A haemagglutinin;    FBS;    foetal bovine serum;    Ig-like;    immunoglobulin-like;    MAG;    myelin-associated glycoprotein;    MAG−/− mice;    mice in which the MAG gene has been disrupted;    PBS;    phosphate-buffered saline;    PNA;    peanut haemagglutinin;    Sia;    sialic acid;    SMP;    Schwann cell myelin protein;    Sn;    sialoadhesin;    VCS;    sialidase from Vibrio cholerae;   

DOI  :  10.1016/S0014-5793(99)00029-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The myelin-associated glycoprotein (MAG) has been proposed to be important for the integrity of myelinated axons. For a better understanding of the interactions involved in the binding of MAG to neuronal axons, we performed this study to identify the binding partners for MAG on neuronal cells. Experiments with glycosylation inhibitors revealed that sialylated N-glycans of glycoproteins represent the major binding sites for MAG on the neuroblastoma cell line N₂A. From extracts of [³H]glucosamine-labelled N₂A cells several glycoproteins with molecular weights between 20 and 230 kDa were affinity-precipitated using immobilised MAG. The interactions of these proteins with MAG were sialic acid-dependent and specific for MAG.

【 授权许可】

Unknown