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

FEBS Lett. 1999 Feb 5;444(1):59-64. doi: 10.1016/s0014-5793(99)00029-0.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylgalactosamine / analogs & derivatives
  • Acetylgalactosamine / pharmacology
  • Animals
  • Benzyl Compounds / pharmacology
  • Binding Sites
  • Binding, Competitive
  • Concanavalin A / metabolism
  • Glucosamine / metabolism
  • Glycoproteins / metabolism*
  • Glycosylation / drug effects
  • Mice
  • Molecular Weight
  • Myelin-Associated Glycoprotein / metabolism*
  • N-Acetylneuraminic Acid / metabolism
  • Neuraminidase / pharmacology
  • Neuroblastoma
  • Neurons / drug effects
  • Neurons / metabolism*
  • Polysaccharides / metabolism
  • Protein Binding / drug effects
  • Staphylococcal Protein A / metabolism
  • Swainsonine / pharmacology
  • Tumor Cells, Cultured

Substances

  • Benzyl Compounds
  • Glycoproteins
  • Myelin-Associated Glycoprotein
  • Polysaccharides
  • Staphylococcal Protein A
  • Concanavalin A
  • benzyl-alpha-N-acetylgalactosamine
  • Neuraminidase
  • N-Acetylneuraminic Acid
  • Acetylgalactosamine
  • Glucosamine
  • Swainsonine