Binding partners for the myelin-associated glycoprotein of N(2)A neuroblastoma cells

The myelin-associated glycoprotein (MAG) has been proposed to be important for the integrity of myelinated axons. For a better understanding of the in teractions involved in the binding of MAG to neuronal axons, we performed t his study to identify the binding partners for MAG on neuronal cells. Exper iments with glycosylation inhibitors revealed that sialylated N-glycans of glycoproteins represent the major binding sites for MAG on the neuroblastom a cell line N(2)A. From extracts of [H-3]glucosamine-labelled N2A cells sev eral glycoproteins with molecular weights between 20 and 230 kDa mere affin ity-precipitated using immobilised MAG. The interactions of these proteins with MAG were sialic acid-dependent and specific for MAG. (C) 1999 Federati on of European Biochemical Societies.