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Myelin-Associated Glycoprotein Interacts With Neurons Via A Sialic Acid Binding Site At Arg118 And A Distinct Neurite Inhibition Site, Song Tang, Ying Jing Shen, Maria Elena Debellard, Gitali Mukhopadhyay, James L. Salzer, Paul R. Crocker, Marie T. Filbin

Publications and Research

Inhibitory components in myelin are largely responsible for the lack of regeneration in the mammalian CNS. Myelin-associated glycoprotein (MAG), a sialic acid binding protein and a component of myelin, is a potent inhibitor of neurite outgrowth from a variety of neurons both in vitro and in vivo. Here, we show that MAG’s sialic acid binding site is distinct from its neurite inhibitory activity. Alone, sialic acid–dependent binding of MAG to neurons is insufficient to effect inhibition of axonal growth. Thus, while soluble MAG-Fc (MAG extracellular domain fused to Fc), a truncated form of MAG-Fc missing Ig-domains 4 and 5, MAG(d1-3)-Fc, …