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Myelin‐associated glycoprotein (MAG): past, present and beyond
Author(s) -
Quarles Richard H.
Publication year - 2007
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2006.04319.x
Subject(s) - myelin associated glycoprotein , myelin , microbiology and biotechnology , biology , glycoprotein , axon , receptor , epitope , transmembrane protein , immunoglobulin superfamily , schwann cell , signal transduction , glycoconjugate , sialic acid , neurite , oligodendrocyte , antigen , biochemistry , neuroscience , immunology , central nervous system , in vitro
The myelin‐associated glycoprotein (MAG) is a type I transmembrane glycoprotein localized in periaxonal Schwann cell and oligodendroglial membranes of myelin sheaths where it functions in glia–axon interactions. It contains five immunoglobulin (Ig)‐like domains and is in the sialic acid‐binding subgroup of the Ig superfamily. It appears to function both as a ligand for an axonal receptor that is needed for the maintenance of myelinated axons and as a receptor for an axonal signal that promotes the differentiation, maintenance and survival of oligodendrocytes. Its function in the maintenance of myelinated axons may be related to its role as one of the white matter inhibitors of neurite outgrowth acting through a receptor complex involving the Nogo receptor and/or gangliosides containing 2,3‐linked sialic acid. MAG is expressed as two developmentally regulated isoforms with different cytoplasmic domains that may activate different signal transduction pathways in myelin‐forming cells. MAG contains a carbohydrate epitope shared with other glycoconjugates that is a target antigen in autoimmune peripheral neuropathy associated with IgM gammopathy and has been implicated in a dying back oligodendrogliopathy in multiple sclerosis.