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Role for myelin‐associated glycoprotein as a functional tenascin‐R receptor
Author(s) -
Yang Huibin,
Xiao Zhicheng,
Becker Bruno,
Hillenbrand Rainer,
Rougon Geneviève,
Schachner Melitta
Publication year - 1999
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19990315)55:6<687::aid-jnr4>3.0.co;2-6
Subject(s) - neurite , myelin associated glycoprotein , chinese hamster ovary cell , microbiology and biotechnology , glycoprotein , chemistry , inhibitory postsynaptic potential , biology , receptor , in vitro , myelin , biochemistry , neuroscience , central nervous system
The expression of the immunoglobulin superfamily member myelin‐associated glycoprotein (MAG) and the extracellular matrix glycoprotein tenascin‐R (TN‐R) by oligodendrocytes overlaps in time and space. The two molecules can be neurite outgrowth‐ inhibitory or ‐promoting depending on the neuronal cell type and the environment in which they are presented. Here we show that the two molecules directly bind to each other in vitro and that binding sites on TN‐R localize to two domains, the fibrinogen domain and the epidermal growth factor‐like repeat domain with the N‐terminal cysteine‐rich stretch. We further show by a functional assay, namely the repulsion of MAG‐transfected Chinese hamster ovary cells (CHO) cells from a TN‐R substrate, that MAG is part of the signalling pathway of TN‐R for cell repulsion. When coated as a uniform substrate, MAG was inhibitory for neurite outgrowth of hippocampal and cerebellar neurons in vitro, when compared to poly‐ l ‐lysine, while TN‐R enhanced neurite outgrowth. When added to MAG, TN‐R neutralized the neurite outgrowth‐inhibitory effects of MAG, presumably by blocking the neurite outgrowth‐inhibitory domain of MAG. J. Neurosci. Res. 55:687–701, 1999. © 1999 Wiley‐Liss, Inc.