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Nerve growth factor modulates myelin‐associatedglycoprotein binding to sensory neurons
Author(s) -
Turnley Ann M.,
Bartlett Perry F.
Publication year - 1999
Publication title -
international journal of developmental neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.761
H-Index - 88
eISSN - 1873-474X
pISSN - 0736-5748
DOI - 10.1016/s0736-5748(98)00068-9
Subject(s) - myelin associated glycoprotein , nerve growth factor , remyelination , myelin , axon , microbiology and biotechnology , downregulation and upregulation , chemistry , biology , galactocerebroside , schwann cell , oligodendrocyte , neurofilament , neuroscience , central nervous system , biochemistry , immunohistochemistry , receptor , immunology , gene
Myelin‐associated glycoprotein (MAG) is a molecule expressed by myelinating cells atthe myelin:axon interface, which binds to an as yet unidentified molecule on neurons. We haveused a MAG‐immunoglobulin Fc fusion protein to examine the expression and regulation of theMAG binding molecule on sensory neurons in culture. Binding of the MAG‐Fc reached amaximum at 24‐48 h and was higher on neurons which expressed high levels of neurofilament.Nerve growth factor (NGF) upregulated expression of the MAG binding molecule in a dosedependent manner. Schwann cells co‐cultured with sensory neurons in serum‐free mediumstimulated maximal expression of the MAG binding molecule, which was decreased by addition ofanti‐NGF to the co‐cultures. This indicated that Schwann cells can modulate expression of theMAG binding molecule via production of NGF and may represent a physiological mechanism forregulation of MAG MAG binding molecule interactions during myelination and remyelination. 1999 ISDN. Published by Elsevier Science Ltd. All rights reserved