Abstract
Malignant gliomas are common and aggressive brain tumours associated with significant morbidity and mortality. We showed in this report that substratum adherence and migration by human U87MG glioma cells in culture were significantly attenuated by the extracellular domains of Nogo-A (Nogo-66) and the myelin-associated glycoprotein (MAG). U87MG cells contained significant amounts of endogenous Nogo-66 receptor (NgR), and treatment of the cells with phosphatidylinositol-specific phospholipase C (PI-PLC) or NgR antibodies resulted in an increase in their ability to adhere to, or migrate through, Nogo-66- and MAG-coated substrates. Nogo-66 and MAG may therefore modulate glioma growth and migration by acting through the NgR, a phenomenon that has potential therapeutic implications.
Copyright 2004 International Society for Neurochemistry
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Antibodies / pharmacology
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Blotting, Western / methods
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Brain / metabolism
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Cell Adhesion / drug effects
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Cell Count
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Cell Line
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Cell Movement / drug effects*
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Dose-Response Relationship, Drug
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GPI-Linked Proteins
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Gene Expression Regulation / drug effects*
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Glioblastoma
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Humans
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Myelin Proteins / genetics
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Myelin Proteins / metabolism*
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Myelin Proteins / pharmacology*
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Myelin-Associated Glycoprotein / pharmacology*
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Nogo Proteins
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Nogo Receptor 1
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Phosphatidylinositol Diacylglycerol-Lyase / pharmacology
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Phosphoinositide Phospholipase C
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Precipitin Tests / methods
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / metabolism*
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Recombinant Proteins / pharmacology
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Time Factors
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Tumor Cells, Cultured
Substances
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Antibodies
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GPI-Linked Proteins
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Myelin Proteins
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Myelin-Associated Glycoprotein
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Nogo Proteins
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Nogo Receptor 1
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RTN4 protein, human
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RTN4R protein, human
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Receptors, Cell Surface
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Recombinant Proteins
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Phosphoinositide Phospholipase C
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Phosphatidylinositol Diacylglycerol-Lyase