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Nogo‐66 and myelin‐associated glycoprotein (MAG) inhibit the adhesion and migration of Nogo‐66 receptor expressing human glioma cells
Author(s) -
Liao Hong,
Duka Tetyana,
Teng Felicia Y. H.,
Sun Li,
Bu Wenyu,
Ahmed Sohail,
Tang Bor Luen,
Xiao ZhiCheng
Publication year - 2004
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.1471-4159.2004.02573.x
Subject(s) - glioma , myelin , receptor , glycoprotein , myelin associated glycoprotein , cancer research , extracellular , biology , phospholipase c , endogeny , chemistry , microbiology and biotechnology , neuroscience , endocrinology , central nervous system , biochemistry
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.