Oligodendrocyte-myelin glycoprotein is present in lipid rafts and caveolin-1-enriched membranes

被引:20
作者
Boyanapalli, M
Kottis, V
Lahoud, O
Bamri-Ezzine, S
Braun, PE
Mikol, DD [1 ]
机构
[1] Univ Michigan, Dept Neurol, Ann Arbor, MI 48109 USA
[2] McGill Univ, Dept Biochem, Montreal, PQ, Canada
关键词
axolemma; CNP; MO3.13; MOG; OMgp;
D O I
10.1002/glia.20237
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The oligodendrocyte-myelin glycoprotein is a ligand of the neuronal Nogo receptor and a potent inhibitor of neurite outgrowth, but its physiological function remains to be elucidated. The oligodendrocyte-myelin glycoprotein is anchored solely in the outer leaflet of the plasma membrane via its glycosylphosphatidylinositol anchor, and through its leucine-rich repeat domain, it likely interacts with other proteins. In the present study, we compare its buoyancy and detergent solubility characteristics with those of other myelin proteins. Based on its detergent solubility profile and membrane fractionation using established ultracentrifugation procedures, we conclude that the oligodendrocyte-myelin glycoprotein is a lipid raft component that is closely associated with the axolemma. Moreover, it associates with caveolin-1 and caveolin-l-enriched membranes. We postulate that, by virtue of its concentration in lipid rafts and perhaps through interactions with caveolin-1, the oligodendrocyte-myelin glycoprotein may influence signaling pathways. (c) 2005 Wiley-Liss, Inc.
引用
收藏
页码:219 / 227
页数:9
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