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Oligodendrocyte‐myelin glycoprotein is present in lipid rafts and caveolin‐1‐enriched membranes
Author(s) -
Boyanapalli Madanamohan,
Kottis Vicky,
Lahoud Oscar,
BamriEzzine Saoussen,
Braun Peter E.,
Mikol Daniel D.
Publication year - 2005
Publication title -
glia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.954
H-Index - 164
eISSN - 1098-1136
pISSN - 0894-1491
DOI - 10.1002/glia.20237
Subject(s) - myelin , oligodendrocyte , axolemma , lipid raft , myelin associated glycoprotein , biology , microbiology and biotechnology , glycoprotein , caveolae , neurite , membrane protein , biochemistry , membrane , signal transduction , in vitro , central nervous system , neuroscience
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‐1‐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. © 2005 Wiley‐Liss, Inc.