Phosphorylation of myelin-associated glycoprotein in cultured oligodendrocytes.
The myelin-associated glycoprotein (MAG) in primary cultures of oligodendrocytes is subject to phosphorylation in the absence of neurons. The positive response of this phosphorylation to vanadate suggests that one of the modified sites in MAG is phosphotyrosine. We found that phosphorylation was enhanced by brief treatment of the cells with insulin-like growth factor I and active phorbol ester, agents that stimulate oligodendrocyte differentiation. Preliminary observations suggest that phosphorylation enhances the association of MAG with the cytoskeleton.
Bambrick
L L
LL
McGill University, Department of Biochemistry, Montreal, Canada.
Braun
P E
PE
D000818:Animals; D001345:Autoradiography; D015153:Blotting, Western; D002478:Cells, Cultured; D003599:Cytoskeleton / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005455:Fluorescent Antibody Technique; D007334:Insulin-Like Growth Factor I / Q000494:pharmacology; D009185:Myelin Proteins / Q000378:metabolism*; D018992:Myelin-Associated Glycoprotein; D009836:Oligodendroglia / Q000378:metabolism*; D010703:Phorbol Esters / Q000494:pharmacology; D010766:Phosphorylation; D011247:Pregnancy; D051381:Rats; D011919:Rats, Inbred Strains; D014638:Vanadates / Q000494:pharmacology
D009185:Myelin Proteins; D018992:Myelin-Associated Glycoprotein; D010703:Phorbol Esters; D014638:Vanadates; D007334:Insulin-Like Growth Factor I