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Effect of riboflavin on monoamine oxidase activity in cultured neuroblastoma cells
V Bonnefil1, C M Castiglione, R M Cawthon
1Department of Human Genetics, Yale University School of Medicine, New Haven, Connecticut 06510.
Cellular and Molecular Neurobiology
|December 1, 1981
Abstract:
Monoamine oxidase (MAO) depends on a covalently attached FAD cofactor for activity. Activity is depressed in mouse neuroblastoma cells (N1E-115) grown in synthetic N2 medium lacking riboflavin. MAO activity in depleted cells is stimulated by added riboflavin, and this recovery is blocked by inhibitors of RNA and protein synthesis, and not by an inhibitor of protein glycosylation Recovery from riboflavin depletion appears to depend upon new RNA and protein synthesis, and not on the addition of FAD cofactor to an inactive MAO precursor.