Abstract
Monoamine oxidase (MAO) depends on a covalently attached FAD cofactor for activity. Activity is depressed in mouse neuroblastoma cells (NIE-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.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
References
Addison, R., and McCormick, D. B. (1978). Biogenesis of flavoprotein and cytochrome components in hepatic mitochondria from riboflavin-deficient rats.Biochem. Biophys. Res. Commun. 81133–138.
Amano, T., Richelson, E., and Nirenberg, M. (1972). Neurotransmitter synthesis by neuroblastoma clones.Proc. Natl. Acad. Sci. USA 69258–263.
Bottenstein, J. E., And Sato, G. H. (1979). Growth of a rat neuroblastoma cell line in serum-free supplemented medium.Proc. Natl. Acad. Sci. USA 76514–517.
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Anal. Biochem. 72248–254.
Breakefield, X. O., Castiglione, C., Edelstein, S. (1976). Monoamine oxidase activity decreased in cells lacking hypoxanthine phosphoribosyltransferase activity.Science 1921018–1020.
Cawthon, R. M., Pintar, J. E., Haseltine, F. P., and Breakefield, X. O. (1981). Differences in the structure of A and B forms of human monoamine oxidase.J. Neurochem. 37363–372.
Chuang, H. Y. K., Patek, D. R., and Hellerman, V. (1974). Mitochondrial monoamine oxidase. Inactivation by pargyline adduct formation.J. Biol. Chem. 2492381–2384.
Costa, M. R. C., and Breakefield, X. O. (1979). Electrophoretic characterization of monoamine oxidase by3H-pargyline binding in rat hepatoma cells with A and B activity.Mol. Pharmacol. 16242–249.
Costa, M. R. C., Edelstein, S. B., Castiglione, C. M., Chao, H., and Breakefield, X. O. (1980). Properties of monoamine oxidase in control and Lesch-Nyhan fibroblasts.Biochem. Genet. 18577–589.
Donnelley, C. H., Richelson, E., and Murphy, D. L. (1976). Properties of monoamine oxidase in mouse neuroblastoma N1E-115 cells.Biochem. Pharmacol. 251639–1643.
Edelstein, S. B., and Breakefield, X. O. (1981). Dexamethasone selectively increases monoamine oxidase type A in human skin fibroblasts.Biochem. Biophys. Res. Commun. 98836–843.
Erwin, V. G., and Deitrich, R. A. (1971). The labelingin vivo of monoamine oxidase by14C-pargyline: A tool for studying the synthesis of the enzyme.Mol. Pharmacol. 7219–228.
Hamm, H. -H., and Decker, K. (1978). FAD is covalently attached to peptidyl-tRNA during cell-free synthesis of 6-hydroxy-D-nicotine oxidase.Eur. J. Biochem. 92449–454.
Hawkins, M., Jr., and Breakefield, X. O. (1978). Monoamine oxidase A and B in cultured cells.J. Neurochem. 301391–1397.
Horvitz, H. R. (1973). Polypeptide bound to the host RNA polymerase is specified by T4 control gene 33.Nature New Biol. 244137–140.
Houslay, M. D., and Marchmont, R. J. (1980). Exposure of mitochondrial outer membranes to neuroaminidinase selectively destroys monoamine oxidase A activity.J Pharm. Pharmacol. 3265–66.
Houslay, M. D., Tipton, K. F., and Youdim, M. B. H. (1976). Multiple forms of monoamine oxidase: Fact and artefact.Life Sci. 19467–478.
Kim, Y. S., and Lambooy, J. P. (1978). Loss of hepatic monoamine oxidase activity resulting from replacement of its coenzyme flavin.Proc. Soc. Exp. Biol. Med. 157466–471.
Kwatra, M. M., and Sourkes, T. L. (1980). Monoamine oxidase A and B activities in liver of riboflavindeficient rats.Biochem. Pharmacol. 292693–2694.
Martinez, P., and McCauley, R. (1977). Studies on the flavins in rat liver mitochondrial outer membranes.Biochim. Biophys. Acta. 497437–446.
McKeehan, W. L., and Ham, R. G. (1976). Stimualtion of clonal growth of normal fibroblasts with substrate coated with basic polymers.J. Cell Biol. 71727–734.
Murphy, D. L. (1978). Substrate-selective monoamine oxidases—inhibitor, tissue, species and functional differences.Biochem. Pharmacol. 271889–1893.
Olson, A. D., and Hamelin, W. B. (1969). A new method for serum iron and total iron-binding capacity by atomic absorption spectrometry.Clin. Chem. 15438–444.
Oreland, L., Kinemuchi, H., and Stigbrand, T. (1973). Pig liver monoamine oxidase: Studies on subunit structure.Arch. Biochem. Biophys. 159854–860.
Pintar, J. E., Cawthon, R. M., Costa, M. R. C., and Breakefield, X. O. (1979). A search for structural differences in MAO: Electrophoretic analysis of3H-pargyline labelled proteins. InMonoamine Oxidase: Structure, Function and Altered Functions (T. P. Singer, R. W. Von Korff, and D. L. Murphy, Eds.), Academic Press, New York, pp. 81–86.
Pollack, S., Vanderhoff, G., and Laskey, F. (1977). Iron removal from transferrin.Biochim. Biophys. Acta 497481–487.
Salach, J. I. (1979). Monoamine oxidase from beef liver mitochondria: Simplified isolation procedure, properties and determination of its cysteinyl flavin content.Arch. Biochem. Biophys. 192128–137.
Sato, M., Ohishi, N., Nishikimi, M., and Yagi, K. (1977). Proteins with covalently-bound flavin in rat liver mitochondria.Biochem. Biophys. Res. Commun. 78868–873.
Sottocasa, G. L., Kuylenstierna, B., Ernster, L., and Bergstrand, A. (1967). An electron transport system associated with the outer membrane of liver mitochondria. A biochemical and morphologic study.J. Cell Biol. 32415–438.
Weyler, W., and Salach, J. I. (1981). Iron content and spectral properties of highly purified bovine liver monoamine oxidase.Arch. Biochem. Biophys. 212147–153.
Wurtman, R. J., and Axelrod, J. (1963). A specific and sensitive assay for monoamine oxidase.Biochem. Pharmacol. 121439–1440.
Youdim, M. B. H. (1976). Rat liver mitochondrial monoamine oxidase—an iron requiring flavoprotein. InFlavins and Flavoproteins (T. P. Singer, Ed.), Elsevier, Amsterdam, pp. 593–609.
Youdim, M. B. H., and Green, A. R. (1978). Iron deficiency and neurotransmitter synthesis and function.Proc. Nutr. Soc. 37173–179.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Bonnefil, V., Castiglione, C.M., Cawthon, R.M. et al. Effect of riboflavin on monoamine oxidase activity in cultured neuroblastoma cells. Cell Mol Neurobiol 1, 351–359 (1981). https://doi.org/10.1007/BF00716270
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00716270