Enzymological and pharmacological aspects of monoamine oxidase

  • K. F. Tipton
  • A. M. O’Carroll
  • F. Hasan
Chapter

Abstract

Although inhibitors of monoamine oxidase [amine: oxygen oxido-reductase (deaminating) (flavin-containing) EC 1.4.3.4] (MAO) have been of value in the treatment of certain types of depression (see for example, Pare, 1976), their use has been limited by a range of possible adverse reactions in subjects treated with these compounds (see for instance, Dostert, 1984). Particular attention has been focused on the, potentially fatal, hypertensive effect that may result if patients treated with monoamine oxidase inhibitors ingest foodstuffs containing tyramine (the tyramine pressor response or ‘cheese reaction’ — see for example Marley, 1977).

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References

  1. ASK, A.-L., FLAGERVALL, I. & ROSS, S.B. (1984). Amiflavine (FLA 336(+)), a reversible MAO-A in hibitor selective for serotoninergic neurones. In Monoamine Oxidase and Disease: Prospects for Therapy with Reversible Inhibitors. Dostert, P., Strolin Benedetti, M. & Tipton, K.F. (eds), London: Academic Press (in press).Google Scholar
  2. ASK, A.-L., HELLSTRÖM, W., NORRMAN, S., ÖGREN, S.- O. & ROSS, S.B. (1982). Selective inhibition of the A form of monoamine oxidase by 4-dimethylamino-a- methylphenylalkylamine derivatives in the rat. Neuropharmacology, 21, 299–308.CrossRefGoogle Scholar
  3. BIRKMEYER, W., RIEDERER, P., AMBROZI, L. & YOUDIM, M.B.H. (1977). Implications of combined treatment with ‘Madopar’ and 1-deprenyl in Parkinson’s disease. A long term therapy. Lancet, i, 439–443.CrossRefGoogle Scholar
  4. CALLINGHAM, B.A. (1981). Resolution of amine oxidase activities by irreversible inhibitors. In Monoamine Oxidase Basic and Clinical Frontiers. Kamijo, K., Usdin, E. & Nagatsu, T.(eds) pp. 100–111, Amsterdam: Excerpta Medica.Google Scholar
  5. CARLSSON, A., FOWLER, C.J., MAGNUSSON, T., ORELAND, L. & WIBERG, A. (1981). The activities of monoamine oxidase-A and -B, succinic dehydrogenase and acid phosphatase in the rat brain after hemitransac- tion. Naunyn-Schmiedebergs Arch. Pharmac, 316, 51–55.CrossRefGoogle Scholar
  6. CARMAN, J.S., GILLIN, J.C., MURPHY, D.L., WEINBER GER, D.R., KLEINMAN, J.E., BIGELOW, L.B. & WYATT, R.J. (1978). Effects of a selective inhibitor of type A monoamine oxidase — Lilly 51641 — on behaviour, sleep and circadian rhythms in depressed and schizophrenic patients. Commun. Psychopharmac, 2, 512–523.Google Scholar
  7. DA PRADA, M., KETTLER, R., KELLER, H.H. & HAEFELY, W.E. (1983). Neurochemical effects in vitro and in vivo of the antidepressant Ro 11–1163, a specific and short acting MAO-A inhibitor. In Monoamine Oxidase and its Selective Inhibitors. Beckmann, H. & Riederer, P. (eds) pp. 231–245, Basel: Karger.Google Scholar
  8. DELLA CORTE, L. & TIPTON, K.F. (1980). The turnover of the A- and B-forms of monoamine oxidase in rat liver. Biochem. Pharmac, 29, 891–895.CrossRefGoogle Scholar
  9. DEMAREST, KT., SMITH, D.J. & AZZARO, A.J. (1980). The presence of the type A form of monoamine oxidase within nigrostriatal dopamine-containing neurones. J. Pharmac. exp. Ther., 215, 461–468.Google Scholar
  10. DOSTERT, P. (1984). Myth and reality of the classical MAO inhibitors. Reasons for seeking a new generation. In Monoamine Oxidase and Disease: Prospects for Therapy with Reversible Inhibitors. Dostert, P., Strolin Benedetti, M. & Tipton, K.F. (eds), London: Academic Press (in press).Google Scholar
  11. ELSWORTH, J.D., GLOVER, V., REYNOLDS, G.P., SAND LER, M., LEES, A.J., PHUAPRADIT, P., SHAW, K.M., STERN, G.M. & KUMAR, P. (1978). Deprenyl administration in man. A selective MAO-B inhibitor without the ‘cheese effect’. Psychopharmacology, 57, 33–38.CrossRefGoogle Scholar
  12. FOWLER, C.J. & STROLIN BENEDETTI, M. (1983). Cimoxatone is a reversible tight-binding inhibitor of the A form of rat brain monoamine oxidase. J. Neurochem., 40, 510–513.CrossRefGoogle Scholar
  13. FOWLER, C.J. & TIPTON, K.F. (1981). Concentration dependence of the oxidation of tyramine by the two forms of rat liver mitochondrial monoamine oxidase. Biochem. Pharmac, 30, 3329–3332.CrossRefGoogle Scholar
  14. FOWLER, C.J. & TIPTON, K.F. (1982). Deamination of 5- hydroxytryptamine by both forms of monoamine oxidase in the rat brain. J. Neurochem., 38, 733–736.CrossRefGoogle Scholar
  15. FOWLER, C.J., MANTLE, T.J. & TIPTON, K.F. (1982a). The nature of the inhibition of rat liver monoamine oxidase types A and B by the acetylenic inhibitors clorgyline, 1- deprenyl and pargyline. Biochem. Pharmac, 31, 3555–3561.CrossRefGoogle Scholar
  16. FOWLER, C.J., TIPTON, K.F., STROLIN BENEDETTI, M. & DOW, J. (1982b). Inhibitory properties of MD 780236 and its alcohol metabolite towards monoamine oxidase- B. Acta physiol. scand., Suppl. 508, 39.Google Scholar
  17. FOWLER, C.J., TIPTON, K.F., MacKAY, A.V.P. & YOUDIM, M.B.H. (1982c). Human platelet monoamine oxidase — a useful enzyme in the study of psychiatric disorders? Neuroscience, 7, 1577–1594.CrossRefGoogle Scholar
  18. GARRICK, N.A. & MURPHY, D.L. (1982). Monoamine oxidase type A: differences in selectivity towards 1- norepinephrine compared to serotonin. Biochem. Phar mac, 31, 4061–4066.CrossRefGoogle Scholar
  19. GLOVER, V., SANDLER, M., OWEN, F. & RILEY, GJ. (1977). Dopamine is a monoamine oxidase B substrate in man. Nature, 265, 80–81.CrossRefGoogle Scholar
  20. GORIDIS, C. & NEFF, N.H. (1971). Monoamine oxidase in sympathetic nerves: a transmitter specific enzyme type. Br. J. Pharmac, 31, 4061–4066.Google Scholar
  21. GREEN, A.L. (1981). The kinetics of inhibition of type-B monoamine oxidase by clorgyline, pargyline and deprenyl. J. Pharm. Pharmac, 33, 798–800.CrossRefGoogle Scholar
  22. HALL, D.W.R., LOGAN, B.W. & PARSONS, G.H. (1969). Further studies on the inhibition of monoamine oxidase by M & B 9302 (clorgyline). I. Substrate specificity in various mammalian species. Biochem. Pharmac, 18, 1447–1454.CrossRefGoogle Scholar
  23. HERD, J.A. (1969). A new antidepressant M & B 9302. A pilot study and double blind controlled trial. Clin. Trials, 6, 119–126.Google Scholar
  24. HOUSLAY, M.D. & TIPTON, K.F. (1974). A kinetic evalua tion of monoamine oxidase activity in rat liver mitochon drial outer membranes. Biochem. J., 139, 645–652.CrossRefGoogle Scholar
  25. JOHNSTON, J.P. (1968). Some observations upon a new inhibitor of monoamine oxidase in brain tissue. Biochem. Pharmac, 17, 1285–1297.CrossRefGoogle Scholar
  26. KINEMUCHI, H., WAKUI, W. & KAMIJO, K. (1980). Sub strate selectivity of type A and type B monoamine oxidase in rat brain. J. Neurochem., 39,109–115.CrossRefGoogle Scholar
  27. LEVITT, P., PINTAR, J.E. & BREAKEFIELD, X.O. (1982). Immunocytochemical demonstration of monoamine oxidase B in brain astrocytes and serotoninergic neurons. Proc. natn. Acad. Sci. U.S.A.., 79,6385–6389.CrossRefGoogle Scholar
  28. LEWINSON, R., GLOVER, V. & SANDLER, M. (1980). ß- Phenylethylamine and benzylamine as substrates for human monoamine oxidase A: a source of some anomolies? Biochem. Pharmac, 29, 1221–1230.CrossRefGoogle Scholar
  29. MANN, J. & GERSHON, S. (1980). L-Deprenyl, a selective monoamine oxidase type B inhibitor in endogenous depression. Life Sci., 26, 877–882.CrossRefGoogle Scholar
  30. MANTLE, T.J., TIPTON, K.F. & GARRETT, N.J. (1976). In hibition of monoamine oxidase by amphetamine and related compounds. Biochem. Pharmac, 25, 2073–2077.CrossRefGoogle Scholar
  31. MARLEY, E. (1977). Monoamine oxidase inhibitors and drug interactions. In Drug Interactions. Grahame-Smith, D.G. (ed.), pp. 171–194, London: Macmillan.Google Scholar
  32. MENDIS, N., PARE, C.M.B., SANDLER, M., GLOVER, V. & STERN, G. (1981). (-)-Deprenyl in treatment of depression. In Monoamine Oxidase Inhibitors — The State of the Art. Youdim, M.B.H. & Paykel, E.S. (eds) pp. 171–176, Chichester: Wiley.Google Scholar
  33. MENDLEWICZ, J. & YOUDIM, M.B.H. (1980). Anti depressant potentiation of 5-HTP by l-deprenyl in affective illness. J. Affect. Dis., 2,137–142.CrossRefGoogle Scholar
  34. MURPHY, D.L., LIPPER, S., CAMPBELL, I.C., MAJOR, L.F., SLATER, S. & BUCHSBAUM, M.S. (1979). Comparative studies of MAO-A and MAO-B inhibitors in man. In Monoamine Oxidase, Structure, Function and Altered Functions. Singer, T.P., Von Korff, R.W. & Murphy, D.L. (eds) pp. 457–475, New York: Academic Press.Google Scholar
  35. MURPHY, D.L., ROY, B., PICKAR, D., LIPPER, S., COHEN, R.M., JIMERSON, P., LAKE, C.R., MUSCETTOLA, G., SAAVEDRA, J. & KOPIN, I.(1981). Cardiovascular changes accompanying MAO inhibition in man. In Func tion and Regulation of Monoamine Enzymes. Usdin, E., Weiner, N. & Youdim, M.B.H. (eds) pp. 549–560, Lon don: Macmillan.Google Scholar
  36. NEFF, N.H. & GORIDIS, C. (1972). Neuronal monoamine oxidases, specific enzyme types and their rate of formation. Adv. Biochem. Psychopharmac, 5, 307–323.Google Scholar
  37. NELSON, D.L., HERBERT, A., PETILLOT, Y., PICHAT, L., GLOWINSKI, J. & HAMON M., (1979). [3H]Harmaline as a specific ligand for MAO-A. Properties of the active site of MAO-A from rat and bovine brains. J. Neurochem., 32, 1817–1827.CrossRefGoogle Scholar
  38. O’BRIEN, R.D. (1968). Kinetics of the carbamylation of cholinesterase. Mol. Pharmac, 4, 121–130.Google Scholar
  39. O’CARROLL, A.-M., FOWLER, C.J., PHILLIPS, J.P., TOB-BIA, I. & TIPTON, K.F. (1983). The deamination of dopamine by human brain monoamine oxidase. Specificity for the two enzyme forms in seven brain regions. Naunyn-Schmiedebergs Arch. Pharmac, 322, 198–202.CrossRefGoogle Scholar
  40. PALFREYMAN, M.G., McDONALD, I., ZREIKA, M. & FOZARD, J.P. (1983). MDL 72394: the prodrug approach to monoamine oxidase inhibition. L’Encephale, 9, Suppl. 1, 55A.Google Scholar
  41. PARE, C.M.B. (1976). Introduction to clinical aspects of monoamine oxidase inhibitors in the treatment of depression. Ciba Found. Symp., 39, 271–280.Google Scholar
  42. PICKAR, D., COHEN, R.M., JIMERSON, D.L. & MURPHY, D.L. (1981). Tyramine infusions and selective monoamine oxidase inhibitor treatment. Psychophar-macology, 74, 4–7.CrossRefGoogle Scholar
  43. POWELL, J.F. & CRAIG, I.W. (1977). Biochemical and immunological studies of the monoamine oxidase activities of cultured human cells. Biochem. Soc Trans., 5, 180–182.CrossRefGoogle Scholar
  44. SMITH, T.E., WEISSBACH, H. & UDENFRIEND, S. (1963). Studies on monoamine oxidase: The mechanism of inhibition of monoamine oxidase by iproniazid. Biochemistry, 2, 746–751.CrossRefGoogle Scholar
  45. STROLIN BENEDETTI, M., BOUCHER, T. & FOWLER, C.J. (1983a). The deamination of noradrenaline and 5- hydroxytryptamine by rat brain and heart monoamine oxidase and their inhibition by cimoxatone, toloxatone and MD 770222. Naunyn-Schmiedebergs Arch. Pharmac, 323, 315–320.CrossRefGoogle Scholar
  46. STROLIN BENEDETTI, M., BOUCHER, T., CARLSSON, A. & FOWLER, C.J. (1983b). Intestinal metabolism of tyramine by both forms of monoamine oxidase in the rat. Biochem. Pharmac, 32, 47–52.CrossRefGoogle Scholar
  47. STUDENT, A.K. & EDWARDS, D.J. (1977). Subcellular localisation of type A and type B monoamine oxidase in rat brain. Biochem. Pharmac, 26, 2337–2342.CrossRefGoogle Scholar
  48. SUZUKI, O., HATTORI, H., OYA, M., KATSUMATA, Y. & MATSUMOTO, T. (1979). Oxidation of ß-phenyl- ethylamine by both types of monoamine oxidase: effects of substrate concentration and pH. Life Sci., 25, 1843–1850.CrossRefGoogle Scholar
  49. TIPTON, K.F. (1980). Kinetics and enzyme inhibition studies. In Enzyme Inhibitors as Drugs. Sandler, M. (ed.) pp. 1–23, London: Macmillan.Google Scholar
  50. TIPTON, K.F., HOUSLAY, M.D. & MANTLE, T.J. (1976). The nature and locations of the multiple forms of monoamine oxidase. Ciba Found. Symp., 39, 5–16.Google Scholar
  51. TIPTON, K.F., FOWLER, C.J. & HOUSLAY, M.D. (1982a). Specificities of the two forms of monoamine oxidase. In Monoamine Oxidase: Basic and Clinical Frontiers, Kamijo, K., Usdin, E. & Nagatsu, T. (eds) pp. 87–99, Amsterdam: Excerpta Medica.Google Scholar
  52. TIPTON, K.F., McCRODDEN, J.M., KALIR, A.S. & YOUDIM, M.B.H. (1982a). Inhibition of rat liver monamine oxidase by a-methyl- and N-propargyl-amine derivatives. Biochem. Pharmac, 31, 1251–1255.CrossRefGoogle Scholar
  53. TIPTON, K.F., FOWLER, C.J., McCRODDEN, J.M. & STROLIN BENEDETTI, M. (1983). The enzyme- activated irreversible inhibition of type-B monoamine oxidase by 3-[4-[(3-chlorophenyl)methoxy] phenyl]-5- [(methylamino) methyl]-2-oxazolidinone methane sulphate (compound MD 780236) and the enzyme- catalysed oxidation of this compound as competing reactions. Biochem. J., 209, 235–242.CrossRefGoogle Scholar
  54. TIPTON, K.F., McCRODDEN, J.M., HENEHAN, G.T.M., BOUCHER, T. & FOWLER, C.J. (1984). The formation of the acidic and alcoholic metabolites of MD 780236. Biochem. Pharmac, 33, 1377–1378.CrossRefGoogle Scholar
  55. VAN DER KROGT, J.A., KOOT-GRONSVELD, E. & VAN DEN BERG, C. (1983). Localization of rat striatal monoamine oxidase activities towards dopamine, serotonin and kynuramine by gradient centrifugation and nigro-striatal lesions. Life Sci., 33, 615–623.CrossRefGoogle Scholar
  56. WALDMEIER, P.C., FELNER, A.E. & TIPTON, K.F. (1983). The monoamine oxidase inhibiting properties of CGP 11305A. Eur. J. Pharmac, 94, 73–83.CrossRefGoogle Scholar
  57. WHEATLEY, D. (1970). Comparative trial of a new monoamine oxidase inhibitor in depression. Br. J. Psychiat., 117,573–574.CrossRefGoogle Scholar
  58. WHITE, H.L. & TANSIK, R.L. (1979). Characterization of multiple substrate binding sites of MAO. In Monoamine Oxidase Structure, Function and Altered Functions. Singer, T.P., Von Korff, R.W., & Murphy, D.L. (eds) pp. 129–144, New York: Academic Press.Google Scholar
  59. WILLIAMS, J.W. & MORRISON, J.F. (1979). The kinetics of reversible tight-binding inhibition. Meth. Enzymol., 63A, 437–467.CrossRefGoogle Scholar
  60. YANG, H.-Y.T. & NEFF, N.H. (1973). ß-Phenylethylamine: a specific substrate for type B monoamine oxidase of brain. J. Pharmac. exp. Ther., 187, 365–371.Google Scholar
  61. YOUDIM, M.B.H. (1983). In vivo, noradrenaline is a sub strate for rat brain monoamine oxidase A and B. Br. J. Pharmac, 79, 477–486.CrossRefGoogle Scholar

Copyright information

© Macmillan Publishers Limited 1984

Authors and Affiliations

  • K. F. Tipton
    • 1
  • A. M. O’Carroll
    • 1
  • F. Hasan
    • 1
  1. 1.Department of BiochemistryTrinity CollegeDublin 2Ireland

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