Skip to main content
Log in

Localization of monoamine oxidases A and B in primate brains relative to neuron-specific and non-neuronal enolases

  • Original Articles
  • Published:
Neurochemical Research Aims and scope Submit manuscript

Abstract

Using serotonin and phenylethylamine deamination as measures of MAO A and MAO B activity respectively, positive correlations were observed between the activities of MAO A and MAO B in different areas of rhesus monkey and human brains. When the activities of MAO A and MAO B were compared with those of neuron-specific enolase and nonneuronal enolase (isozymes which are markers for neurons and glia), a slight but non-significant correlation was observed, suggesting that a simple distribution of MAO A in neurons and MAO B in glia is unlikely. This conclusion is supported by studies using synaptosomes, but contrasts with that from investigations of MAO from peripheral tissues, where experiments indicate that MAO A is predominantly localized in neurones.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Johnston, J. P. 1968. Some observations upon a new inhibitor of monoamine oxidase in brain tissue. Biochem. Pharmac. 17:1285–1297.

    Google Scholar 

  2. Coquil, J. F., Goridis, C., Mack, G., andNeff, N. H. 1973. Monoamine oxidase in rat arteries: evidence for different forms and selective localization. Br. J. Pharmacol. 48:590–599.

    Google Scholar 

  3. Goridis, C., andNeff, N. H. 1971. Monoamine oxidase in sympathetic nerves: a transmitter specific enzyme type. Br. J. Pharmac. 43:814–818.

    Google Scholar 

  4. Jarrot, B. 1971. Occurrence and properties of monoamine oxidase in adrenergic neurones. J. Neurochem. 18:7–16.

    Google Scholar 

  5. Hall, D. W. R., Logan, G. W., andParsons, G. H. 1969. Further studies on the inhibition of MAO by M & B 9302 (clorgyline) I. Substrate specificity in various mammalian species. Biochem. Pharmac. 18:1447–1454.

    Google Scholar 

  6. Hough, L. B., andDomino, E. F. 1979. Tele-methylhistamine oxidase. J. Pharmac. Exp. Ther. 208:422–428.

    Google Scholar 

  7. Student, A. K., andEdwards, D. J. 1977. Subcellular localization of types A and monoamine oxidase in rat brain. Biochem. Pharmacol. 26:2337–2342.

    Google Scholar 

  8. Suzuki, O., Katumata, Y. andOya, 1979. 1,4 methylhistamine in a specific substrate for type B monoamine oxidase. Life Sci. 24:2227–2230.

    Google Scholar 

  9. Yang, H.-Y. T., andNeff, N. H. 1973. B-phenylethylamine: a specific substrate for type B monoamine oxidase of brain. J. Pharmac. Exp. Ther. 18:365–371.

    Google Scholar 

  10. Donnelly, C. H., Richelson, E., andMurphy, D. L. 1976. Properties of monoamine oxidase in mouse neuroblastoma NIE-115 cells. Biochem. Pharmacol. 25:1639–1643.

    Google Scholar 

  11. Saavedra, J. M., Brownstein, M. J., andPalkovits, M. 1976. Distribution of catecholo-methyltransferase, histamine n-methyltransferase and monoamine oxidase in specific areas of the rat brain. Brain Res. 118:152–156.

    Google Scholar 

  12. Goridis, C., andNeff, N. H. 1971. Monoamine oxidase in sympathetic nerves: a transmitter specific enzyme type. Br. J. Pharmac. 43:814–818.

    Google Scholar 

  13. Bock, E., andDissing, J. 1975. Demonstration of enolase activity connected to the brain specific protein 14.-3-2. Scand. J. Immunol. (Suppl. 2) 4:31–36.

    Google Scholar 

  14. Marangos, P. J., andZomzely-Neurath, C. 1976. Determination and characterization of neuron-specific protein (NSP) associated enolase activity. Biochem. Biophys. Res. Commun. 68:1309–1319.

    Google Scholar 

  15. Pickel, V. M., Reis, D. J., Marangos, P. J., andZomzely-Neurath, C. 1976. Immunocytochemical localization of nervous system protein (NSP-R) in brain. Brain Res. 105:184–188.

    Google Scholar 

  16. Schmechel, D., Marangos, P. J., Zis, A. P., Brightman, M., andGoodwin, F. K. 1977. The brain enolases as specific markers of neuronal and glial cells. Science, 199:313–315.

    Google Scholar 

  17. Marangos, P. J., Zomzely-Neurath, andGoodwin, F. K. 1977. Structural and immunological properties of neuron specific protein (NSP) from rat, cat and human brain: comparison to bovin 14-32-2, J. Neurochem. 28:1097–1107.

    Google Scholar 

  18. Marangos, P. J., Parma, A. M., andGoodwin, F. K. 1978. Functional properties of neuronal and glial isoenzymes of the glycolytic enzyme enolase in brain. J. Neurochem. 31:727–732.

    Google Scholar 

  19. Marangos, P. J., Zis, A. P., Clark, R. L., andGoodwin, F. K. 1978. Neuronal (NSE), non-neuronal (NNE), and hybrid forms of enolase in brain: structural, immunological, and functional comparison, Brain Res. 150:117–133.

    Google Scholar 

  20. Marangos, P. J., Schmechel, D., Parma, A. M., Clark, R. L., andGoodwin, F. K. 1979. Measurement of neuronal and non-neuronal enolase in rat, monkey, and human tissues. J. Neurochem. 33:319–329.

    Google Scholar 

  21. Garrick, N. A., Redmond, D. E. Jr. andMurphy, D. L. 1979. Primate-rodent monoamine oxidase differences. Pages 351–359.in Singer, T. P., Von Korff, B. W. andMurphy, D. L. (eds). Monoamine Oxidase: Structure Function and Altered Functions. Academic Press, New York.

    Google Scholar 

  22. Pahm, S. andCote, L. J. 1977. Stability of enzymes in postmortem rat brain. J. Neurochem. 26:1039–1042.

    Google Scholar 

  23. Robinson, D. S., Lovenberg, W., Keiser, H., andSjoerdsma, J. 1968. Effects of drugs on human blood platelet and plasma amine oxidase activity in vitro an in vivo. Biochem. Pharmac. 17:109–119.

    Google Scholar 

  24. Campbell, I. C., Robinson, D. S., Lovenberg, W., andMurphy, D. L. 1979. The effects of chronic regimens of clorgyline and pargyline on monoamine metabolism in the rat brain. J. Neurochem. 32:49–55.

    Google Scholar 

  25. Whittaker, V. P., Michaelson, I. A., andKirkland, R. J. A. 1964. The separation of synaptic vesicles from nerve-ending particles (synaptosomes). Biochem. J. 90:293–303.

    Google Scholar 

  26. Lowry, O. H., Rosebrough, N. J., Farr, A. L., andRandall, R. J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–275.

    Google Scholar 

  27. Murphy, D. L., Redmond, D. E., Garrick, N. andBaulu, J. 1979. Brain region differences and some characteristics of monoamine oxidase type A and B activities in the vervet monkey. Neurochem. Res. 4:53–62.

    Google Scholar 

  28. Delaunoy, J. B., Hog, F., Defeudis, F. V., andMandel, P. 1979. Estimation of glial contamination of synaptosomal-mitochondrial fractions of rat brain by radioimmunoassay of carbonic anhydrase (CA II), J. Neurochem. 33:611–612.

    Google Scholar 

  29. Oreland, L., Fowler, C. J., Carlsson, A., andMagnusson, T. 1980. Monoamine oxidase-A and-B activity in the rat brain after hemitransection. Life Sci. 26:139–146.

    Google Scholar 

  30. Murphy, D. L., Donnelly, C. H., Richelson, E., andFuller, R. W. 1978. N-substituted cyclopropylamines as inhibitors of MAO A and B forms. Biochem. Pharmacol. 27:1767–1769.

    Google Scholar 

  31. Murphy, D. L., Donnelly, C. H., andRichelson, E. 1976. Substrate and inhibitor related characteristics of monoamine oxidase in C6 rat cells. J. Neurochem. 26:1231–1235.

    Google Scholar 

  32. Arnaiz, G., andDe Robertis, E. 1962. Cholinergic and non-cholinergic nerve endings in the rat brain. J. Neurochem. 9:503–508.

    Google Scholar 

  33. Ekstedt, B., andOreland, L. 1975. Effect of lipid depletion on the different forms of monoamine oxidase. Biochem. Pharmac. 25:119–124.

    Google Scholar 

  34. Houslay, M. D., Tipton, K. F., andYoudim, M. B. H. 1976. Multiple forms of monoamine oxidase: Fact and artefact. Life Sci. 19:467–478.

    Google Scholar 

  35. Diaz Borges, J. M., andD'Iorio, A. 1973. Polyacrylamide gel electrophoresis on rat liver mitochondrial monoamine oxidases. Can. J. Biochem. 51:1089–1095.

    Google Scholar 

  36. Edwards, D. J., andChang, S.-S. 1975. Evidence for interacting catalytic sites of human platelet monoamine oxidase. Biochem. Biophys. Res. Commun. 65:1018–1025.

    Google Scholar 

  37. Kaplan, N. O., Everse, J. andAdmiraal, J. 1968. Significance of substrate inhibition of dehydrogenases. Ann. N.Y. Acad. Sci. 151:400–412.

    Google Scholar 

  38. Cawthon, R. M., andBreakfield, X. O. 1979. Differences in A and B forms of monoamine oxidase revealed by limited proteolysis and peptide mapping. Nature 281:692–694.

    Google Scholar 

  39. Callingham, B. A., andParkinson, D. 1979. Tritiated pargyline binding to rat liver mitochondrial MAO. Pages 81–86.in Singer, T. P., Von Korff, R. W., andMurphy, D. L. (eds) Monoamine Oxidase: Structure Function and Altered Functions. Academic Press. New York.

    Google Scholar 

  40. Campbell, I. C., andTodrick, A. 1973. On the pharmacology and biochemistry of the amine uptake mechanism in human blood platelets. Br. J. Pharmacol. 49:279–287.

    Google Scholar 

  41. Lingjaerde, O. 1977. Platelet uptake and storage of serotonin. Pages 139–199,in Essman, W. (ed). Serotonin in Health and Disease, Spectrum, New York.

    Google Scholar 

  42. Pletscher, A. 1968. Metabolism, transfer and storage of 5-hydroxytryptamine in blood platelets. Br. J. Pharmac. 32:1–16.

    Google Scholar 

  43. Sneddon, J. 1973. Blood platelets as a model for monoamine containing neurones. Pages 153–198,in Kerkut, G. A., andPhillis, J. W. (eds), Progress in Neurobiology Vol. 1. Pergamon, New York.

    Google Scholar 

  44. Murphy, D. L., andDonnelly, C. H. 1974. Monoamine oxidase in man: enzyme characteristics in platelets, plasma and other human tissues, Pages 71–85,in Usdin, E. (ed). Adv. in Biochem. Pharmacology, 12, Academic Press, New York.

    Google Scholar 

  45. Marangos, P. J., Campbell, I. C., Schmechel, D. E., Murphy, D. L., andGoodwin, F. K. 1980. Blood platelets contain a neuron-specific enolase subunit, J. Neurochem. 34:1254–1258.

    Google Scholar 

  46. Kennedy, C., Sakurada, O., Shenohara, M., Jehle, J., andSokoloff, L. 1978. Local cerebral glucose utilization in the normal conscious Macaque monkey. Ann. Neurol. 4:293–301.

    Google Scholar 

  47. Sokoloff, L., Reivich, M., Kennedy, C., De Rosiers, M. H., Patlak, C. S., Pettigrew, K. D., andShinohara, M. 1977. The [14C]deoxyglucose method for the measurement of local cerebral glucose utilization: theory procedure and normal values in the conscious and anaesthetized albino rat. J. Neurochem. 28:897–916.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Campbell, I.C., Marangos, P.J., Parma, A. et al. Localization of monoamine oxidases A and B in primate brains relative to neuron-specific and non-neuronal enolases. Neurochem Res 7, 657–666 (1982). https://doi.org/10.1007/BF00965519

Download citation

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00965519

Keywords

Navigation