MAO - The Mother of all Amine Oxidases

1. Front Matter

   Pages I-XIX

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2. Determination of regions important for Monoamine Oxidase (MAO) A and B substrate and inhibitor selectivities

   • J. C. Shih, K. Chen, R. M. Geha

   Pages 1-8

3. Monoamine oxidase A deficiency: Biogenic amine metabolites in random urine samples

   • N. G. G. M. Abeling, A. H. van Gennip, A. G. van Cruchten, H. Overmars, H. G. Brunner

   Pages 9-15

4. Relationship between monoamine oxidase (MAO) A specific activity and proportion of human skin fibroblasts which express the enzyme in culture

   • R. M. Denney

   Pages 17-27

5. Are MAO-A deficiency states in the general population and in putative high-risk populations highly uncommon?

   • D. L. Murphy, K. Sims, G. Eisenhofer, B. D. Greenberg, T. George, F. Berlin et al.

   Pages 29-38

6. Differential trace amine alterations in individuals receiving acetylenic inhibitors of MAO-A (clorgyline) or MAO-B (selegiline and pargyline)

   • D. L. Murphy, F. Karoum, D. Pickar, R. M. Cohen, S. Lipper, A. M. Mellow et al.

   Pages 39-48

7. Experience with tranylcypromine in early Parkinson’s disease

   • S. Fahn, S. Chouinard

   Pages 49-61

8. Deprenyl monotherapy improves visuo-motor control in early parkinsonism

   • S. Hocherman, G. Levin, N. Giladi, M. B. H. Youdim

   Pages 63-69

9. Endogenous monoamine oxidase A inhibitory activity (tribulin), measured in saliva, is related to cardiovascular reactivity in normal individuals

   • A. Clow, A. Doyle, F. Hucklebridge, D. Carroll, C. Ring, J. Shrimpton et al.

   Pages 71-77

10. MAO inhibitory side effects of neuroleptics and platelet serotonin content in schizophrenic patients

    • Z. Mészáros, D. Borcsiczky, M. Máté, J. Tarcali, K. Tekes, K. Magyar

    Pages 79-85

11. Modulation of glutamate neurotoxicity in the transformed cell culture by monoamine oxidase inhibitors, clorgyline and deprenyl

    • O. Yu. Abakumova, O. V. Podobed, T. A. Tsvetkova, I. V. Yakusheva, T. A. Moskvitina, L. I. Kondakova et al.

    Pages 87-91

12. A cell culture model of cerebral ischemia as a convenient system to screen for neuroprotective drugs

    • J. Ekblom, H. Garpenstrand, O. Tottmar, J. A. Prince, L. Oreland

    Pages 93-98

13. Neuroprotection by selegiline and other MAO inhibitors

    • G. Stern

    Pages 99-107

14. The neuroprotective and neuronal rescue effects of (—)-deprenyl

    • K. Magyar, B. Szende, J. Lengyel, J. Tarczali, I. Szatmáry

    Pages 109-123

15. Oxidation of N-methyl(R)salsolinol: involvement to neurotoxicity and neuroprotection by endogenous catechol isoquinolines

    • M. Naoi, W. Maruyama, T. Kasamatsu, P. Dostert

    Pages 125-138

16. Substrate regulation of monoamine oxidases

    • R. R. Ramsay

    Pages 139-147

17. Monoamine oxidases and related amine oxidases as phase I enzymes in the metabolism of xenobiotics

    • M. Strolin Benedetti, K. F. Tipton

    Pages 149-171

18. Monoamine oxidases: from brain maps to physiology and transgenics to pathophysiology

    • J. G. Richards, J. Saura, J. M. Luque, A. M. Cesura, J. Gottowik, P. Malherbe et al.

    Pages 173-187

19. Structure-function relationships of mitochondrial monoamine oxidase A and B: chimaeric enzymes and site-directed mutagenesis studies

    • A. M. Cesura, J. Gottowik, G. Lang, P. Malherbe, M. Da Prada

    Pages 189-200

20. Deamination of methylamine and angiopathy; toxicity of formaldehyde, oxidative stress and relevance to protein glycoxidation in diabetes

    • P. H. Yu

    Pages 201-216

Monoamine oxidase (MAO) is linked to psychiatric and neurological disorders, because inhibitors of the enzyme are used clinically for treatment of affective disorders and Parkinson’s disease. One of the interesting new aspects of MAO is the occurrence in the human population of deletions of genes coding for one or the other enzyme subtype (A or B). This leads to the possibility of a genetic basis for psychiatric disorders based on MAO. Subjects with deletions of type A or B, and combined deletions, have been described. In the first group of 6 papers in this book, the occurrence and characterization of these phenotypes, as well as the structure of MAO genes, is explored. Advances in the biochemistry of MAO subtypes and their physiological function and localization in brain and periphery is included. Other sections of the book deal with the neuroprotective action of MAO inhibitors and their pharmacology, especially the pharmacology of new MAO-B inhibitors.

• MAO
• Monoamine Oxidase
• Parkinson's Disease
• affective disorder
• inhibitor
• biochemistry
• brain
• cell culture
• enzyme
• enzymes
• metabolism
• mitochondria
• Oxidation
• Parkinson
• Parkinson's disease
• pathophysiology
• pharmacology
• physiology
• protein
• receptor

"... the book is of particular value and a rich source of information for basic neuroscientists in the field. But it also can be of substantial interest to the rest of the neuroscientific community to get a glimpse of the current status of research in the field of MAO.” Acta Neurologica Belgica

• Department of Pharmacology, The Bruce Rappaport Faculty of Medicine, Technion — Israel Institute of Technology, Haifa, Israel

  J. P. M. Finberg, M. B. H. Youdim

• Clinical Neurochemistry, Department of Psychiatry, University of Würzburg, Federal Republic of Germany

  P. Riederer

• Biochemistry Department, Trinity College, Dublin, Ireland

  K. F. Tipton

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