Abstract
It would not be practical to attempt to deal with all the advances that have informed our understanding of the behavior and functions of this enzyme over the past 90 years. This account concentrates key advances that explain why the monoamine oxidases remain of pharmacological and biochemical interest and on some areas of continuing uncertainty. Some issues that remain to be understood or are in need of further clarification are highlighted.
Similar content being viewed by others
Abbreviations
- PD:
-
Parkinson’s disease
- PEA:
-
2-Phenylethylamine
- MAO:
-
Monoamine oxidase
- MAOI:
-
Monoamine oxidase inhibitor
- MPTP:
-
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
- THP:
-
Tetrahydropapaveroline
References
Achee FM, Gabay S (1981) Studies of monoamine oxidases. Effect of triton X-100 and bile salts on monoamine oxidase in brain mitochondria. Biochem Pharmacol 30:3151–3157. https://doi.org/10.1016/0006-2952(81)90512-8
Alemany R, Olmos G, García-Sevilla JA (1997) Labelling of I2B-imidazoline receptors by [3H]2-(2-benzofuranyl)-2-imidazoline (2-BFI) in rat brain and liver: characterization, regulation and relation to monoamine oxidase enzymes. Naunyn Schmiedebergs Arch Pharmacol 356:39–47. https://doi.org/10.1007/pl00005026
Anderson MC, Hasan F, McCrodden JM, Tipton KF (1993) Monoamine oxidase inhibitors and the cheese effect. Neurochem Res 18:1145–1149. https://doi.org/10.1007/bf00978365
Ansari KS, Yu PH, Kruck TP, Tatton WG (1993) Rescue of axotomized immature rat facial motoneurons by R(−)-deprenyl: stereospecificity and independence from monoamine oxidase inhibition. J Neurosci 13:4042–4053
Armstrong J, Barlow RB (1976) The ionization of phenolic amines, including apomorphine, dopamine and catecholamines and an assessment of zwitterion constants. Br J Pharmacol 57:501–516. https://doi.org/10.1111/j.1476-5381.1976.tb10377.x
Arnett CD, Fowler JS, MacGreggor RR, Schyler DJ, Wolf AP, Langström B, Haldin CJ (1987) Turnover of brain monoamine oxidase measured in vivo by positron emission tomography using l-[14C] deprenyl. J Neurochem 49:522–527. https://doi.org/10.1111/j.1471-4159.1987.tb02895.x
Arshad A, Qing H, Wang R, Lu J, Deng Y (2011) Enzymatic condensation of dopamine and acetaldehyde: a salsolinol synthase from rat brain. Biologia 66:1183–1188. https://doi.org/10.2478/s11756-011-0134-y
Asanuma M, Miyazaki I, Ogawa N (2003) Dopamine- or l-DOPA-induced neurotoxicity: the role of dopamine quinone formation and tyrosinase in a model of Parkinson’s disease. Neurotox Res 5:165–176. https://doi.org/10.1007/bf03033137
Ask AL (1984) Selective inhibition by amiflamine of monoamine oxidase type A in rat brain, liver and duodenum. Naunyn Schmiedebergs Arch Pharmacol 327(1):56–63. https://doi.org/10.1016/0006-2952(84)90205-3
Atkinson RM, Ditman KS (1965) Tranylcypromine: a review. Clin Pharmacol Ther 6:631–665. https://doi.org/10.1002/cpt196565631
Audi SH, Dawson CA, Ahlf SB, Roerig DL (2001) Oxygen dependency of monoamine oxidase activity in the intact lung. Am J Physiol Lung Cell Mol Physiol 281:L969-681. https://doi.org/10.1152/ajplung.2001.281.4.l969
Avila M, Balsa MD, Fernandez-Alvarez E, Tipton KF, Unzeta M (1993) The effect of side chain substitution at positions 2 and 3 of the heterocyclic ring of N-acetylenic analogues of tryptamine as monoamine oxidase inhibitors. Biochem Pharmacol 45:2231–2237. https://doi.org/10.1016/0006-2952(93)90194-2
Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC (1988) cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci USA 85:4934–4938
Bar-Am O, Weinreb O, Amit T, Youdim MBH (2005) Regulation of Bcl-2 family proteins, neurotrophic factors, and APP processing in the neurorescue activity of propargylamine. FASEB J 19:1899–1901. https://doi.org/10.1096/fj.05-3794fje
Bartosz G (2009) Reactive oxygen species: destroyers or messengers? Biochem Pharmacol 77:1303–1315. https://doi.org/10.1016/j.bcp.2008.11.009
Barwell CJ, Ebrahimi SA (1994) Some kinetic properties of guinea pig liver monoamine oxidase. J Neural Transm Suppl 41:41–45
Baudhuin P, Beaufay H, Rahman-Li Y, Sellinger OZ, Wattiaux R, Jacques P, De Duve C (1964) Tissue fractionation studies. 17. Intracellular distribution of monoamine oxidase, aspartate aminotransferase, alanine aminotransferase, d-amino acid oxidase and catalase in rat-liver tissue. Biochem J 92:184–205. https://doi.org/10.1042/bj0920179
Becker RE, Giambalvo C, Fox RA, Macho M (1983) Endogenous inhibitors of monoamine oxidase present in human cerebrospinal fluid. Science 221:476–478. https://doi.org/10.1126/science.6867724
Beckmann H, Moises HW (1983) MAO inhibition as antidepressive mechanism reevaluated. A controlled study with tranylcypromine isomers. Mod Probl Pharmopsychiat 19:211–214. https://doi.org/10.1159/000407517
Ben Ramadan Z, Tipton KF (2012) Suicide inhibition of monoamine oxidase from different species by milacemide. Jordan J Biol Sci 5:209–214
Ben Ramadan Z, Wrang ML, Tipton KF (2007) Species differences in the selective inhibition of monoamine oxidase (1-methyl-2-phenylethyl)hydrazine and its potentiation by cyanide. Neurochem Res 32:1783–1790. https://doi.org/10.1007/s11064-007-9309-x
Berlin I, Zimmer R, Thiede HM, Payan C, Hergueta T, Robin L, Puech AJ (1990) Comparison of monoamine oxidase inhibiting properties of two reversible and selective monoamine oxidase-A inhibitors moclobemide and toloxatone, and assessment of their effect on psychometric performance in healthy subjects. Br J Clin Pharmacol 30:805–816
Berlin I, Saïd S, Spreux-Varoquaux O, Launay JM, Olivares R, Millet V, Lecrubier Y, Puech AJ (1995) A reversible monoamine oxidase A inhibitor (moclobemide) facilitates smoking cessation and abstinence in heavy, dependent smokers. Clin Pharmacol Ther 58:444–452. https://doi.org/10.1016/0009-9236(95)90058-6
Berman SB, Hastings TG (1999) Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria. Implications for Parkinson’s disease. J Neurochem 73:1127–1137. https://doi.org/10.1046/j.1471-4159.1999.0731127.x
Bieck PR, Antonin KH (1988) Oral tyramine pressor test and the safety of monoamine oxidase inhibitor drugs: comparison of brofaromine and tranylcypromine in healthy subjects. J Clin Psychopharmacol 8:237–245
Bieck PR, Antonin KH, Balon R, Oxenkrug G (1988) Effect of brofaromine and pargyline on human plasma melatonin concentrations. Prog Neuropsychopharmacol Biol Psychiatry 12:93–101. https://doi.org/10.1016/0278-5846(88)90064-4
Binda C, Newton-Vinson P, Hubálek F, Edmondson DE, Mattevi A (2002) Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat Struct Biol 9:22–26. https://doi.org/10.1038/nsb732
Binda C, Li M, Hubalek F, Restelli N, Edmondson DE, Mattevi A (2003) Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures. Proc Natl Acad Sci USA 100:9750–9755. https://doi.org/10.1073/pnas.1633804100
Binda C, Wang J, Li M, Hubalek F, Mattevi A, Edmondson DE (2008) Structural and mechanistic studies of arylalkylhydrazine inhibition of human monoamine oxidases A and B. Biochemistry 47:5616–5625. https://doi.org/10.1021/bi8002814
Birkmayer W, Knoll J, Riederer P, Youdim MBH (1983) (−)-Deprenyl leads to prolongation of l-dopa efficacy in Parkinson’s disease. Mod Probl Pharmacopsychiatry 19:170–176. https://doi.org/10.1159/000407513
Birkmayer W, Knoll J, Riederer P, Youdim MBH, Hars V, Marton J (1985) Increased life expectancy resulting from addition of l-deprenyl to Madopar treatment in Parkinson’s disease: a longterm study. J Neural Transm 64:113–127. https://doi.org/10.1007/bf01245973
Blackwell B, Marley E, Price J, Taylor D (1967) Hypertensive interactions between monoamine oxidase inhibitors and foodstuffs. Br J Psychiatry 113:349–365. https://doi.org/10.1192/bjp.113.497.349
Blaschko H, Richter D, Schlossmann H (1937) The oxidation of adrenaline and other amines. Biochem J 31:2187–2196. https://doi.org/10.1042/bj0312187
Boulton AA (1991) Phenylethylaminergic modulation of catecholaminergic neurotransmission. Prog Neuropsychopharmacol Biol Psychiatry 115:139–156. https://doi.org/10.1016/0278-5846(91)90076-d
Braissant O, McLin VA, Cudalbu C (2013) Ammonia toxicity to the brain. J Inherit Metab Dis 36:595–612. https://doi.org/10.1007/s10545-012-9546-2
Brunner HG, Nelen M, Breakefield XO, Ropers HH, van Oost BA (1993) Abnormal behavior associated with a point mutation in the structural gene for monoamine oxidase A. Science 262:578–580. https://doi.org/10.1126/science.8211186
Buckman TD, Eiduson S, Boscia R (1983) Investigations of the mechanism of selective inhibition of type B mitochondrial monoamine oxidase by phosphatidylserine. Biochem Pharmacol 32:3639–3647. https://doi.org/10.1016/0006-2952(83)90316-7
Buys YM, Trope GE, Tatton WG (1995) (−)-Deprenyl increases the survival of rat retinal ganglion cells after optic nerve crush. Curr Eye Res 14:119–126. https://doi.org/10.3109/02713689508999923
Calabrese F, Rossetti AC, Racagni G, Gass P, Riva MA, Molteni R (2014) Brain-derived neurotrophic factor: a bridge between inflammation and neuroplasticity. Front Cell Neurosci 8:430. https://doi.org/10.3389/fncel.2014.00430
Callingham BA (1989) Biochemical aspects of the pharmacology of moclobemide. The implications of animal studies. Br J Psychiatry (Suppl. 6):53–60 (Abstract)
Callingham BA, Mazel P, Porter JC (1985) Some properties of amine oxidase activities in the rat intestine. Br J Pharmacol 86(Suppl):553P (Abstract)
Campbell IC, Murphy DL, Walker MN, Lovenberg W, Robinson DS (1980) Monoamine oxidase inhibitors (MAOI) increase rat brain aromatic amino acid decarboxylase activity. Br J Clin Pharmacol 9:431–432. https://doi.org/10.1111/j.1365-2125.1980.tb01073
Campillos M, Kuhn M, Gavin AC, Jensen LJ, Bork P (2008) Drug target identification using side-effect similarity. Science 321:263–266. https://doi.org/10.1126/science.1158140
Carpéné C, Collon P, Remaury A, Cordi A, Hudson A, Nutt D, Lafontan M (1995) Inhibition of amine oxidase activity by derivatives that recognize imidazoline I2 sites. J Pharmacol Exp Ther 272:681–688
Carradori S, Gidaro MC, Petzer A, Costa G, Guglielmi P, Chimenti P, Alcaro S, Petzer JP (2016) Inhibition of human monoamine oxidase: biological and molecular modeling studies on selected natural flavonoids. J Agric Food Chem 64:9004–9011. https://doi.org/10.1021/acs.jafc.6b03529
Carrillo MC, Kanai S, Sato Y, Ivy GO, Kitani K (1992) Sequential changes in activities of superoxide dismutase and catalase in brain regions and liver during (−)deprenyl infusion in male rats. Biochem Pharmacol 44:2185–2189. https://doi.org/10.1016/0006-2952(92)90345-j
Castagnoli K, Steyn SJ, Magnin G, Van Der Schyf CJ, Fourie I, Khalil A, Castagnoli N Jr (2002) Studies on the interactions of tobacco leaf and tobacco smoke constituents and monoamine oxidase. Neurotox Res 4:151–160. https://doi.org/10.1080/10298420290015854henX
Cawthon RM, Breakefield XO (1983) Differences in the structures of monoamine oxidases A and B in rat clonal cell lines. Biochem Pharmacol 32:441–448. https://doi.org/10.1016/0006-2952(83)90521-x
Cenit MC, Sanz Y, Codoñer-Franch P (2017) Influence of gut microbiota on neuropsychiatric disorders. World J Gastroenterol 23:5486–5498. https://doi.org/10.3748/wjg.v23.i30.5486
Chen XC, Wu GS, Lu JQ, Iqbal J, Qing H, Deng YL (2013) Existence and characterization of salsolinol synthase in neuronal cells and rat brain. Neurochem J 7:192–197. https://doi.org/10.1134/s1819712413030045
Christmas AJ, Coulson CJ, Maxwell DR, Riddell D (1972) A comparison of the pharmacological and biochemical properties of substrate-selective monoamine oxidase inhibitors. Br J Pharmacol 45:490–503. https://doi.org/10.1111/j.1476-5381.1972.tb08106.x
Clark A Jr, Clark PA (1985) Local oxygen gradients near isolated mitochondria. Biophys J 48:931–938. https://doi.org/10.1016/s0006-3495(85)83856-x
Clineschmidt BV, Horita A (1969) The monoamine oxidase catalyzed degradation of phenelzine-l-14C, an irreversible inhibitor of monoamine oxidase-I. Studies in vitro. Biochem Pharmacol 18:1011–1020. https://doi.org/10.1016/0006-2952(69)90104-x
Clow A, Glover V, Oxenkrug GF, Sandler M (1989) Stress reduces in vivo inhibition of monoamine oxidase by phenelzine in rat brain. Neurosci Lett 107:331–334. https://doi.org/10.1016/0304-3940(89)90841-0
Coelho Cerqueira E, Netz PA, Diniz C, Petry do Canto V, Follmer C (2011) Molecular insights into human monoamine oxidase (MAO) inhibition by 1,4-naphthoquinone: evidences for menadione (vitamin K3) acting as a competitive and reversible inhibitor of MAO. Bioorg Med Chem 19:1724–7416. https://doi.org/10.1016/j.bmc.2011.10.049
Copley SD (2012) Moonlighting is mainstream: paradigm adjustment required. Bioessays 34:578–588. https://doi.org/10.1002/bies.201100191
Curet O, Damoiseau G, Aubin N, Sontag N, Rovei V, Jarreau FX (1996) Befloxatone, a new reversible and selective monoamine oxidase-A inhibitor. I. Biochemical profile. J Pharmacol Exp Ther 277:253–264
Cuthbert MF, Greenberg MP, Morley SW (1969) Cough and cold remedies: a potential danger to patients on monoamine oxidase inhibitors. Br Med J 5641:404–406. https://doi.org/10.1136/bmj.1.5641.404
Da Prada M, Zurcher G, Wurthrich I, Haefely WE (1988) On tyramine, food beverages and the reversible MAO inhibitor moclobemide. J Neural Transm 26(Suppl):33–56
Da Prada M, Kettler R, Keller HH, Cesura AM, Richards JG, Saura Marti J, Muggli-Maniglio D, Wyss PC, Kyburz E, Imhof R (1990) From moclobemide to Ro 19-6327 and Ro 41-1049: the development of a new class of reversible, selective MAO-A and MAO-B inhibitors. J Neural Transm Suppl 29:279–292
Damberg M (2005) Transcription factor AP-2 and monoaminergic functions in the central nervous system. J Neural Transm 112:1281–1296. https://doi.org/10.1007/s00702-005-0325-1
Dantzer R, O’Connor JC, Freund GG, Johnson RW, Kelley KW (2008) From inflammation to sickness and depression: when the immune system subjugates the brain. Nat Rev Neurosci 9:46–56. https://doi.org/10.10378/nrn2297
Das PK, Guha SR (1980) MAO types in guinea pig liver mitochondria. Biochem Pharmacol 29:2049–2053. https://doi.org/10.1016/0006-2952(80)90490-6
De Girolamo LA, Hargreaves AJ, Billett EE (2001) Protection from MPTP-induced neurotoxicity in differentiating mouse N2a neuroblastoma cells. J Neurochem 76:650–660
de Vos WM, de Vos EA (2012) Role of the intestinal microbiome in health. Nutr Rev 70(Suppl 1):S45–S56. https://doi.org/10.1111/j.1753-4887.2012.00505.x
Della Corte L, Tipton KF (1980) The turnover of the A- and B-forms of monoamine oxidase in rat liver. Biochem Pharmacol 29:891–895. https://doi.org/10.1016/0006-2952(80)90219-1
Deshwal S, Di Sante M, Di Lisa F, Kaludercic N (2017) Emerging role of monoamine oxidase as a therapeutic target for cardiovascular disease. Curr Opin Pharmacol 33:64–69. https://doi.org/10.1016/j.coph.2017.04.003
Di Giovanni G, Svob Strac D, Sole M, Unzeta M, Tipton KF, Mück-Šeler D, Bolea I, Della Corte L, Nikolac Perkovic M, Pivac N, Smolders IJ, Stasiak A, Fogel WA, De Deurwaerdère P (2016) Monoaminergic and histaminergic strategies and treatments in brain diseases. Front Neurosci 10:541. https://doi.org/10.3389/fnins.2016.00541
Dostert PL (1984) Myth and reality of the classical MAO inhibitors, reasons for seeking a new generation. In: Tipton KF, Dostert P, Strolin Benedetti M (eds) Monoamine oxidase and disease. Academic Press, London, pp 487–497 (Book chapter)
Dostert PL, Strolin Benedetti M, Tipton KF (1989) Interactions of monoamine oxidase with substrates and inhibitors. Med Res Rev 9:45–89
Duan J, Martinez M, Sanders AR, Hou C, Saitou N, Kitano T, Mowry BJ, Crowe RR, Silverman JM, Levinson DF, Gejman PV (2004) Polymorphisms in the trace amine receptor 4 (TRAR4) gene on chromosome 6q23.2 are associated with susceptibility to schizophrenia. Am J Hum Genet 75:624–638. https://doi.org/10.1086/424887
Duboué-Dijon E, Pluhařová E, Domin D, Sen K, Fogarty AC, Chéron N, Laage D (2017) Coupled valence-bond state molecular dynamics description of an enzyme-catalyzed reaction in a non-aqueous organic solvent. J Phys Chem 121:7027–7041. https://doi.org/10.1021/acs.jpcb.7b03102
Dunn RV, Marshall KR, Munro AW, Scrutton NS (2008) The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilization of the neutral amine in the enzyme–substrate complex. FEBS J 275:3850–3858. https://doi.org/10.1111/j.1742-4658.2008.06532.x
Dyck LE, Durden DA, Boulton AA (1985) Formation of beta-phenylethylamine from the antidepressant, beta-phenylethylhydrazine. Biochem Pharmacol 34:1925–1929. https://doi.org/10.1016/0006-2952(85)90310-7
Edelstein SB, Breakefield XO (1986) Monoamine oxidases A and B are differentially regulated by glucocorticoids and ‘aging’ in human skin fibroblasts. Cell Mol Neurobiol 6:121–150. https://doi.org/10.1007/bf00711066
Edmondson DE, Bhattacharyya AK, Walker MC (1993) Spectral and kinetic studies of imine product formation in the oxidation of p-(N, N-dimethylamino)-benzylamine analogues by monoamine oxidase B. Biochemistry 32:5196–5202. https://doi.org/10.1021/bi00070a031
Edmondson DE, Mattevi A, Binda C, Li M, Hubalek F (2004) Structure and mechanism of monoamine oxidase. Curr Med Chem 11:1983–1993. https://doi.org/10.2174/0929867043364784
Egashira T, Takano R, Yamanaka Y (1986) Demonstration of endogenous inhibitors of monoamine oxidase in dog cerebrospinal fluid. Jpn J Pharmacol 42:583–586. https://doi.org/10.1254/jjp.42.583
Egashira T, Obata T, Nagai T, Kimba Y, Takano R, Yamanaka Y (1989) Endogenous monoamine oxidase inhibitor-like substances in monkey brain. Biochem Pharmacol 38:597–602. https://doi.org/10.1254/jjp.81.115
Egashira T, Takayama F, Yamanaka Y (1999) The inhibition of monoamine oxidase activity by various antidepressants: differences found in various mammalian species. Jpn J Pharmacol 81:115–121. https://doi.org/10.1254/jjp.81.115
Eglen RM, Hudson AL, Kendall DA, Nutt DJ, Morgan NG, Wilson VG, Dillon MP (1998) ‘Seeing through a glass darkly’: casting light on imidazoline ‘I’ sites. Trends Pharmacol Sci 19:381–390. https://doi.org/10.1016/S0165-6147(98)01244-9
Emerit J, Edeas M, Bricaire F (2004) Neurodegenerative diseases and oxidative stress. Biomed Pharmacother 58:39–46. https://doi.org/10.1016/j.biopha.2003.11.004
Erwin VG, Deitrich RA (1971) The labeling in vivo of monoamine oxidase by 14 C-pargyline: a tool for studying the synthesis of the enzyme. Mol Pharmacol 7:219–228
Fagervall I, Ross SB (1989) Inhibition of monoamine oxidase within monoaminergic neurons in the rat brain by (E)-beta-fluoromethylene-m-tyrosine (MDL 72394). J Neurochem 52:467–471. https://doi.org/10.1111/j.1471-4159.1989.tb09144.x
Fang J, Yu PH, Gorrod JW, Boulton AA (1995) Inhibition of monoamine oxidases by haloperidol and its metabolites: pharmacological implications for the chemotherapy of schizophrenia. Psychopharmacology 118:206–212. https://doi.org/10.1007/bf0224584
Felner AE, Waldmeier PC (1979) Cumulative effects of irreversible MAO inhibitors in vivo. Biochem Pharmacol 28:995–1002. https://doi.org/10.1016/0006-2952(79)90293-4
Fernandez-Novoa L, Pastuszko A, Wilson DF (1991) Neurocatin-induced inhibition of monoamine oxidase A in rat brain synaptosomes. Biochem Pharmacol 42:2351–2354. https://doi.org/10.1016/0006-2952(91)90240-6
Finberg JP (2014) Update on the pharmacology of selective inhibitors of MAO-A and MAO-B: focus on modulation of CNS monoamine neurotransmitter release. Pharmacol Ther 143:133–152
Fischer AG, Schulz AR, Oliner L (1968) Thyroidal biosynthesis of iodothyronines. II. General characteristics and purification of mitochondrial monoamine oxidase. Biochim Biophys Acta 159:460–471. https://doi.org/10.1016/0005-2744(68)90130-7
Fitzgerald JC, Ugun-Klusek A, Allen G, De Girolamo LA, Hargreaves I, Ufer C, Abramov AY, Billett EE (2014) Monoamine oxidase-A knockdown in human neuroblastoma cells reveals protection against mitochondrial toxins. FASEB J 28:218–229. https://doi.org/10.1096/fj.13-235481
Fitzpatrick PF (2010) Oxidation of amines by flavoproteins. Arch Biochem Biophys 493:13–25. https://doi.org/10.1016/j.abb.2009.07.019
Fowler CJ 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
Fowler CJ, Oreland L (1981) Substrate- and stereoselective inhibitor of human brain monoamine oxidase by 4-dimethylamino-alpha, 2-dimethylphenethylamine (FLA 336). J Pharm Pharmacol 33:403–406
Fowler CJ, Ross SB (1984) Selective inhibitors of monoamine oxidase A and B: biochemical, pharmacological, and clinical properties. Med Res Rev 4:323–358. https://doi.org/10.1002/med.2610040303
Fowler CJ, Mantle TJ, Tipton KF (1982) The nature of the inhibition of rat liver monoamine oxidase types A and B by the acetylenic inhibitors clorgyline, l-deprenyl and pargyline. Biochem Pharmacol 3:3555–3561
Fowler JS, Volkow ND, Logan J, Wang GJ, MacGregor RR, Schlyer D et al (1994) Slow recovery of human brain MAO B after l-deprenyl (Selegiline) withdrawal. Synapse 18:86–93
Fowler JS, Volkow ND, Wang GJ, Pappas N, Logan J, Shea C, Alexoff D, MacGregor RR, Schlyer DJ, Zezulkova I, Wolf AP (1996) Brain monoamine oxidase A inhibition in cigarette smokers. Proc Natl Acad Sci USA 93:14065–14069
Fowler JS, Logan J, Wang GJ, Volkow ND, Telang F, Zhu W, Franceschi D et al (2003) Low monoamine oxidase B in peripheral organs in smokers. Proc Natl Acad Sci USA 100:11600–11605
Fowler JS, Logan J, Volkow ND, Shumay E, McCall-Perez F et al (2015) Evidence that formulations of the selective MAO-B inhibitor, selegiline, which bypass first-pass metabolism, also inhibit MAO-A in the human brain. Neuropsychopharmacol 40:650–657. https://doi.org/10.1038/npp.2014.214
Freinbichler W, Colivicchi MA, Stefanini C, Bianchi L, Ballini C, Misini B, Weinberger P, Linert W, Varešlija D, Tipton KF, Corte Della (2011) Highly reactive oxygen species: detection, formation, and possible functions. Cell Mol Life Sci 68:2067–2079. https://doi.org/10.1007/s00018-011-0682-x
Fuller RW, Hemrick SK (1978) Steric influence on inhibition of monoamine oxidase forms by 2,3-dichloro-alpha-methylbenzylamine. Res Commun Chem Pathol Pharmacol 20:199–202
Galter D, Buervenich S, Carmine A, Anvret M, Olson L (2003) ALDH1 mRNA: presence in human dopamine neurons and decreases in substantia nigra in Parkinson’s disease and in the ventral tegmental area in schizophrenia. Neurobiol Dis 14:637–647. https://doi.org/10.1016/j.nbd.2003.09.001
Gandal MJ, Haney JR, Parikshak NN, Leppa V, Ramaswami G, Hartl C, Schork AJ, Appadurai V, Buil A, Werge TM, Liu C, White KP; CommonMind Consortium; PsychENCODE Consortium; iPSYCH-BROAD Working Group, Horvath S, Geschwind DH (2018) Shared molecular neuropathology across major psychiatric disorders parallels polygenic overlap. Science 359:693–697. https://doi.org/10.1126/science.aad6469
Gareri P, Falconi U, De Fazio P, De Sarro G (2000) Conventional and new antidepressant drugs in the elderly. Progr Neurobiol 61:353–396
Garrick NA, Murphy DL (1980) Species differences in the deamination of dopamine and other substrates for monoamine oxidase in brain. Psychopharmacology 72:27–33. https://doi.org/10.1007/bf00433804
Garrick NA, Murphy DL (1982) Monoamine oxidase type A: differences in selectivity towards l-norepinephrine compared to serotonin. Biochem Pharmacol 31:4061–4066. https://doi.org/10.1016/0006-2952(82)90656-6
Gärtner B, Hemmerich P, Zeller EA (1976) Structure of flavin adducts with acetylenic substrates. Chemistry of monoamine oxidase and lactate oxidase inhibition. Eur J Biochem 63:211–221
Gerlach M, Youdim MB, Riederer P (1996) Pharmacology of selegiline. Neurology 47(9 Suppl 3):S137–S145
Gessa GL, Cuenca E, Costa E (1963) On the mechanism of the hypotensive effects of MAO inhibitors. Ann NY Acad Sci 107:935–941
Godar SC, Fite PJ, McFarlin KM, Bortolato M (2016) The role of monoamine oxidase A in aggression: current translational developments and future challenges. Prog Neuropsychopharmacol Biol Psychiatry 69:90–100. https://doi.org/10.1016/j.pnpbp.2016.01.001
Grancara S, Ohkubo S, Artico M, Ciccariello M, Manente S, Bragadin M, Toninello A, Agostinelli E (2016) Milestones and recent discoveries on cell death mediated by mitochondria and their interactions with biologically active amines. Amino Acids 48:2313–2326. https://doi.org/10.1007/s00726-016-2323-z
Green AR, Mitchell D, Todoff A, Youdim MBH (1977) Evidence for dopamine deamination by both type A and type B monoamine oxidase in rat brain in vivo and for the degree of inhibition necessary for increased functional activity of dopamine and 5-hydroxytryptamine. Br J Pharmacol 60:343–349
Grimsby J, Toth M, Chen K, Kumazawa T, Klaidman L, Adams JD, Karoum F, Gal J, Shih JC (1997) Increased stress response and beta-phenylethylamine in MAOB-deficient mice. Nat Genet 17:206–210. https://doi.org/10.1038/ng1097-206
Guimarães JT, Vindis C, Soares-da-Silva P, Parini A (2003) Differential substrate specificity of monoamine oxidase in the rat heart and renal cortex. Life Sci 73:955–967
Guzior N, Wieckowska A, Panek D, Malawska B (2015) Recent development of multifunctional agents as potential drug candidates for the treatment of Alzheimer’s disease. Curr Med Chem 22:373–404. https://doi.org/10.2174/0929867321666141106122628
Hall DW, Logan BW, Parsons GH (1969) Further studies on the inhibition of monoamine oxidase by M and B 9302 (clorgyline). I. Substrate specificity in various mammalian species. Biochem Pharmacol 18:1447–1454. https://doi.org/10.1016/0006-2952(69)90258-5
Hara MR, Thomas B, Cascio MB, Bae BI, Hester LD, Dawson VL, Dawson TM, Sawa A, Snyder SH (2006) Neuroprotection by pharmacologic blockade of the GAPDH death cascade. Proc Natl Acad Sci USA 103(10):3887–3889. https://doi.org/10.1073/pnas.0511321103
Hare ML (1928) Tyramine oxidase: a new enzyme system in liver. Biochem J 22:968–979. https://doi.org/10.1042/bj0220968
Harman D (2006) Free radical theory of aging: an update: increasing the functional life span. Ann N Y Acad Sci 1067:10–21. https://doi.org/10.1196/annals.1354.003
Hasan F, McCrodden JM, Kennedy NP, Tipton KF (1988) The involvement of intestinal monoamine oxidase in the transport and metabolism of tyramine. J Neural Transm Suppl 26:1–9
Holt A, Berry MD, Boulton AA (1994) On the binding of monoamine oxidase inhibitors to some sites distinct from the MAO active site, and effects thereby elicited. Neurotoxicology 25:251–266. https://doi.org/10.1016/s0161-813x(03)00104-9
Horwitz D, Sjoerdsma A (1963) A basis for the use of monoamine oxidase inhibitors in angina pectoris. Ann NY Acad Sci 107:1033–1042
Houslay MD, Tipton KF (1973) The reaction pathway of membrane-bound rat liver mitochondrial monoamine oxidase. Biochem J 135:735–750. https://doi.org/10.1042/bj1350735
Houslay MD, Tipton KF (1974) A kinetic evaluation of monoamine oxidase activity in rat liver mitochondrial outer membranes. Biochem J 139:645–652. https://doi.org/10.1042/bj1390645
Houslay MD, Tipton KF (1975) Rat liver mitochondrial monoamine oxidase. A change in the reaction mechanism on solubilization. Biochem J 145:311–321. https://doi.org/10.1042/bj1450311
Houtsmuller EJ, Thornton JA, Stitzer M (2002) Effects of selegiline (l-deprenyl) during smoking and short-term abstinence. Psychopharmacology 163:213–220
Hsu YP, Weyler W, Chen S, Sims KB, Rinehart WB, Utterback MC, Powell JF, Breakefield XO (1988) Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences. J Neurochem 51:1321–1324. https://doi.org/10.1042/bj2590407
Huebner CF, Donoghue EM, Plummer AJ, Furness PA (1966) N-methyl-n-2-propynyl-l-indanamine. A potent monoamine oxidase inhibitor. J Med Chem 9:830–832
Hunter KR, Boakes AJ, Laurence DR, Stern GM (1970) Monoamine oxidase inhibitors and l-Dopa. Br Med J 3:388. https://doi.org/10.1136/bmj.3.5719.388
Husain M, Edmondson DE, Singer TP (1982) Kinetic studies on the catalytic mechanism of liver monoamine oxidase. Biochemistry 21:595–600. https://doi.org/10.1021/bi00532a028
Huszti Z (1972) Kinetic studies on rat brain monoamine oxidase. Mol Pharmacol 8:385–897
Inoue H, Castagnoli K, Van Der Schyf C, Mabic S, Igarashi K, Castagnoli N Jr (1999) Species-dependent differences in monoamine oxidase A and B-catalyzed oxidation of various C4 substituted 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridinyl derivatives. J Pharmacol Exp Ther 291:856–864
Islam MT (2017) Oxidative stress and mitochondrial dysfunction-linked neurodegenerative disorders. Neurol Res 39:73–82. https://doi.org/10.1080/01616412.2016.1251711
Janssens de Varebeke P, Cavalier R, David-Remacle M, Youdim MBH (1988) Formation of the neurotransmitter glycine from the anticonvulsant milacemide is mediated by brain monoamine oxidase B. J Neurochem 50:1011–1016. https://doi.org/10.1111/j.1471-4159.1988.tb10566.x
Johnston JP (1968) Some observations upon a new inhibitor of monoamine oxidase in brain tissue. Biochem Pharmacol 17:1285–1297. https://doi.org/10.1016/0006-2952(68)90066-x
Jones TZ, Balsa D, Unzeta M, Ramsay RR (2007a) Variations in activity and inhibition with pH: the protonated amine is the substrate for monoamine oxidase, but uncharged inhibitors bind better. J Neural Transm 114:707–712. https://doi.org/10.1007/s00702-007-0675-y
Jones TZ, Giurato L, Guccione S, Ramsay RR (2007b) Interactions of imidazoline ligands with the active site of purified monoamine oxidase A. FEBS J 274:1567–1575. https://doi.org/10.1111/j.1742-4658.2007.05704.x
Kalaria RN, Harik SI (1987) Blood-brain barrier monoamine oxidase: enzyme characterization in cerebral microvessels and other tissues from six mammalian species, including human. J Neurochem 49:856–864. https://doi.org/10.1111/j.1471-4159.1987.tb00973.x
Kelsoe JR, Ginns EI, Egeland JA, Gerhard DS, Goldstein AM, Bale SJ, Pauls DL, Long RT, Kidd KK, Conte G et al (1989) Re-evaluation of the linkage relationship between chromosome 11p loci and the gene for bipolar affective disorder in the Old Order Amish. Nature 342:238–243. https://doi.org/10.1038/342238a0
Khan FH, Saha M, Chakrabarti S (2001) Dopamine induced protein damage in mitochondrial-synaptosomal fraction of rat brain. Brain Res 895:245–249. https://doi.org/10.1016/s0006-8993(00)03284-4
Kim D, Lee J, Lee S, Park J, Lee D (2016) Predicting unintended effects of drugs based on off-target tissue effects. Biochem Biophys Res Commun 469:399–404. https://doi.org/10.1016/j.bbrc.2015.11.095
Kinemuchi H, Arai Y, Oreland L, Tipton KF, Fowler CJ (1982) Time-dependent inhibition of monoamine oxidase by beta-phenethylamine. Biochem Pharmacol 31:959–964. https://doi.org/10.1016/0006-2952(82)90327-6
Kinemuchi H, Fowler CJ, Tipton KF (1987) The neurotoxicity of 1-methyl-4-phenyl-1,2,3,6,-tetrahydropyridine (MPTP) and its relevance to Parkinson’s disease. Neurochem Int 11:359–373
Kline NS (1958) Clinical experience with iproniazid (Marsilid). J Clin Exp Psychopathol 19(Suppl. 1):72–78 (discussion 78–79)
Knoll J (1988) The striatal dopamine dependency of life span in male rats. Longevity study with (−)deprenyl. Mech Ageing Dev 46:237–262. https://doi.org/10.1016/0047-6374(88)90128-5
Knoll J (1992) (−)Deprenyl-medication: a strategy to modulate the age-related decline of the striatal dopaminergic system. J Am Geriatr Soc 40:839–847. https://doi.org/10.1111/j.1532-5415.1992.tb01860.x
Knoll J, Magyar K (1972) Some puzzling pharmacological effects of monoamine oxidase inhibitors. Adv Biochem Psychopharmacol 5:393–408
Knoll J, Miklya I (1994) Multiple, small dose administration of (−)deprenyl enhances catecholaminergic activity and diminishes serotoninergic activity in the brain and these effects are unrelated to MAO-B inhibition. Arch Int Pharmacodyn Ther 328:1–15
Knoll J, Ecsery Z, Magyar K, Sátory E (1978) Novel (−)deprenyl-derived selective inhibitors of B-type monoamine oxidase. The relation of structure to their action. Biochem Pharmacol 27:1739–1747
Kopin IJ (1968) False adrenergic transmitters. Annu Rev Pharmacol 8:377–394. https://doi.org/10.1146/annurev.pa.08.040168.00211
Kotera M, McDonald AG, Boyce S, Tipton KF (2008) Functional group and substructure searching as a tool in metabolomics. PLoS One 3:e1537. https://doi.org/10.1371/journal.pone.0001537
Kragten E, Lalande I, Zimmermann K, Roggo S, Schindler P, Muller D, van Oostrum J, Waldmeier P, Furst P (1998) Glyceraldehyde-3-phosphate dehydrogenase, the putative target of the antiapoptotic compounds CGP 3466 and R-(−)-deprenyl. J Biol Chem 273:5821–5828
Krueger MJ, Mazouz F, Ramsay RR, Milcent R, Singer TP (1995) Dramatic species differences in the susceptibility of monoamine oxidase B to a group of powerful inhibitors. Biochem Biophys Res Commun 206:556–562. https://doi.org/10.1006/bbrc.1995.1079
Langston JW, Ballard P, Tetrad JW, Irwin I (1983) Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 219:979–980. https://doi.org/10.1126/science.6823561
Lenders JW, Eisenhofer G, Abeling NG, Berger W, Murphy DL et al (1996) Specific genetic deficiencies of the A and B isoenzymes of monoamine oxidase are characterized by distinct neurochemical and clinical phenotypes. J Clin Investig 97:1010–1019. https://doi.org/10.1172/jci118492
Long RF, Mantle TJ, Wilson K (1976) Substrate-selective inhibition of monoamine oxidase by some cyclopropylamino substituted oxadiazoles. Biochem Pharmacol 25:247–252
Macedo D, Filho AJMC, Soares de Sousa CN, Quevedo J, Barichello T, Júnior HVN, Freitas de Lucena D (2017) Antidepressants, antimicrobials or both? Gut microbiota symbiosis in depression and possible implications of the antimicrobial effects of antidepressant drugs for antidepressant effectiveness. J Affect Disord 208:22–32. https://doi.org/10.1016/j.jad.2016.09.012
Magyar K (2011) The pharmacology of selegiline. Int Rev Neurobiol 100:65–84. https://doi.org/10.1016/b978-0-12-386467-3.00004-2
Malcomson T, Yelekci K, Borrello MT, Ganesan A, Semina E, De Kimpe N, Mangelinckx S, Ramsay RR (2015) cis-Cyclopropylamines as mechanism-based inhibitors of monoamine oxidases. FEBS J 282:3190–3198. https://doi.org/10.1111/febs.13260
Mann PJ, Quastel JH (1940) Benzedrine (beta-phenylisopropylamine) and brain metabolism. Biochem J 34:414–431
Mantle TJ, Garrett NJ, Tipton KF (1976a) The development of monoamine oxidase in rat liver and brain. FEBS Lett 64:227–230. https://doi.org/10.1016/0014-5793(76)80289-x
Mantle TJ, Tipton KF, Garrett NJ (1976b) Inhibition of monoamine oxidase by amphetamine and related compounds. Biochem Pharmacol 25:2073–2077. https://doi.org/10.1016/0006-2952(76)90432-9
Marchitti SA, Deitrich RA, Vasiliou V (2007) Neurotoxicity and metabolism of the catecholamine-derived 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylglycolaldehyde: the role of aldehyde dehydrogenase. Pharmacol Rev 59:125–150. https://doi.org/10.1124/pr.59.2.1
Marconi S, Zwingers T (2014) Comparative efficacy of selegiline versus rasagiline in the treatment of early Parkinson’s disease. Eur Rev Med Pharmacol Sci 18:1879–1882
Maruyama W, Boulton AA, Davis BA, Dostert P, Naoi M (2001) Enantio-specific induction of apoptosis by an endogenous neurotoxin N-methyl(R)salsolinol, in dopaminergic SH-SY5Y cells: suppression of apoptosis by N-(2-heptyl)-N-methylpropargylamine. J Neural Transm 108:11–24
Maruyama W, Akao Y, Carrillo MC, Kitani K, Youdim MB, Naoi M (2002) Neuroprotection by propargylamines in Parkinson's disease: suppression of apoptosis and induction of prosurvival genes. Neurotoxicol Teratol 24:675–682. https://doi.org/10.1016/s0892-0362(02)00221-0
Marzo A, Dal Bo L, Monti NC, Crivelli F, Ismaili S, Caccia C, Cattaneo C, Fariello RG (2004) Pharmacokinetics and pharmacodynamics of safinamide, a neuroprotectant with antiparkinsonian and anticonvulsant activity. Pharmacol Res 50:77–85
Mathew B, Suresh J, Mathew GE, Parasuraman R, Abdulla N (2014) Plant secondary metabolites-potent inhibitors of monoamine oxidase isoforms. Cent Nerv Syst Agents Med Chem 14:28–33. https://doi.org/10.2174/1871524914666140826111930
Matveychuk D, Nunes E, Ullah N, Aldawsari FS, Velázquez-Martínez CA, Baker GB (2014) Elevation of rat brain tyrosine levels by phenelzine is mediated by its active metabolite β-phenylethylidenehydrazine. Prog Neuropsychopharmacol Biol Psychiatry 53:67–73
McDonald AG, Tipton KF (2012) Enzymes: irreversible inhibition. In: Encyclopedia of the life sciences. Wiley, Chichester. https://doi.org/10.1002/9780470015902.a0000601.pub2
McEwen CM Jr, Sasaki G, Lenz WR Jr (1968) Human liver mitochondrial monoamine oxidase. I. Kinetic studies of model interactions. J Biol Chem 243:5217–5225
McManus RM, Mills KH, Lynch MA (2015) T cells-protective or pathogenic in Alzheimer’s disease? J Neuroimmune Pharmacol 10:547–560. https://doi.org/10.1007/s11481-015-9612-2
Meda F, Rampon C, Dupont E, Gauron C, Mourton A, Queguiner I, Thauvin M, Volovitch M, Joliot A, Vriz S (2017) Nerves, H2O2 and Shh: three players in the game of regeneration. Semin Cell Dev Biol S1084–9521(17):30448–30502
Medvedev AE, Glover V (2004) Tribulin and endogenous MAO-inhibitory regulation in vivo. Neurotoxicology 25:185–192
Medvedev A, Igosheva N, Crumeyrolle-Arias M, Glover V (2005) Isatin: role in stress and anxiety. Stress 8:175–183
Melzig MF, Putscher I, Henklein P, Haber H (2000) In vitro pharmacological activity of the tetrahydroisoquinoline salsolinol present in products from Theobroma cacao L. like cocoa and chocolate. J Ethnopharmacol 73:153–159. https://doi.org/10.1016/s0378-8741(00)00291-9
Mihalik J, Kravcuková P, Spakovská T, Mareková M, Schmidtová K (2008) Study of high deprenyl dose on the preimplantation embryo development and lymphocyte DNA in rat. Gen Physiol Biophys 27:121–126
Miller JR, Edmondson DE (1999) Influence of flavin analogue structure on the catalytic activities and flavinylation reactions of recombinant human liver monoamine oxidases A and B. J Biol Chem 274:23515–23525
Minkowsky O (1883) Uber Spaltungen im Thierkorper. Naunyn Schmiedebergs Arch Pharmacol 17:445–465. https://doi.org/10.1007/bf02055591
Moran GR, Hoag MR (2017) The enzyme: renalase. Arch Biochem Biophys 632:66–76. https://doi.org/10.1016/j.abb.2017.05.015
Mousseau DD, Baker GB (2012) Recent developments in the regulation of monoamine oxidase form and function: is the current model restricting our understanding of the breadth of contribution of monoamine oxidase to brain [dys]function? Curr Top Med Chem 12:2163–2176. https://doi.org/10.2174/1568026611212200005
Murphy DL (1978) Substrate-selective monoamine oxidases-inhibitor, tissue, species and functional differences. Biochem Pharmacol 27:1889–1893. https://doi.org/10.1016/0006-2952(82)90656-6
Murphy S, Pastuszko A (1994) Effect of neurocatin on the activity of monoamine oxidase B in rat brain synaptosomes. Neurochem Res 19:177–182
Murphy DL, Donnelly CH, Richelson E, Fuller RW (1978) N-substituted cyclopropylamines as inhibitors of MAO-A and -B forms. Biochem Pharmacol 27:1767–17699
Myers RD (1996) Tetrahydroisoquinolines and alcoholism: where are we today? Alcohol Clin Exp Res 20:498–500. https://doi.org/10.1111/j.1530-0277.1996.tb01081.x
Mytilineou C, Leonardi EK, Radcliffe P, Heinonen EH, Han SK, Werner P, Cohen G, Olanow CW (1998) Deprenyl and desmethylselegiline protect mesencephalic neurons from toxicity induced by glutathione depletion. J Pharmacol Exp Ther 284:700–706
Naoi M, Ishiki R, Nomura Y, Hasegawa S, Nagatsu T (1987) Quinolinic acid: an endogenous inhibitor specific for type B monoamine oxidase in human brain synaptosomes. Neurosci Lett 74:232–236
Naoi M, Maruyama W, Nakao N, Ibi T, Sahashi K, Benedetti MS (1988) (R)salsolinol N-methyltransferase activity increases in parkinsonian lymphocytes. Ann Neurol 43:212–216. https://doi.org/10.1002/ana.410430211
Naoi M, Maruyama W, Sasuga S, Deng Y, Dostert P, Ohta S, Takahashi T (1994) Inhibition of type A monoamine oxidase by 2(N)-methyl-6,7-dihydroxyisoquinolinium ions. Neurochem Int 25:475–481
Naoi M, Muruyama W, Dostert P, Hashizume Y, Nakahara D, Takahashi T, Ota M (1996) Dopamine-derived endogenous 1(R),2(N)-dimethyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline, N-methyl-(R-salsolinol, induced parkinsonism in rat: biochemical, pathological and behavioural studies. Brain Res 709:285–295. https://doi.org/10.1016/0006-8993(95)01325-3
Naoi M, Muruyama W, Akao Y, Yi H (2002) Dopamine-derived endogenous N-methyl-(R)-salsolinol. Its role in Parkinson’s disease. Neurotoxicol Teratol 24:579–591. https://doi.org/10.1016/s0892-0362(02)00211-8
Neff NH, Goridis C (1972) Neuronal monoamine oxidase: specific enzyme types and their rates of formation. Adv Biochem Psychopharmacol 5:307–323
Nelson SD, Mitchell JR, Snodgrass WR, Timbrell JA (1978) Hepatotoxicity and metabolism of iproniazid and isopropylhydrazine. J Pharmacol Exp Ther 206:574–585
Nelson DL, Herber A, Petillot Y, Pichat L, Glowinski J, Hamon M (1979) [3H]-Harmaline as a specific ligand for MAO-A from rat and bovine brains. J Neurochem 32:1817–1827
Nic a’ Bháird N, McCrodden M, Wheatley AM, Harrington MC, Sullivan Sullivan, Tipton KF (1990) Determination of amines, amine metabolites and some amine metabolizing enzymes by high performance liquid chromatography. Biomed Chromatogr 4:229–233
O’Carroll AM, Tipton KF, Sullivan JP, Fowler CJ, Ross SB (1987) Intra- and extrasynaptosomal deamination of dopamine and noradrenaline by the two forms of human brain monoamine oxidase. Implications for the neurotoxicity of N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine in man. Biog Amines 4:165–178
O’Brien EM, Tipton KF, Strolin Benedetti M, Bonsignori A, Marrari P, Dostert P (1991) Is the oxidation of milacemide by monoamine oxidase a major factor in its anticonvulsant actions? Biochem Pharmacol 41:1731–1737. https://doi.org/10.1016/0006-2952(91)90177-7
O’Brien EM, Tipton KF, McCrodden JM, Youdim MBH (1994) The interactions of milacemide with monoamine oxidase. Biochem Pharmacol 47:617–623. https://doi.org/10.1016/0006-2952(94)90123-6
O’Brien EM, Dostert P, Tipton KF (1995) Species differences in the interactions of the anticonvulsant milacemide and some analogues with monoamine oxidase-B. Biochem Pharmacol 50:317–324. https://doi.org/10.1016/0006-2952(95)00145-p
O’Carroll AM, Bardsley ME, Tipton KF (1986) The oxidation of adrenaline and noradrenaline by the two forms of monoamine oxidase from human and rat brain. Neurochem Int 8:493–500. https://doi.org/10.1016/0197-0186(86)90182-8
O’Carroll AM, Anderson MC, Tobbia I, Phillips JP, Tipton KF (1989) Determination of the absolute concentrations of monoamine oxidase A and B in human tissues. Biochem Pharmacol 38:901–905
Oi S, Yasunobu KT (1973) Mechanistic aspects of the oxidation of amines by monoamine oxidase. Biochem Biophys Res Commun 53:631–637. https://doi.org/10.1016/0006-291x(73)90708-0
Oi S, Shimada K, Inamasu M, Yasunobu KT (1970) Mechanistic studies of beef liver mitochondrial amine oxidase XVIII. Amine oxidase. Arch Biochem Biophys 139:28–37. https://doi.org/10.1016/0003-9861(70)90041-x
Oi S, Yasunobu KT, Westley J (1971) The effect of pH on the kinetic parameters and mechanism of beef liver monoamine oxidase. Arch Biochem Biophys 145:557–564. https://doi.org/10.1016/s0003-9861(71)80015-2
Oja SS, Saransaari P, Esa R, Korpi ER (2017) Neurotoxicity of ammonia. Neurochem Res 42:713–720. https://doi.org/10.1007/s11064-016-2014-x
Olivecrona T, Oreland L (1971) Reassociation of soluble monoamine oxidase with lipid-depleted mitochondria in the presence of phospholipids. Olivecrona T, Oreland L. Biochemistry 10:332–340. https://doi.org/10.1021/bi00778a021
Oreland L (2004) Platelet monoamine oxidase. Personality and alcoholism: the rise, fall and resurrection. Neurotoxicology 25:79–89
Orologas AG, Buckman TD (1986) A comparison of platelet monoamine oxidase activity and phosphatidylserine content between chronic paranoid schizophrenics and normal controls. Neurosci Lett 88:293–298
Orru R, Aldeco M, Edmondson DE (2013) Do MAO A and MAO B utilize the same mechanism for the C–H bond cleavage step in catalysis? Evidence suggesting differing mechanisms. J Neural Transm 120:847–851
Oxenkrug GF (1999) Antidepressive and antihypertensive effects of MAO-A inhibition: role of N-acetylserotonin. A review. Neurobiology 7:213–224 (Book Chapter)
Ozaita A, Olmos G, Boronat MA, Lizcano JM, Unzeta M, García-Sevilla JA (1997) Inhibition of monoamine oxidase A and B activities by imidazol(ine)/guanidine drugs, nature of the interaction and distinction from I2-imidazoline receptors in rat liver. Br J Pharmacol 121:901–912. https://doi.org/10.1038/sj.bjp.0701214
Palfreyman MG, McDonald IA, Fozard JR, Mely Y, Sleight AJ, Zreika M, Wagner J, Bey P, Lewis PJ (1985) Inhibition of monoamine oxidase selectively in brain monoamine nerves using the bioprecursor (E)-beta-fluoromethylene-m-tyrosine (MDL 72394), a substrate for aromatic l-amino acid decarboxylase. J Neurochem 45:1850–1860. https://doi.org/10.1111/j.1471-4159.1985.tb10543.x
Parkinson Study Group (1996) Effect of lazabemide on the progression of disability in early Parkinson’s disease. Ann Neurol 40:99–107
Parkinson D, Lyles GA, Browne BJ, Callingham BA (1980) Some factors influencing the metabolism of benzylamine by type A and B monoamine oxidase in rat heart and liver. J Pharm Pharmacol 32:844–850. https://doi.org/10.1111/j.2042-7158.1980.tb13088.x
Patek DR, Hellerman L (1974) Mitochondrial monoamine oxidase. Mechanism of inhibition by phenylhydrazine and by aralkylhydrazines. Role of enzymatic oxidation. J Biol Chem 249:2373–2380
Patel M (2016) Targeting oxidative stress in central nervous system disorders. Trends Pharmacol Sci 37:768–778. https://doi.org/10.1016/j.tips.2016.06.007
Pearce LB, Roth JA (1985) Human brain monoamine oxidase type B: mechanism of deamination as probed by steady-state methods. Biochemistry 24:1821–1826. https://doi.org/10.1021/bi00329a003
Peretz C, Segev H, Rozan V, Gurevich T, El-Ad B, Judith Tsamir J, Nir Giladi N (2016) Comparison of selegiline and rasagiline therapies in parkinson disease: a real-life study. Clin Neuropharmacol 39:227–231. https://doi.org/10.1097/wnf.0000000000000167
Raddatz R, Parini A, Lanier SM (1995) Imidazoline/guanidinium binding domains on monoamine oxidases. Relationship to subtypes of imidazoline-binding proteins and tissue-specific interaction of imidazoline ligands with monoamine oxidase B. J Biol Chem 270:27961–27968. https://doi.org/10.1074/jbc.270.46.27961
Raddatz R, Parini A, Lanier SM (1997) Localization of the imidazoline binding domain on monoamine oxidase B. Mol Pharmacol 52:549–553. https://doi.org/10.1124/mol.52.4.549
Ramsay RR (1991) Kinetic mechanism of monoamine oxidase (1991). Biochemistry 30:4624–4629. https://doi.org/10.1021/bi00232a038
Ramsay RR, Tipton KF (2017) Assessment of enzyme inhibition: a review with examples from the development of monoamine oxidase and cholinesterase inhibitory drugs. Molecules 22(7):E1192. https://doi.org/10.3390/molecules22071192
Rebrin I, Geha RM, Chen K, Shih JC (2001) Effects of carboxyl-terminal truncations on the activity and solubility of human monoamine oxidase B. J Biol Chem 276:29499–29506. https://doi.org/10.1074/jbc.m100431200
Rebsam A, Seif I, Gaspar P (2005) Dissociating barrel development and lesion-induced plasticity in the mouse somatosensory cortex. J Neurosci 25:706–710
Reid AA, Hill JL, Murphy DL (1988) Interactions of tricyclic antidepressant drugs with human and rat monoamine oxidase type B. Naunyn Schmiedebergs Arch Pharmacol 338:678–683
Remaury A, Raddatz R, Ordener C, Savic S, Shih JC, Chen K, Seif I, De Maeyer E, Lanier SM, Parini A (2000) Analysis of the pharmacological and molecular heterogeneity of I(2)-imidazoline-binding proteins using monoamine oxidase-deficient mouse models. Mol Pharmacol 58:1085–1090. https://doi.org/10.1124/mol.58.5.1085
Riederer P, Lachenmayer L (2003) Selegiline’s neuroprotective capacity revisited. J. Neural Transm 110:1273–1278
Ringheim GE, Conant K (2004) Neurodegenerative disease and the neuroimmune axis (Alzheimer’s and Parkinson’s disease, and viral infections). J Neuroimmunol 147:43–49. https://doi.org/10.1016/j.jneuroim.2003.10.013
Rommelspacher H, May T, Salewski B (1994) Harman (1-methyl-beta-carboline) is a natural inhibitor of monoamine oxidase type A in rats. Eur J Pharmacol 252:51–59
Rose RM, Castellani S, Boeringa JA, Malek-Ahmadi P, Lankford DA, Bessman JD, Fritz RR, Denney CB, Denney RM, Abell CW (1986) Platelet MAO concentration and molecular activity: II. Comparison of normal and schizophrenic populations. Psychiatr Res 17:141–151
Roth JA, Eddy BJ (1980) Kinetic properties of membrane-bound and Triton X-100-solubilized human brain monoamine oxidase. Arch Biochem Biophys 205:260–266. https://doi.org/10.1016/0003-9861(80)90106-x
Sacher J, Houle S, Parkes J, Rusjan P, Sagrati S, Wilson AA, Meyer JH (2011) Monoamine oxidase A inhibitor occupancy during treatment of major depressive episodes with moclobemide or St. John's wort: an [11C]-harmine PET study. J Psychiatry Neurosci 36:375–382. https://doi.org/10.1503/jpn.100117
Sandler M, Glover V, Clow A, Elsworth JD (1985) Tribulin: an endogenous monoamine oxidase inhibitor/benzodiazepine receptor ligand. Prog Clin Biol Res 192:359–362
Schlappi B (1985) The lack of hepatotoxicity in the rat with the new reversible MAO-A inhibitor moclobemide in contrast to iproniazid. Arzneimittel Forschung (Drug Research) 35:800–803
Schmiedeberg O (1877) Ueber das Verhältniss des Ammoniaks und der primären Monaminbasen zur Harnstoffbildung im Thierkörper. Naunyn Schmiedebergs Arch Pharmacol 8:1–14. https://doi.org/10.1007/bf01831350
Schoepp DD, Azzaro AJ (1981) Specificity of endogenous substrates for types A and B monoamine oxidase in rat striatum. J Neurochem 36:2025–2031. https://doi.org/10.1111/j.1471-4159.1981.tb10829.x
Schoerlin MP, Da Prada M (1990) Species-specific biotransformation of moclobemide: a comparative study in rats and humans. Acta Psychiatr Scand Suppl 360:108–110
Schousboe A, Scafidi S, Bak LK, Waagepetersen HS, McKenna MC (2014) Glutamate metabolism in the brain focusing on astrocytes. Adv Neurobiol 11:13–30. https://doi.org/10.1007/978-3-319-08894-5_2
Schweitzer JW, Friedhoff AJ, Schwartz R (1975) Letter: chocolate, beta-phenethylamine and migraine re-examined. Nature 257:256
Sen NP (1969) Analysis and significance of tyramine in foods. J Food Sci 34:22–26
Seymour CB, Mothersill C, Mooney R, Moriarty M, Tipton KF (2003) Monoamine oxidase inhibitors l-deprenyl and clorgyline protect nonmalignant human cells from ionising radiation and chemotherapy toxicity. Br J Cancer 89:1979–1986
Sharon G, Sampson TR, Geschwind DH, Mazmanian SK (2016) The central nervous system and the gut microbiome. Cell 167:915–932. https://doi.org/10.1016/j.cell.2016.10.027
Shi X, Walter NA, Harkness JH, Neve KA, Williams RW, Lu L, Belknap JK, Eshleman AJ, Phillips TJ, Janowsky A (2016) Genetic polymorphisms affect mouse and human trace amine-associated receptor 1 function. PLoS One 11(3):e0152581. https://doi.org/10.1371/journal.pone.0152581
Shih JC (2004) Cloning, after cloning, knock-out mice, and physiological functions of MAO A and B. Neurotoxicology 25:21–30
Shih JC, Chen K, Ridd MJ (1999) Monoamine oxidase: from genes to behavior. Ann Rev Neurosci 22:197–217. https://doi.org/10.1146/annurev.neuro.22.1.197
Silverman RB (1995) Radical thoughts about the life of MAO. Prog Brain Res 106:23–31. https://doi.org/10.1016/s0079-6123(08)61198-x
Silverman RB, Zieske PA (1985) Mechanism of inactivation of monoamine oxidase by 1-phenylcyclopropylamine. Biochemistry 24:2128–2138
Singer TP, Ramsay RR, Sonsalla PK, Nicklas WJ, Heikkila RE (1993) Biochemical mechanisms underlying MPTP-induced and idiopathic Parkinsonism. New vistas. Adv Neurol 60:300–305
Smeyne RJ, Jackson-Lewis V (2005) The MPTP model of Parkinson’s disease. Brain Res Mol Brain Res 134:57–66. https://doi.org/10.1016/j.molbrainres.2004.09.017
Smith TE, Weissbach H, Udenfriend S (1963) Studies on monoamine oxidase: the mechanism of inhibition of monoamine oxidase by iproniazid. Biochemistry 2:746–751. https://doi.org/10.1021/bi00904a021
Squires RF (1972) Multiple forms of monoamine oxidase in intact mitochondria as characterized by selective inhibitors and thermal stability: a comparison of eight mammalian species. Adv Biochem Psychopharmacol 5:355–370
Starlinger H (1977) An endogenous inhibitor of amine oxidase (flavine-containing) in the carotid body of the cat. Hoppe Seylers Z Physiol Chem 358:491–497
Strebhardt K, Ullrich A (2008) Paul Ehrlich’s magic bullet concept: 100 years of progress. Nat Rev Cancer 8:473–480. https://doi.org/10.1038/nrc239
Strolin Benedetti M, Dostert P, Tipton KF (1992) Developmental aspects of the monoamine-degrading enzyme monoamine oxidase. Dev Pharmacol Ther 18:191–200
Sullivan JP, Tipton KF (1992) Interactions of the neurotoxin MPTP and its demethylated derivative (PTP) with monoamine oxidase-B. Neurochem Res 17:791–796
Swett LR, Martin WB, Taylor JD, Everett GM, Wykes AA, Gladish YC (1963) Structure-activity relations in the pargyline series. Ann N Y Acad Sci 107:891–898
Szutowicz A, Tomaszewicz M, Orsulak PJ (1989) Modification of substrate-inhibitor affinities of human platelet monoamine oxidase B in vitro. J Biol Chem 264:17660–17664
Tan AK, Ramsay RR (1993) Substrate-specific enhancement of the oxidative half-reaction of Monoamine-Oxidase. Biochemistry 32:2137–2143. https://doi.org/10.1021/bi00060a003
Tan AK, Weyler W, Salach JI, Singer TP (1991) Differences in substrate specificities of monoamine oxidase A from human liver and placenta. Biochem Biophys Res Commun 181:1084–1088
Taylor JD, Wykes AA, Gladish YC, Martin WB (1960) New inhibitor of monoamine oxidase. Nature 187:941–942
Tesson F, Limon-Boulez I, Urban P, Puype M, Vandekerckhove J, Coupry I, Pompon D, Parini A (1995) Localization of I2-imidazoline binding sites on monoamine oxidases. J Biol Chem 270:9856–9861. https://doi.org/10.1074/jbc.270.17.9856
Thrane VR, Thrane AS, Wang S, Cotrina ML et al (2013) Ammonia triggers neuronal disinhibition and seizures by impairing astrocyte potassium buffering. Nat Med 19:1643–1648. https://doi.org/10.1038/nm.3400
Tipton KF (1968) The reaction pathway of pig brain mitochondrial monoamine oxidase. Eur J Biochem 5:316–320. https://doi.org/10.1111/j.1432-1033.1968.tb00372.x
Tipton KF (1980) Kinetic mechanism and enzyme function. Biochem Soc Trans 8:242–245. https://doi.org/10.1042/bst0080242
Tipton KF, Dixon HBF (1979) Effects of pH on enzymes. Methods Enzymol 63:183–234. https://doi.org/10.1016/0076-6879(79)63011-2
Tipton KF, Spires IP (1971) The kinetics of phenethylhydrazine oxidation by monoamine oxidase. Biochem J 125:521–524. https://doi.org/10.1042/bj1250521
Tipton KF, Fowler CJ, McCrodden JM, 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 methanesulphonate (compound MD 780236) and the enzyme-catalysed oxidation of this compound as competing reactions. Biochem J 209:235–242
Tipton KF, McCrodden JM, Youdim MBH (1986) Oxidation and enzyme-activated irreversible inhibition of rat liver monoamine oxidase-B by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Biochem J 240:379–383
Tipton KF, O’Sullivan MI, Davey GP, O’Sullivan J (2003) It can be a complicated life being an enzyme. Biochem Soc Trans 31:711–771. https://doi.org/10.1042/bst0310711
Tipton KF, Davey G, Motherway M (2006) Monoamine oxidase assays. Curr Protoc Toxicol 30, Chapter 4: Unit4.21, pp 1–43. https://doi.org/10.1002/0471141755.tx0421s30
Tipton KF, Davey GP, McDonald AG (2011) Kinetic behavior and reversible inhibition of monoamine oxidases–enzymes that many want dead. Int Rev Neurobiol 100:43–64. https://doi.org/10.1016/b978-0-12-386467-3.00003-0
Toyoshima Y, Kinemuchi H, Kamijo K (1979) Nonexistence of a type C monoamine oxidase in rat brain. J Neurochem 32:1183–1189
Unzeta M, Castro J, Gomez N, Tipton KF (1983) Comparisons between the monoamine oxidase activities associated with mitochondria and microsomes in rat liver. M. Br J Pharmacol 80:662P (Abstract)
Unzeta M, Esteban G, Bolea I, Fogel WA, Ramsay RR, Youdim MB, Tipton KF, Marco-Contelles J (2016) Multi-target directed donepezil-like ligands for Alzheimer’s disease. Front Neurosci 25(10):205. https://doi.org/10.3389/fnins.2016.00205
Upadhyay AK, Borbat PP, Wang J, Freed JH, Edmondson DE (2008) Determination of the oligomeric states of human and rat monoamine oxidases in the outer mitochondrial membrane and octyl beta-d-glucopyranoside micelles using pulsed dipolar electron spin resonance spectroscopy. Biochemistry 47:1554–1566. https://doi.org/10.1021/bi7021377
Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, Telser J (2007) Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol 39:44–84. https://doi.org/10.1023/b:mcbi.0000049134.69131.89
Vazquez ML, Silverman RB (1985) Revised mechanism for inactivation of mitochondrial monoamine oxidase by N-cyclopropylbenzylamine. Biochemistry 24:6538–6543
Vilar S, Quezada E, Uriarte E, Costanzi S, Borges F, Viña D, Hripcsak G (2016) Computational drug target screening through protein interaction profiles. Sci Rep 15(6):36969. https://doi.org/10.1038/srep36969
Waldmeier PC (1993) Newer aspects of the reversible inhibitor of MAO-A and serotonin reuptake, brofaromine. Prog Neuropsychopharmacol Biol Psychiatry 17:183–198
Wang CC, Borchert A, Ugun-Klusek A, Tang LY, Lui WT, Chu CY, Billett E, Kuhn H, Ufer C (2011) Monoamine oxidase A expression is vital for embryonic brain development by modulating developmental apoptosis. J Biol Chem 286:28322–28330. https://doi.org/10.1074/jbc.m111.241422
Wang CC, Man GC, Chu CY, Borchert A, Ugun-Klusek A, Billett EE, Kühn H, Ufer C (2014) Serotonin receptor 6 mediates defective brain development in monoamine oxidase A-deficient mouse embryos. J Biol Chem 289:8252–8263. https://doi.org/10.1074/jbc.m113.522094
Wassermann AM, Lounkine E, Urban L, Whitebread S, Chen S, Hughes K, Guo H, Kutlina E, Fekete A, Klumpp M, Glick M (2014) A screening pattern recognition method finds new and divergent targets for drugs and natural products. ACS Chem Biol 9:1622–1631. https://doi.org/10.1021/cb5001839
Weinreb O, Amit T, Riederer P, Youdim MB, Mandel SA (2011) Neuroprotective profile of the multitarget drug rasagiline in Parkinson’s disease. Int Rev Neurobiol 100:127–149. https://doi.org/10.1016/b978-0-12-386467-3.00007-8
Weinreb O, Mandel S, Youdim MB, Amit T (2013) Targeting dysregulation of brain iron homeostasis in Parkinson’s disease by iron chelators. Free Radic Biol Med 62:52–64. https://doi.org/10.1016/j.freeradbiomed.2013.01.017
Weissbach H, Redfield BG, Udenfriend S (1957) Soluble monoamine oxidase; its properties and actions on serotonin. J Biol Chem 229:953–963
Westlund KN, Denney RM, Rose RM, Abell CW (1988) Localization of distinct monoamine oxidase A and monoamine oxidase B cell populations in human brainstem. Neuroscience 25:439–456. https://doi.org/10.1016/0306-4522(88)90250-3
Weyler W, Hsu YP, Breakefield XO (1990) Biochemistry and genetics of monoamine oxidase. Pharmacol Ther 47:391–417. https://doi.org/10.1016/0163-7258(90)90064-9
Whitaker-Azmitia PM, Zhang X, Clarke C (1994) Effects of gestational exposure to monoamine oxidase inhibitors in rats: preliminary behavioral and neurochemical studies. Neuropsychopharmacology. 11:125–132. https://doi.org/10.1038/npp.1994.42
Williams CH (1974) Monoamine oxidase. I. Specificity of some substrates and inhibitors. Biochem Pharmacol 23:615–628. https://doi.org/10.1016/0006-2952(74)90626-1
Wise CD, Potkin S, Bridge P, Wyatt RJ (1979) An endogenous inhibitor of platelet MAO activity in chronic schizophrenia: failure to replicate. Am J Psychiatry 197136:1336–1337
Woo JCG, Silverman RB (1995) Monoamine oxidase B catalysis in low aqueous medium. Direct evidence for an imine product. J Am Chem Soc 117:1663–1664. https://doi.org/10.1021/ja00110a033
Worland PJ, Ilett KF (1983) Intestinal contribution to the presystemic elimination of beta-phenethylamine in the rat. J Pharm Pharmacol 35:636–640
Wu Y, Kazumura K, Maruyama W, Osawa T, Naoi M (2015) Rasagiline and selegiline suppress calcium efflux from mitochondria by PK11195-induced opening of mitochondrial permeability transition pore: a novel anti-apoptotic function for neuroprotection. J Neural Transm 122:1399–1407. https://doi.org/10.1007/s00702-015-1398-0
Yelekçi K, Karahan O, Toprakçi M (2007) Docking of novel reversible monoamine oxidase-B inhibitors: efficient prediction of ligand binding sites and estimation of inhibitors thermodynamic properties. J Neural Transm 114:725–732. https://doi.org/10.1007/s00702-007-0679-7
Yera ER, Cleves AE, Jain AN (2011) Chemical structural novelty: on-targets and off-targets. J Med Chem 54:6771–6785. https://doi.org/10.1021/jm200666a
Yoshida T, Yamada Y, Yamamoto T, Kuroiwa Y (1986) Metabolism of deprenyl, a selective monoamine oxidase (MAO) B inhibitor in rat: relationship of metabolism to MAO-B inhibitory potency. Xenobiotica 16:129–136. https://doi.org/10.3109/00498258609043515
Youdim MBH, Tipton KF (2002) Rat striatal monoamine oxidase-B inhibition by l-deprenyl and rasagiline: its relationship to 2-phenylethylamine-induced stereotypy and Parkinson’s disease. Parkinsonism Relat Disord 8:247–253
Youdim MBH, Weinstock M (2004) Therapeutic applications of selective and non-selective inhibitors of monoamine oxidase A and B that do not cause significant tyramine potentiation. Neurotoxicology 25:243–250. https://doi.org/10.1016/s0161-813x(03)00103-7
Youdim MBH, Aronson JK, Blau K, Green AR, Grahame-Smith DG (1979) Tranylcypromine (‘Parnate’) overdose: measurement of tranylcypromine concentrations and MAO inhibitory activity and identification of amphetamines in plasm. Psychol Med 9:377–382
Youdim MBH, Finberg JPM, Tipton KF (1988) Monoamine oxidase. In: Trendelenburg U, Weiner N (eds) Catecholamine II. Handbook of experimental pharmacology. Springer, Berlin, pp 127–199 (Book Chapter)
Youdim MBH, Banerjee DK, Kelner K, Offutt L, Pollard HB (1989) Steroid regulation of monoamine oxidase activity in the adrenal medulla. FASEB J 3:1753–1759. https://doi.org/10.1096/fasebj.3.6.2495232
Youdim MBH, Gross A, Finberg JP (2001) Rasagiline [N-propargyl-1R(+)-aminoindan], a selective and potent inhibitor of mitochondrial monoamine oxidase B. Br J Pharmacol 132:500–506
Youdim MBH, Edmondson D, Tipton KF (2006) The therapeutic potential of monoamine oxidase inhibitors. Nat Rev Neurosci 7:295–309. https://doi.org/10.1038/nrn1883
Yu PH, Davis BA (1988) Stereospecific deamination of benzylamine catalyzed by different amine oxidases. Int J Biochem 20:1197–1201
Yu PH, Tipton KF (1989) Deuterium isotope effect of phenelzine on the inhibition of rat liver mitochondrial monoamine oxidase activity. Biochem Pharmacol 38:4245–4251. https://doi.org/10.1016/0006-2952(89)90522-4
Zeller EA (1938) Über den enzymatischen Abbau von Histamin und Diaminen. 2. Mitteilung. Helv Chim Acta 21:880–890. https://doi.org/10.1002/hlca.193802101115
Zeller EA, Barsky J (1952) In vivo inhibition of liver and brain monoamine oxidase by 1-Isonicotinyl-2-isopropyl hydrazine. Proc Soc Exp Biol Med 81:459–461. https://doi.org/10.3181/00379727-81-19910
Zeller P, Pletscher A, Gey KF, Gutmann H, Hegedüs B, Straub O (1959) Amino acid and fatty acid hydrazides: chemistry and action on monoamine oxidase. Ann N Y Acad Sci 80:555–567. https://doi.org/10.1111/j.1749-6632.1959.tb49234.x
Zhuang ZP, Marks B, McCauley RB (1992) The insertion of monoamine oxidase A into the outer membrane of rat liver mitochondria. J Biol Chem 267:591–596
Zucchi R, Chiellini G, Scanlan TS, Grandy DK (2006) Trace amine-associated receptors and their ligands. Br J Pharmacol 149:967–978. https://doi.org/10.1038/sj.bjp.0706948
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Tipton, K.F. 90 years of monoamine oxidase: some progress and some confusion. J Neural Transm 125, 1519–1551 (2018). https://doi.org/10.1007/s00702-018-1881-5
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00702-018-1881-5