Monoamine oxidases as sources of oxidants in the heart

Journal of Molecular and Cellular Cardiology

Volumn 73, Issue , 2014, Pages 34-42

  Kaludercic, Nina ^a   Mialet Perez, Jeanne ^b,c   Paolocci, Nazareno ^d   Parini, Angelo ^b,c   Di Lisa, Fabio ^a,e  

^a CNR   (Italy)

^b University Hospital of Toulouse   (France)

^c UNIVERSITÉ PAUL SABATIER   (France)

^d DEPARTMENT OF PATHOLOGY   (United States)

^e UNIVERSITY OF PADOVA   (Italy)

Author keywords

Heart failure; Ischemia reperfusion injury; Mitochondrial dysfunction; Monoamine oxidase; Oxidative stress

Indexed keywords

ALDEHYDE; AMINE OXIDASE (FLAVIN CONTAINING); CATECHOLAMINE; DOPAMINE; NORADRENALIN; REACTIVE OXYGEN METABOLITE; SEROTONIN; HYDROGEN PEROXIDE; OXIDIZING AGENT;

APOPTOSIS; CARDIOVASCULAR DISEASE; CELLULAR DISTRIBUTION; DISEASE SEVERITY; DISORDERS OF MITOCHONDRIAL FUNCTIONS; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME LOCALIZATION; HEART FUNCTION; HEART MUSCLE CELL; HEART MUSCLE INJURY; HEART PROTECTION; HEART VENTRICLE HYPERTROPHY; HUMAN; NONHUMAN; NORADRENALIN RELEASE; NORADRENALIN UPTAKE; OXIDATIVE STRESS; PATHOGENESIS; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; REVIEW; ANIMAL; ENZYMOLOGY; HEART MUSCLE; METABOLISM; PHYSIOLOGY;

ALDEHYDES; ANIMALS; HUMANS; HYDROGEN PEROXIDE; MONOAMINE OXIDASE; MYOCARDIUM; OXIDANTS; OXIDATIVE STRESS;

EID: 84901850631     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2013.12.032     Document Type: Review

References (119)

1. Balaban R.S., Nemoto S., Finkel T. Mitochondria, oxidants, and aging. Cell 2005, 120:483-495.
2. Droge W. Free radicals in the physiological control of cell function. Physiol Rev 2002, 82:47-95.
3. Murphy M.P. How mitochondria produce reactive oxygen species. Biochem J 2009, 417:1-13.
4. Turrens J.F. Mitochondrial formation of reactive oxygen species. J Physiol 2003, 552:335-344.
5. Brand M.D. The sites and topology of mitochondrial superoxide production. Exp Gerontol 2010, 45:466-472.
6. Li Y., Huang T.T., Carlson E.J., Melov S., Ursell P.C., Olson J.L., et al. Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat Genet 1995, 11:376-381.
7. Dai D.F., Chen T., Wanagat J., Laflamme M., Marcinek D.J., Emond M.J., et al. Age-dependent cardiomyopathy in mitochondrial mutator mice is attenuated by overexpression of catalase targeted to mitochondria. Aging Cell 2010, 9:536-544.
8. Dai D.F., Santana L.F., Vermulst M., Tomazela D.M., Emond M.J., MacCoss M.J., et al. Overexpression of catalase targeted to mitochondria attenuates murine cardiac aging. Circulation 2009, 119:2789-2797.
9. Lee H.Y., Choi C.S., Birkenfeld A.L., Alves T.C., Jornayvaz F.R., Jurczak M.J., et al. Targeted expression of catalase to mitochondria prevents age-associated reductions in mitochondrial function and insulin resistance. Cell Metab 2010, 12:668-674.
10. Schriner S.E., Linford N.J., Martin G.M., Treuting P., Ogburn C.E., Emond M., et al. Extension of murine life span by overexpression of catalase targeted to mitochondria. Science 2005, 308:1909-1911.
11. Giorgio M., Migliaccio E., Orsini F., Paolucci D., Moroni M., Contursi C., et al. Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell 2005, 122:221-233.
12. Migliaccio E., Giorgio M., Mele S., Pelicci G., Reboldi P., Pandolfi P.P., et al. The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature 1999, 402:309-313.
13. Orsini F., Migliaccio E., Moroni M., Contursi C., Raker V.A., Piccini D., et al. The life span determinant p66Shc localizes to mitochondria where it associates with mitochondrial heat shock protein 70 and regulates trans-membrane potential. J Biol Chem 2004, 279:25689-25695.
14. Trinei M., Giorgio M., Cicalese A., Barozzi S., Ventura A., Migliaccio E., et al. A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis. Oncogene 2002, 21:3872-3878.
15. Giorgio M., Berry A., Berniakovich I., Poletaeva I., Trinei M., Stendardo M., et al. The p66Shc knocked out mice are short lived under natural condition. Aging Cell 2012, 11:162-168.
16. Carpi A., Menabo R., Kaludercic N., Pelicci P., Di Lisa F., Giorgio M. The cardioprotective effects elicited by p66(Shc) ablation demonstrate the crucial role of mitochondrial ROS formation in ischemia/reperfusion injury. Biochim Biophys Acta 2009, 1787:774-780.
17. Spescha R.D., Shi Y., Wegener S., Keller S., Weber B., Wyss M.M., et al. Deletion of the ageing gene p66(Shc) reduces early stroke size following ischaemia/reperfusion brain injury. Eur Heart J 2013, 34:96-103.
18. Fadini G.P., Albiero M., Menegazzo L., Boscaro E., Pagnin E., Iori E., et al. The redox enzyme p66Shc contributes to diabetes and ischemia-induced delay in cutaneous wound healing. Diabetes 2010, 59:2306-2314.
19. Rota M., LeCapitaine N., Hosoda T., Boni A., De Angelis A., Padin-Iruegas M.E., et al. Diabetes promotes cardiac stem cell aging and heart failure, which are prevented by deletion of the p66shc gene. Circ Res 2006, 99:42-52.
20. Menini S., Amadio L., Oddi G., Ricci C., Pesce C., Pugliese F., et al. Deletion of p66Shc longevity gene protects against experimental diabetic glomerulopathy by preventing diabetes-induced oxidative stress. Diabetes 2006, 55:1642-1650.
21. Camici G.G., Schiavoni M., Francia P., Bachschmid M., Martin-Padura I., Hersberger M., et al. Genetic deletion of p66(Shc) adaptor protein prevents hyperglycemia-induced endothelial dysfunction and oxidative stress. Proc Natl Acad Sci U S A 2007, 104:5217-5222.
22. Touyz R.M., Montezano A.C. Vascular Nox4: a multifarious NADPH oxidase. Circ Res 2012, 110:1159-1161.
23. Martyn K.D., Frederick L.M., von Loehneysen K., Dinauer M.C., Knaus U.G. Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases. Cell Signal 2006, 18:69-82.
24. Lyle A.N., Deshpande N.N., Taniyama Y., Seidel-Rogol B., Pounkova L., Du P., et al. Poldip2, a novel regulator of Nox4 and cytoskeletal integrity in vascular smooth muscle cells. Circ Res 2009, 105:249-259.
25. Park H.S., Chun J.N., Jung H.Y., Choi C., Bae Y.S. Role of NADPH oxidase 4 in lipopolysaccharide-induced proinflammatory responses by human aortic endothelial cells. Cardiovasc Res 2006, 72:447-455.
26. Mahadev K., Motoshima H., Wu X., Ruddy J.M., Arnold R.S., Cheng G., et al. The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction. Mol Cell Biol 2004, 24:1844-1854.
27. Gorin Y., Ricono J.M., Kim N.H., Bhandari B., Choudhury G.G., Abboud H.E. Nox4 mediates angiotensin II-induced activation of Akt/protein kinase B in mesangial cells. Am J Physiol Renal Physiol 2003, 285:F219-F229.
28. Kuroda J., Ago T., Matsushima S., Zhai P., Schneider M.D., Sadoshima J. NADPH oxidase 4 (Nox4) is a major source of oxidative stress in the failing heart. Proc Natl Acad Sci U S A 2010, 107:15565-15570.
29. Zhang M., Brewer A.C., Schroder K., Santos C.X., Grieve D.J., Wang M., et al. NADPH oxidase-4 mediates protection against chronic load-induced stress in mouse hearts by enhancing angiogenesis. Proc Natl Acad Sci U S A 2010, 107:18121-18126.
30. Kleinschnitz C., Grund H., Wingler K., Armitage M.E., Jones E., Mittal M., et al. Post-stroke inhibition of induced NADPH oxidase type 4 prevents oxidative stress and neurodegeneration. PLoS Biol 2010, 8.
31. Maalouf R.M., Eid A.A., Gorin Y.C., Block K., Escobar G.P., Bailey S., et al. Nox4-derived reactive oxygen species mediate cardiomyocyte injury in early type 1 diabetes. Am J Physiol Cell Physiol 2012, 302:C597-C604.
32. Sorescu D., Weiss D., Lassegue B., Clempus R.E., Szocs K., Sorescu G.P., et al. Superoxide production and expression of nox family proteins in human atherosclerosis. Circulation 2002, 105:1429-1435.
33. Schroder K., Zhang M., Benkhoff S., Mieth A., Pliquett R., Kosowski J., et al. Nox4 is a protective reactive oxygen species generating vascular NADPH oxidase. Circ Res 2012, 110:1217-1225.
34. Youdim M.B., Edmondson D., Tipton K.F. The therapeutic potential of monoamine oxidase inhibitors. Nat Rev Neurosci 2006, 7:295-309.
35. Sturza A., Leisegang M.S., Babelova A., Schroder K., Benkhoff S., Loot A.E., et al. Monoamine oxidases are mediators of endothelial dysfunction in the mouse aorta. Hypertension 2013, 62:140-146.
36. Kaludercic N., Carpi A., Menabo R., Di Lisa F., Paolocci N. Monoamine oxidases (MAO) in the pathogenesis of heart failure and ischemia/reperfusion injury. Biochim Biophys Acta 1813, 2011:1323-1332.
37. Riederer P., Lachenmayer L., Laux G. Clinical applications of MAO-inhibitors. Curr Med Chem 2004, 11:2033-2043.
38. Bach A.W., Lan N.C., Johnson D.L., Abell C.W., Bembenek M.E., Kwan S.W., et al. cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A 1988, 85:4934-4938.
39. Edmondson D.E., Mattevi A., Binda C., Li M., Hubalek F. Structure and mechanism of monoamine oxidase. Curr Med Chem 2004, 11:1983-1993.
40. Edmondson D.E., Binda C., Mattevi A. The FAD binding sites of human monoamine oxidases A and B. Neurotoxicology 2004, 25:63-72.
41. Abell C.W., Kwan S.W. Molecular characterization of monoamine oxidases A and B. Prog Nucleic Acid Res Mol Biol 2001, 65:129-156.
42. Binda C., Mattevi A., Edmondson D.E. Structural properties of human monoamine oxidases A and B. Int Rev Neurobiol 2011, 100:1-11.
43. Son S.Y., Ma J., Kondou Y., Yoshimura M., Yamashita E., Tsukihara T. Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors. Proc Natl Acad Sci U S A 2008, 105:5739-5744.
44. Li M., Hubalek F., Newton-Vinson P., Edmondson D.E. High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr Purif 2002, 24:152-162.
45. Newton-Vinson P., Hubalek F., Edmondson D.E. High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr Purif 2000, 20:334-345.
46. Bortolato M., Shih J.C. Behavioral outcomes of monoamine oxidase deficiency: preclinical and clinical evidence. Int Rev Neurobiol 2011, 100:13-42.
47. Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 2006, 23:607-618.
48. Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., et al. Regulation of cellular metabolism by protein lysine acetylation. Science 2010, 327:1000-1004.
49. Lundby A., Lage K., Weinert B.T., Bekker-Jensen D.B., Secher A., Skovgaard T., et al. Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Cell Rep 2012, 2:419-431.
50. Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., et al. Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun 2012, 3:876.
51. Cao X., Rui L., Pennington P.R., Chlan-Fourney J., Jiang Z., Wei Z., et al. Serine 209 resides within a putative p38(MAPK) consensus motif and regulates monoamine oxidase-A activity. J Neurochem 2009, 111:101-110.
52. Berry M.D., Juorio A.V., Paterson I.A. The functional role of monoamine oxidases A and B in the mammalian central nervous system. Prog Neurobiol 1994, 42:375-391.
53. Kitahama K., Maeda T., Denney R.M., Jouvet M. Monoamine oxidase: distribution in the cat brain studied by enzyme- and immunohistochemistry: recent progress. Prog Neurobiol 1994, 42:53-78.
54. Luque J.M., Biou V., Nicholls J.G. Three-dimensional visualization of the distribution, growth, and regeneration of monoaminergic neurons in whole mounts of immature mammalian CNS. J Comp Neurol 1998, 390:427-438.
55. Arai R., Kimura H., Nagatsu I., Maeda T. Preferential localization of monoamine oxidase type A activity in neurons of the locus coeruleus and type B activity in neurons of the dorsal raphe nucleus of the rat: a detailed enzyme histochemical study. Brain Res 1997, 745:352-356.
56. Levitt P., Pintar J.E., Breakefield X.O. Immunocytochemical demonstration of monoamine oxidase B in brain astrocytes and serotonergic neurons. Proc Natl Acad Sci U S A 1982, 79:6385-6389.
57. Westlund K.N., Denney R.M., Rose R.M., Abell C.W. Localization of distinct monoamine oxidase A and monoamine oxidase B cell populations in human brainstem. Neuroscience 1988, 25:439-456.
58. Westlund K.N., Denney R.M., Kochersperger L.M., Rose R.M., Abell C.W. Distinct monoamine oxidase A and B populations in primate brain. Science 1985, 230:181-183.
59. Huang Y.H., Ito A., Arai R. Immunohistochemical localization of monoamine oxidase type B in pancreatic islets of the rat. J Histochem Cytochem 2005, 53:1149-1158.
60. Huang Y.H., Jiang M., Fu B.Y. Immunocytochemical localization of monoamine oxidase type B in rat liver. Eur J Histochem 2008, 52:11-18.
61. Sivasubramaniam S.D., Finch C.C., Rodriguez M.J., Mahy N., Billett E.E. A comparative study of the expression of monoamine oxidase-A and -B mRNA and protein in non-CNS human tissues. Cell Tissue Res 2003, 313:291-300.
62. Saura J., Kettler R., Da P.M., Richards J.G. Quantitative enzyme radioautography with 3H-Ro 41-1049 and 3H-Ro 19-6327 in vitro: localization and abundance of MAO-A and MAO-B in rat CNS, peripheral organs, and human brain. J Neurosci 1992, 12:1977-1999.
63. de Champlain J., Mueller R.A., Axelrod J. Subcellular localization of monoamine oxidase in rat tissues. J Pharmacol Exp Ther 1969, 166:339-345.
64. Wang J., Edmondson D.E. Topological probes of monoamine oxidases A and B in rat liver mitochondria: inhibition by TEMPO-substituted pargyline analogues and inactivation by proteolysis. Biochemistry 2011, 50:2499-2505.
65. Binda C., Milczek E.M., Bonivento D., Wang J., Mattevi A., Edmondson D.E. Lights and shadows on monoamine oxidase inhibition in neuroprotective pharmacological therapies. Curr Top Med Chem 2011, 11:2788-2796.
66. Edmondson D.E., Binda C., Wang J., Upadhyay A.K., Mattevi A. Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases. Biochemistry 2009, 48:4220-4230.
67. Martinelle K., Haggstrom L. Mechanisms of ammonia and ammonium ion toxicity in animal cells: transport across cell membranes. J Biotechnol 1993, 30:339-350.
68. Visek W.J. Some aspects of ammonia toxicity in animal cells. J Dairy Sci 1968, 51:286-295.
69. Eisenhofer G., Kopin I.J., Goldstein D.S. Catecholamine metabolism: a contemporary view with implications for physiology and medicine. Pharmacol Rev 2004, 56:331-349.
70. Jinsmaa Y., Florang V.R., Rees J.N., Anderson D.G., Strack S., Doorn J.A. Products of oxidative stress inhibit aldehyde oxidation and reduction pathways in dopamine catabolism yielding elevated levels of a reactive intermediate. Chem Res Toxicol 2009, 22:835-841.
71. Chen C.H., Budas G.R., Churchill E.N., Disatnik M.H., Hurley T.D., Mochly-Rosen D. Activation of aldehyde dehydrogenase-2 reduces ischemic damage to the heart. Science 2008, 321:1493-1495.
72. Ikeda K., Tojo K., Otsubo C., Udagawa T., Kumazawa K., Ishikawa M., et al. 5-Hydroxytryptamine synthesis in HL-1 cells and neonatal rat cardiocytes. Biochem Biophys Res Commun 2005, 328:522-525.
73. Rouzaud-Laborde C., Hanoun N., Baysal I., Rech J.S., Mias C., Calise D., et al. Role of endothelial AADC in cardiac synthesis of serotonin and nitrates accumulation. PLoS One 2012, 7:e34893.
74. Nebigil C.G., Jaffre F., Messaddeq N., Hickel P., Monassier L., Launay J.M., et al. Overexpression of the serotonin 5-HT2B receptor in heart leads to abnormal mitochondrial function and cardiac hypertrophy. Circulation 2003, 107:3223-3229.
75. Hutcheson J.D., Setola V., Roth B.L., Merryman W.D. Serotonin receptors and heart valve disease-it was meant 2B. Pharmacol Ther 2011, 132:146-157.
76. Rajesh K.G., Suzuki R., Maeda H., Murio Y., Sasaguri S. 5-HT2 receptor blocker sarpogrelate prevents downregulation of antiapoptotic protein Bcl-2 and protects the heart against ischemia-reperfusion injury. Life Sci 2006, 79:1749-1755.
77. Levy R.J. Serotonin transporter mechanisms and cardiac disease. Circulation 2006, 113:2-4.
78. Nebigil C.G., Maroteaux L. Functional consequence of serotonin/5-HT2B receptor signaling in heart: role of mitochondria in transition between hypertrophy and heart failure?. Circulation 2003, 108:902-908.
79. Bianchi P., Pimentel D.R., Murphy M.P., Colucci W.S., Parini A. A new hypertrophic mechanism of serotonin in cardiac myocytes: receptor-independent ROS generation. FASEB J 2005, 19:641-643.
80. Villeneuve C., Guilbeau-Frugier C., Sicard P., Lairez O., Ordener C., Duparc T., et al. p53-PGC-1alpha pathway mediates oxidative mitochondrial damage and cardiomyocyte necrosis induced by monoamine oxidase-A upregulation: role in chronic left ventricular dysfunction in mice. Antioxid Redox Signal 2013, 18:5-18.
81. Himura Y., Felten S.Y., Kashiki M., Lewandowski T.J., Delehanty J.M., Liang C.S. Cardiac noradrenergic nerve terminal abnormalities in dogs with experimental congestive heart failure. Circulation 1993, 88:1299-1309.
82. Liang C.S., Fan T.H., Sullebarger J.T., Sakamoto S. Decreased adrenergic neuronal uptake activity in experimental right heart failure. A chamber-specific contributor to beta-adrenoceptor downregulation. J Clin Invest 1989, 84:1267-1275.
83. Nozawa T., Igawa A., Yoshida N., Maeda M., Inoue M., Yamamura Y., et al. Dual-tracer assessment of coupling between cardiac sympathetic neuronal function and downregulation of beta-receptors during development of hypertensive heart failure of rats. Circulation 1998, 97:2359-2367.
84. Backs J., Haunstetter A., Gerber S.H., Metz J., Borst M.M., Strasser R.H., et al. The neuronal norepinephrine transporter in experimental heart failure: evidence for a posttranscriptional downregulation. J Mol Cell Cardiol 2001, 33:461-472.
85. Eisenhofer G., Friberg P., Rundqvist B., Quyyumi A.A., Lambert G., Kaye D.M., et al. Cardiac sympathetic nerve function in congestive heart failure. Circulation 1996, 93:1667-1676.
86. Lee C.M., Javitch J.A., Snyder S.H. Recognition sites for norepinephrine uptake: regulation by neurotransmitter. Science 1983, 220:626-629.
87. Chidsey C.A., Sonnenblick E.H., Morrow A.G., Braunwald E. Norepinephrine stores and contractile force of papillary muscle from the failing human heart. Circulation 1966, 33:43-51.
88. Kaludercic N., Takimoto E., Nagayama T., Feng N., Lai E.W., Bedja D., et al. Monoamine oxidase A-mediated enhanced catabolism of norepinephrine contributes to adverse remodeling and pump failure in hearts with pressure overload. Circ Res 2010, 106:193-202.
89. Schroeder C., Jordan J. Norepinephrine transporter function and human cardiovascular disease. Am J Physiol Heart Circ Physiol 2012, 303:H1273-H1282.
90. Pool P.E., Covell J.W., Levitt M., Gibb J., Braunwald E. Reduction of cardiac tyrosine hydroxylase activity in experimental congestive heart failure. Its role in the depletion of cardiac norepinephrine stores. Circ Res 1967, 20:349-353.
91. Dorris R.L. A simple method for screening monoamine oxidase (MAO) inhibitory drugs for type preference. J Pharmacol Methods 1982, 7:133-137.
92. Kaludercic N., Carpi A., Nagayama T., Sivakumaran V., Zhu G., Lai E.W., et al. Monoamine oxidase B prompts mitochondrial and cardiac dysfunction in pressure overloaded hearts. Antioxid Redox Signal 2014, 20:267-280.
93. Bueno O.F., De Windt L.J., Tymitz K.M., Witt S.A., Kimball T.R., Klevitsky R., et al. The MEK1-ERK1/2 signaling pathway promotes compensated cardiac hypertrophy in transgenic mice. EMBO J 2000, 19:6341-6350.
94. Shioda N., Yamamoto Y., Watanabe M., Binas B., Owada Y., Fukunaga K. Heart-type fatty acid binding protein regulates dopamine D2 receptor function in mouse brain. J Neurosci 2010, 30:3146-3155.
95. Ding G., Wiegerinck R.F., Shen M., Cojoc A., Zeidenweber C.M., Wagner M.B. Dopamine increases L-type calcium current more in newborn than adult rabbit cardiomyocytes via D1 and beta2 receptors. Am J Physiol Heart Circ Physiol 2008, 294:H2327-H2335.
96. Cases O., Seif I., Grimsby J., Gaspar P., Chen K., Pournin S., et al. Aggressive behavior and altered amounts of brain serotonin and norepinephrine in mice lacking MAOA. Science 1995, 268:1763-1766.
97. Scott A.L., Bortolato M., Chen K., Shih J.C. Novel monoamine oxidase A knock out mice with human-like spontaneous mutation. Neuroreport 2008, 19:739-743.
98. Bortolato M., Chen K., Godar S.C., Chen G., Wu W., Rebrin I., et al. Social deficits and perseverative behaviors, but not overt aggression, in MAO-A hypomorphic mice. Neuropsychopharmacology 2011, 36:2674-2688.
99. Grimsby J., Toth M., Chen K., Kumazawa T., Klaidman L., Adams J.D., et al. Increased stress response and beta-phenylethylamine in MAOB-deficient mice. Nat Genet 1997, 17:206-210.
100. Chen K., Holschneider D.P., Wu W., Rebrin I., Shih J.C. A spontaneous point mutation produces monoamine oxidase A/B knock-out mice with greatly elevated monoamines and anxiety-like behavior. J Biol Chem 2004, 279:39645-39652.
101. Lairez O., Calise D., Bianchi P., Ordener C., Spreux-Varoquaux O., Guilbeau-Frugier C., et al. Genetic deletion of MAO-A promotes serotonin-dependent ventricular hypertrophy by pressure overload. J Mol Cell Cardiol 2009, 46:587-595.
102. Pchejetski D., Kunduzova O., Dayon A., Calise D., Seguelas M.H., Leducq N., et al. Oxidative stress-dependent sphingosine kinase-1 inhibition mediates monoamine oxidase A-associated cardiac cell apoptosis. Circ Res 2007, 100:41-49.
103. Poon C.C., Seto S.W., Au A.L., Zhang Q., Li R.W., Lee W.Y., et al. Mitochondrial monoamine oxidase-A-mediated hydrogen peroxide generation enhances 5-hydroxytryptamine-induced contraction of rat basilar artery. Br J Pharmacol 2010, 161:1086-1098.
104. Coatrieux C., Sanson M., Negre-Salvayre A., Parini A., Hannun Y., Itohara S., et al. MAO-A-induced mitogenic signaling is mediated by reactive oxygen species, MMP-2, and the sphingolipid pathway. Free Radic Biol Med 2007, 43:80-89.
105. Lymperopoulos A., Rengo G., Koch W.J. Adrenergic nervous system in heart failure: pathophysiology and therapy. Circ Res 2013, 113:739-753.
106. Nigmatullina R.R., Kirillova V.V., Jourjikiya R.K., Mukhamedyarov M.A., Kudrin V.S., Klodt P.M., et al. Disrupted serotonergic and sympathoadrenal systems in patients with chronic heart failure may serve as new therapeutic targets and novel biomarkers to assess severity, progression and response to treatment. Cardiology 2009, 113:277-286.
107. Maurel A., Hernandez C., Kunduzova O., Bompart G., Cambon C., Parini A., et al. Age-dependent increase in hydrogen peroxide production by cardiac monoamine oxidase A in rats. Am J Physiol Heart Circ Physiol 2003, 284:H1460-H1467.
108. Petrak J., Pospisilova J., Sedinova M., Jedelsky P., Lorkova L., Vit O., et al. Proteomic and transcriptomic analysis of heart failure due to volume overload in a rat aorto-caval fistula model provides support for new potential therapeutic targets - monoamine oxidase A and transglutaminase 2. Proteome Sci 2011, 9:69.
109. Kong S.W., Bodyak N., Yue P., Liu Z., Brown J., Izumo S., et al. Genetic expression profiles during physiological and pathological cardiac hypertrophy and heart failure in rats. Physiol Genomics 2005, 21:34-42.
110. Jin H., Yang R., Awad T.A., Wang F., Li W., Williams S.P., et al. Effects of early angiotensin-converting enzyme inhibition on cardiac gene expression after acute myocardial infarction. Circulation 2001, 103:736-742.
111. Strom C.C., Kruhoffer M., Knudsen S., Stensgaard-Hansen F., Jonassen T.E., Orntoft T.F., et al. Identification of a core set of genes that signifies pathways underlying cardiac hypertrophy. Comp Funct Genomics 2004, 5:459-470.
112. Siddiqui A., Mallajosyula J.K., Rane A., Andersen J.K. Ability to delay neuropathological events associated with astrocytic MAO-B increase in a Parkinsonian mouse model: implications for early intervention on disease progression. Neurobiol Dis 2011, 43:527-532.
113. Mallajosyula J.K., Kaur D., Chinta S.J., Rajagopalan S., Rane A., Nicholls D.G., et al. MAO-B elevation in mouse brain astrocytes results in Parkinson's pathology. PLoS One 2008, 3:e1616.
114. Irwin W.A., Bergamin N., Sabatelli P., Reggiani C., Megighian A., Merlini L., et al. Mitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency. Nat Genet 2003, 35:367-371.
115. O'Brien P.J., Siraki A.G., Shangari N. Aldehyde sources, metabolism, molecular toxicity mechanisms, and possible effects on human health. Crit Rev Toxicol 2005, 35:609-662.
116. Alnouti Y., Klaassen C.D. Tissue distribution, ontogeny, and regulation of aldehyde dehydrogenase (Aldh) enzymes mRNA by prototypical microsomal enzyme inducers in mice. Toxicol Sci 2008, 101:51-64.
117. Chen C.H., Sun L., Mochly-Rosen D. Mitochondrial aldehyde dehydrogenase and cardiac diseases. Cardiovasc Res 2010, 88:51-57.
118. Burke W.J., Li S.W., Chung H.D., Ruggiero D.A., Kristal B.S., Johnson E.M., et al. Neurotoxicity of MAO metabolites of catecholamine neurotransmitters: role in neurodegenerative diseases. Neurotoxicology 2004, 25:101-115.
119. van Haelst I.M., van Klei W.A., Doodeman H.J., Kalkman C.J., Egberts T.C., Group M.S. Antidepressive treatment with monoamine oxidase inhibitors and the occurrence of intraoperative hemodynamic events: a retrospective observational cohort study. J Clin Psychiatry 2012, 73:1103-1109.