The Korean Journal of Physiology and Pharmacology

  • 제10권4호
  • /
  • Pages.207-212
  • /
  • 2006
  • /
  • 1226-4512(pISSN)
  • /
  • 2093-3827(eISSN)
대한약리학회 (The Korean Society of Pharmacology)
권호 표지

Monoamine Oxidase Inhibitors Attenuate Cytotoxicity of 1-Methyl-4-phenylpyridinium by Suppressing Mitochondrial Permeability Transition

  • Lee, Chung-Soo (Department of Pharmacology, College of Medicine, Chung-Ang University)
  • 발행 : 2006.08.30
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Mitochondrial permeability transition has been shown to be involved in neuronal cell death. Mitochondrial monoamine oxidase (MAO)-B is considered to play a part in the progress of nigrostriatal cell death. The present study examined the effect of MAO inhibitors against the toxicity of 1-methyl-4-phenylpyridinium $(MPP^+)$ in relation to the mitochondrial permeability transition. Chlorgyline (a selective inhibitor of MAO-A), deprenyl (a selective inhibitor of MAO-B) and tranylcypromine (nonselective inhibitor of MAO) all prevented cell viability loss, cytochrome c release, caspase-3 activation, formation of reactive oxygen species and depletion of GSH in differentiated PC12 cells treated with $500\;{\mu}M$$MPP^+$. The MAO inhibitors at $10\;{\mu}M$ revealed a maximal inhibitory effect and beyond this concentration the inhibitory effect declined. On the basis of concentration, the inhibitory potency was tranylcypromine, deprenyl and chlorgyline order. The results suggest that chlorgyline, deprenyl and tranylcypromine attenuate the toxicity of $MPP^+$ against PC12 cells by suppressing the mitochondrial permeability transition that seems to be mediated by oxidative stress.

키워드

참고문헌

  1. Andoh T, Chock PB, Murphy DL, Chiueh CC. Role of the redox protein thioredox in cytoprotective mechanism evoked by (-)-deprenyl. Mol Pharmacol 68: 1408-1414, 2005 https://doi.org/10.1124/mol.105.012302
  2. Birkmayer W, Knoll J, Riederer P, Youdim MB, Hars V, Marton J. 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, 1985 https://doi.org/10.1007/BF01245973
  3. Cassarino DS, Parks JK, Parker Jr WD, Bennett Jr JP. The Parkinsonian neurotoxin $MPP^+$ opens the mitochondrial permeability transition pore and releases cytochrome c in isolated mitochondria via an oxidative mechanism. Biochim Biophys Acta 1453: 49-62, 1999 https://doi.org/10.1016/S0925-4439(98)00083-0
  4. Chandra J, Samali A, Orrenius S. Triggering and modulation of apoptosis by oxidative stress. Free Radic Biol Med 29: 323-333, 2000 https://doi.org/10.1016/S0891-5849(00)00302-6
  5. Constantini PC, Chernyak BC, Petronilli V, Bernardi P. Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J Biol Chem 271: 6746-6751, 1996 https://doi.org/10.1074/jbc.271.12.6746
  6. Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem J 341: 233-249, 1999 https://doi.org/10.1042/0264-6021:3410233
  7. Crow MT, Mani K, Nam Y-J, Kitsis RN. The mitochondrial death pathway and cardiac myocyte apoptosis. Circ Res 95: 957-970, 2004 https://doi.org/10.1161/01.RES.0000148632.35500.d9
  8. Fonck C, Baudry M. Toxic effects of $MPP^+$ and MPTP in PC12 cells independent of reactive oxygen species formation. Brain Res 905: 199-206, 2001 https://doi.org/10.1016/S0006-8993(01)02551-3
  9. Fu W, Luo H, Parthasarathy S, Mattson MP. Catecholamines potentiate amyloid $\beta$-peptide neurotoxicity: involvement of oxidative stress, mitochondrial dysfunction, and perturbed calcium homeostasis. Neurobiol Dis 5: 229-243, 1998 https://doi.org/10.1006/nbdi.1998.0192
  10. Hall AG. The role of glutathione in the regulation of apoptosis. Eur J Clin Invest 29: 238-245, 1999 https://doi.org/10.1046/j.1365-2362.1999.00447.x
  11. Kadota T, Yamaai T, Saito Y, Akita Y, Kawashima S, Moroi K, Inagaki N, Kadota K. Expression of dopamine transporter at the tips of growing neurites of PC12 cells. J Histochem Cytochem 44: 989-996, 1996 https://doi.org/10.1177/44.9.8773564
  12. Kim R, Emi M, Tanabe K. Role of mitochondria as the gardens of cell death. Cancer Chemother Pharmacol 57: 545-553, 2006 https://doi.org/10.1007/s00280-005-0111-7
  13. Lai C-T, Yu PH. Dopamine- and L-$\beta$-3,4-dihydroxyphenylalanine hydrochloride (L-DOPA)-induced cytotoxicity towards catecholaminergic neuroblastoma SH-SY5Y cells. Effects of oxidative stress and antioxidative factors. Biochem Pharmacol 53: 363-372, 1997 https://doi.org/10.1016/S0006-2952(96)00731-9
  14. Le W, Jankovic J, Xie W, Kong R, Appel SH. (-)-Deprenyl protection of 1-methyl-4-phenylpyridium ion ($MPP^+$)-induced apoptosis independent of MAO-B inhibition. Neurosci Lett 224: 197-200, 1997 https://doi.org/10.1016/S0304-3940(97)00170-5
  15. Lee CS, Han ES, Jang YY, Han JH, Ha HW, Kim DE. Protective effect of harmalol and harmaline on MPTP neurotoxicity in the mouse and dopamine-induced damage of brain mitochondria and PC12 Cells. J Neurochem 75: 521-531, 2000 https://doi.org/10.1046/j.1471-4159.2000.0750521.x
  16. Lee CS, Han JH, Jang YY, Song JH, Han ES. Differential effect of catecholamines and $MPP^+$ on membrane permeability in brain mitochondria and cell viability in PC12 cells. Neurochem Int 40: 361-369, 2002 https://doi.org/10.1016/S0197-0186(01)00069-9
  17. Lee CS, Park SY, Ko HH, Song JH, Shin YK, Han ES. Inhibition of $MPP^+$-induced mitochondrial damage and cell death by rifluoperazine and W-7 in PC12 cells. Neurochem Int 46; 169-178, 2005 https://doi.org/10.1016/j.neuint.2004.07.007
  18. Lotharius J, Dugan LL, O'Malley KL. Distinct mechanisms underlie neurotoxin-mediated cell death in cultured dopaminergic neurons. J Neurosci 19: 1284-1293, 1999 https://doi.org/10.1523/JNEUROSCI.19-04-01284.1999
  19. Maher P, Davis JB. The role of monoamine metabolism in oxidative glutamate toxicity. Neuroscience 16: 6394-6401, 1996 https://doi.org/10.1523/JNEUROSCI.16-20-06394.1996
  20. Marcocci L, De Marchi U, Salvi M, Milella ZG, Nocera S, Agostinelli E, Mondovi B, Toninello A. Tyramine and monoamine oxidase inhibitors as modulators of the mitochondrial membrane permeability transition. J Membr Biol 188: 23-31, 2002 https://doi.org/10.1007/s00232-001-0169-z
  21. Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65: 55-63, 1983 https://doi.org/10.1016/0022-1759(83)90303-4
  22. Obata T. Dopamine efflux by MPTP and hydroxyl radical generation. J Neural Transm 109: 1159-1180, 2002 https://doi.org/10.1007/s00702-001-0683-2
  23. Rojas P, Rios C. Increased striatal lipid peroxidation after intracerebroventricular $MPP^+$ administration to mice. Pharamcol Toxicol 72: 364-368, 1993 https://doi.org/10.1111/j.1600-0773.1993.tb01345.x
  24. Tan S, Sagara Y, Liu Y, Maher P, Schubert D. The regulation of reactive oxygen species production during programmed cell death. J Cell Biol 141: 1423-1432, 1998 https://doi.org/10.1083/jcb.141.6.1423
  25. Tatton WG, Chalmers-Redman RME. Modulation of gene expression rather than monoamine oxidase inhibition. Neurology 47(Suppl. 3): S171-S183, 1996 https://doi.org/10.1212/WNL.47.6_Suppl_3.171S
  26. Tatton WG, Chalmers-Redman RME, Ju WJH. Mammen M, Carlile GW, Pong AW, Tatton NA. Propargylamines induce antiapoptotic new protein synthesis in serum- and nerve growth factor (NGF)-withdrawn, NGF-differentiated PC-12 cells. J Pharmacol Exp Ther 301: 753-764, 2002 https://doi.org/10.1124/jpet.301.2.753
  27. Tatton WG, Chalmers-Redman RME, Tatton NA. Neuroprotection by deprenyl and other propargylamines: glyceraldehydes-3-phosphate dehydrogenase rather than monoamine oxidase B. J Neural Transm 110: 509-515, 2003 https://doi.org/10.1007/s00702-002-0827-z
  28. Vaglini F, Pardini C, Cavalletti M, Maggio R, Corsini GU. L-deprenyl fails to protect mesencephalic dopamine neurons and PC12 cells from the neurotoxic effect of 1-methyl-4-phenylpyridinium ion. Brain Res 741: 68-74, 1996 https://doi.org/10.1016/S0006-8993(96)00898-0
  29. van Klaveren RJ, Hoet PH, Pype JL, Demedts M, Nemery B. Increase in gamma-glutamyltransferase by glutathione depletion in rat type II pneumocytes. Free Radic Biol Med 22: 525-534, 1997 https://doi.org/10.1016/S0891-5849(96)00375-9
  30. Wu RM, Chen RC, Chiueh CC. Effect of MAO-B inhibitors on $MPP^+$ toxicity in Vivo. Ann NY Acad Sci 899: 255-261, 2000 https://doi.org/10.1111/j.1749-6632.2000.tb06191.x
  31. Yi H, Akao Y, Maruyama W, Chen K, Shih J, Naoi M. Type A monoamine oxidase is the target of an endogenous dopaminergic neurotoxin, N-methyl(R)salsolinol, leading to apoptosis to apoptosis in SH-SY5Y cells. J Neurochem 96: 541-549, 2006 https://doi.org/10.1111/j.1471-4159.2005.03573.x