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Volumn 64, Issue 10, 2002, Pages 1503-1512

Cytotoxicity of dopamine-derived tetrahydroisoquinolines on melanoma cells

Author keywords

Cytotoxicity; Melanoma cells; Quinones; ROS; Tetrahydroisoquinolines

Indexed keywords

ACETYLCYSTEINE; ANTIOXIDANT; CATALASE; CATECHOL; DIHYDROLIPOAMIDE DEHYDROGENASE; DOPAMINE; ENZYME; MELANIN; MONOPHENOL MONOOXYGENASE; OXOGLUTARATE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE; SALSOLINOL; SUPEROXIDE DISMUTASE; TETRAHYDROISOQUINOLINE DERIVATIVE; TETRAHYDROPAPAVEROLINE;

EID: 0037112143     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(02)01353-9     Document Type: Article
Times cited : (23)

References (69)
  • 1
    • 0018852663 scopus 로고
    • Biogenic amine-aldehyde condensation products: Tetrahydropapaverolines and tryptolines
    • Dietrich R., Erwin V. Biogenic amine-aldehyde condensation products: tetrahydropapaverolines and tryptolines. Ann. Rev. Pharmacol. Toxicol. 20:1980;55-80.
    • (1980) Ann. Rev. Pharmacol. Toxicol. , vol.20 , pp. 55-80
    • Dietrich, R.1    Erwin, V.2
  • 3
    • 0023194188 scopus 로고
    • Presence of tetrahydroisoquinoline and 2-methyl tetrahydroisoquinoline in Parkinsonian and human brains
    • Niwa T., Takeda N., Kaneda N., Hashizume Y., Nagatsu T. Presence of tetrahydroisoquinoline and 2-methyl tetrahydroisoquinoline in Parkinsonian and human brains. Biochem. Biophys. Res. Commun. 144:1987;1084-1089.
    • (1987) Biochem. Biophys. Res. Commun. , vol.144 , pp. 1084-1089
    • Niwa, T.1    Takeda, N.2    Kaneda, N.3    Hashizume, Y.4    Nagatsu, T.5
  • 4
    • 0015892041 scopus 로고
    • Dopamine derived tetrahydroisoquinolines alkaloids inhibitors of neuroamine metabolism
    • Collins A.C., Cashaw J.L., Davis V.E. Dopamine derived tetrahydroisoquinolines alkaloids inhibitors of neuroamine metabolism. Biochem. Pharmacol. 22:1973;2337-2348.
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 2337-2348
    • Collins, A.C.1    Cashaw, J.L.2    Davis, V.E.3
  • 5
    • 0026635004 scopus 로고
    • Inhibition of tyrosine hydroxylase by R and S enantiomers of salsolinol, 1-methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline
    • Minami M., Takahashi T., Maruyama W., Takahashi A., Dostert P., Nagatsu T., Naoi M. Inhibition of tyrosine hydroxylase by R and S enantiomers of salsolinol, 1-methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline. J. Neurochem. 58:1992;2097-2101.
    • (1992) J. Neurochem. , vol.58 , pp. 2097-2101
    • Minami, M.1    Takahashi, T.2    Maruyama, W.3    Takahashi, A.4    Dostert, P.5    Nagatsu, T.6    Naoi, M.7
  • 6
    • 0027237536 scopus 로고
    • Inhibition of type A and B monoamine oxidase by 6,7-dihydroxy-1,2,3,4-tetrahydroisoquinolines and their N-methylated derivatives
    • Minami M., Maruyama W., Dostert P., Nagata T., Naoi M. Inhibition of type A and B monoamine oxidase by 6,7-dihydroxy-1,2,3,4-tetrahydroisoquinolines and their N-methylated derivatives. J. Neural. Transm. Gen. Sect. 92:1993;125-135.
    • (1993) J. Neural. Transm. Gen. Sect. , vol.92 , pp. 125-135
    • Minami, M.1    Maruyama, W.2    Dostert, P.3    Nagata, T.4    Naoi, M.5
  • 7
    • 0017227670 scopus 로고
    • In vivo and in vitro studies on the effect of tetrahydropapaveroline and salsolinol on COMT and MAO activity in rat brain
    • Giovine A., Renis M., Bertolino A. In vivo and in vitro studies on the effect of tetrahydropapaveroline and salsolinol on COMT and MAO activity in rat brain. Pharmacology. 14:1976;86-94.
    • (1976) Pharmacology , vol.14 , pp. 86-94
    • Giovine, A.1    Renis, M.2    Bertolino, A.3
  • 8
    • 0016701802 scopus 로고
    • 6,7-Dihydroxytetrahydroisoquinoline: Evidence for in vivo inhibition of intraneuronal monoamine oxidase
    • Cohen G., Katz S. 6,7-Dihydroxytetrahydroisoquinoline: evidence for in vivo inhibition of intraneuronal monoamine oxidase. J. Neurochem. 25:1975;719-722.
    • (1975) J. Neurochem. , vol.25 , pp. 719-722
    • Cohen, G.1    Katz, S.2
  • 10
    • 0029553763 scopus 로고
    • Production of melanin pigments by chemical and enzymatic oxidation of tetrahydroisoquinolines
    • Rosei M.A., Mosca L. Production of melanin pigments by chemical and enzymatic oxidation of tetrahydroisoquinolines. Biochem. Mol. Biol. Int. 35:1995;1253-1259.
    • (1995) Biochem. Mol. Biol. Int. , vol.35 , pp. 1253-1259
    • Rosei, M.A.1    Mosca, L.2
  • 12
    • 0031973737 scopus 로고    scopus 로고
    • Melanins from tetrahydroisoquinolines. Spectroscopic characteristics, scavenging activity and redox transfer properties
    • Mosca L., Blarzino C., Coccia R., Foppoli C., Rosei M.A. Melanins from tetrahydroisoquinolines. Spectroscopic characteristics, scavenging activity and redox transfer properties. Free Radic. Biol. Med. 24:1998;161-167.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 161-167
    • Mosca, L.1    Blarzino, C.2    Coccia, R.3    Foppoli, C.4    Rosei, M.A.5
  • 13
    • 0034915751 scopus 로고    scopus 로고
    • Opiomelanins synthesis and properties
    • Rosei M.A. Opiomelanins synthesis and properties. Histol. Histopathol. 16:2001;931-935.
    • (2001) Histol. Histopathol. , vol.16 , pp. 931-935
    • Rosei, M.A.1
  • 14
    • 0027322301 scopus 로고
    • Inhibitory effect of melanin precursors on arachidonic acid peroxidation
    • Napolitano A., Palumbo A., Misuraca G., Prota G. Inhibitory effect of melanin precursors on arachidonic acid peroxidation. Biochim. Biophys. Acta. 1168:1993;175-180.
    • (1993) Biochim. Biophys. Acta , vol.1168 , pp. 175-180
    • Napolitano, A.1    Palumbo, A.2    Misuraca, G.3    Prota, G.4
  • 16
    • 0017785767 scopus 로고
    • L-Dopa: Selective toxicity for melanoma cells in vitro
    • Wick M.M., Byers L., Frei E. L-Dopa: selective toxicity for melanoma cells in vitro. Science. 197:1977;468-469.
    • (1977) Science , vol.197 , pp. 468-469
    • Wick, M.M.1    Byers, L.2    Frei, E.3
  • 18
    • 0020621967 scopus 로고
    • The mechanism of toxicity of 5-S-cysteinyldopa to tumour cells. Hydrogen peroxide as a mediator of cytotoxicity
    • Ito S., Inoue S., Fujita K. The mechanism of toxicity of 5-S-cysteinyldopa to tumour cells. Hydrogen peroxide as a mediator of cytotoxicity. Biochem. Pharmacol. 32:1983;2079-2081.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 2079-2081
    • Ito, S.1    Inoue, S.2    Fujita, K.3
  • 19
    • 0018251759 scopus 로고
    • 5,6-Dihydroxyindole is a melanin precursor showing a potent cytotoxicity
    • Pawelek J.M., Lerner A.B. 5,6-Dihydroxyindole is a melanin precursor showing a potent cytotoxicity. Nature. 276:1978;627-628.
    • (1978) Nature , vol.276 , pp. 627-628
    • Pawelek, J.M.1    Lerner, A.B.2
  • 20
    • 0003904322 scopus 로고
    • San Diego: Harcourt Brace Jovanovich Publishers/Academic Press, Inc.
    • Prota G. Melanins and melanogenesis. San Diego: Harcourt Brace Jovanovich Publishers/Academic Press, Inc., 1992.
    • (1992) Melanins and Melanogenesis
    • Prota, G.1
  • 21
    • 0025082798 scopus 로고
    • Bioreductive activation of quinones: Redox properties and thiol reactivity
    • Wardman P. Bioreductive activation of quinones: redox properties and thiol reactivity. Free Radic. Res. Commun. 8:1990;219-229.
    • (1990) Free Radic. Res. Commun. , vol.8 , pp. 219-229
    • Wardman, P.1
  • 22
    • 0018095085 scopus 로고
    • Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones
    • Graham D.G. Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones. Mol. Pharmacol. 14:1978;633-643.
    • (1978) Mol. Pharmacol. , vol.14 , pp. 633-643
    • Graham, D.G.1
  • 24
    • 0019804120 scopus 로고
    • Toxic drug effects associated with oxygen metabolism: Redox cycling and lipid peroxidation
    • Kappus H., Sies H. Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation. Experientia. 37:1981;1233-1241.
    • (1981) Experientia , vol.37 , pp. 1233-1241
    • Kappus, H.1    Sies, H.2
  • 25
    • 0026072004 scopus 로고
    • Hydrogen peroxide as a mediator of dopac-induced effects on melanoma cells
    • Karg E., Rosengren E., Rorsman H. Hydrogen peroxide as a mediator of dopac-induced effects on melanoma cells. J. Invest. Dermatol. 96:1991;224-227.
    • (1991) J. Invest. Dermatol. , vol.96 , pp. 224-227
    • Karg, E.1    Rosengren, E.2    Rorsman, H.3
  • 26
    • 0023655409 scopus 로고
    • Comparative cytotoxicity of phenols in vitro
    • Passi S., Picardo M., Nazzaro-Porro M. Comparative cytotoxicity of phenols in vitro. Biochem. J. 245:1987;537-542.
    • (1987) Biochem. J. , vol.245 , pp. 537-542
    • Passi, S.1    Picardo, M.2    Nazzaro-Porro, M.3
  • 27
    • 0026049751 scopus 로고
    • Interferon inhibition of neoplastic phenotype in cell lines harbouring human papillomavirus sequences
    • De Marco F., Di Lonardo A., Venuti A., Marcante M.L. Interferon inhibition of neoplastic phenotype in cell lines harbouring human papillomavirus sequences. J. Biol. Regul. Homeost. Agents. 5:1991;65-70.
    • (1991) J. Biol. Regul. Homeost. Agents , vol.5 , pp. 65-70
    • De Marco, F.1    Di Lonardo, A.2    Venuti, A.3    Marcante, M.L.4
  • 28
    • 0023019005 scopus 로고
    • Use of MTT colorimetric assay to measure cell activation
    • Gerlier D., Thomasset N. Use of MTT colorimetric assay to measure cell activation. J. Immunol. Methods. 94:1986;5763-5769.
    • (1986) J. Immunol. Methods , vol.94 , pp. 5763-5769
    • Gerlier, D.1    Thomasset, N.2
  • 29
    • 77957000392 scopus 로고
    • DT-Diaphorase
    • Eastbrook RW, Pullman ME, editors. New York: Academic Press
    • Ernster L. DT-Diaphorase. In: Eastbrook RW, Pullman ME, editors. Methods in enzymology, vol. 10. New York: Academic Press, 1967. p. 309-17.
    • (1967) Methods in Enzymology , vol.10 , pp. 309-317
    • Ernster, L.1
  • 30
    • 0033048258 scopus 로고    scopus 로고
    • Metabolic impairment induces oxidative stress, compromises inflammatory responses, and inactivates a key mitochondrial enzyme in microglia
    • Park L.C., Zhang H., Sheu K.F., Calingasan N.Y., Kristal B.S., Lindsay J.G., Gibson G.E. Metabolic impairment induces oxidative stress, compromises inflammatory responses, and inactivates a key mitochondrial enzyme in microglia. J. Neurochem. 72:1999;1948-1958.
    • (1999) J. Neurochem. , vol.72 , pp. 1948-1958
    • Park, L.C.1    Zhang, H.2    Sheu, K.F.3    Calingasan, N.Y.4    Kristal, B.S.5    Lindsay, J.G.6    Gibson, G.E.7
  • 31
    • 0031896743 scopus 로고    scopus 로고
    • Thiamine deficiency decreases steady-state transketolase and piruvate dehydrogenase but not α-ketoglutarate dehydrogenase mRNA levels in three human cell types
    • Pekovich S.R., Martin P.R., Singleton C.K. Thiamine deficiency decreases steady-state transketolase and piruvate dehydrogenase but not α-ketoglutarate dehydrogenase mRNA levels in three human cell types. J. Nutr. 128:1998;683-687.
    • (1998) J. Nutr. , vol.128 , pp. 683-687
    • Pekovich, S.R.1    Martin, P.R.2    Singleton, C.K.3
  • 32
    • 0024201701 scopus 로고
    • Assays for mammalian tyrosinase: A comparative study
    • Jara J.R., Solano F., Lozano A.L. Assays for mammalian tyrosinase: a comparative study. Pigment Cell Res. 1:1988;332-339.
    • (1988) Pigment Cell Res. , vol.1 , pp. 332-339
    • Jara, J.R.1    Solano, F.2    Lozano, A.L.3
  • 33
    • 0025910929 scopus 로고
    • New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase
    • Winder A.J., Harris H. New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase. Eur. J. Biochem. 198:1991;317-326.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 317-326
    • Winder, A.J.1    Harris, H.2
  • 34
    • 0034726055 scopus 로고    scopus 로고
    • +-ATPase inhibitors in amelanotic, tyrosinase positive human and mouse melanoma cells
    • +-ATPase inhibitors in amelanotic, tyrosinase positive human and mouse melanoma cells. FEBS Lett. 478:2000;57-60.
    • (2000) FEBS Lett. , vol.478 , pp. 57-60
    • Ancans, J.1    Thody, A.J.2
  • 35
    • 0034047538 scopus 로고    scopus 로고
    • Limitations of the nested reverse transcriptase polymerase chain reaction on tyrosinase for the detection of malignant melanoma micrometastases in lymph nodes
    • Calogero A., Timmer-Bosscha H., Schrafford Koops H., Tiebosch A.T., Mulder N.H., Hospers G.A. Limitations of the nested reverse transcriptase polymerase chain reaction on tyrosinase for the detection of malignant melanoma micrometastases in lymph nodes. Br. J. Cancer. 83:2000;184-187.
    • (2000) Br. J. Cancer , vol.83 , pp. 184-187
    • Calogero, A.1    Timmer-Bosscha, H.2    Schrafford Koops, H.3    Tiebosch, A.T.4    Mulder, N.H.5    Hospers, G.A.6
  • 36
    • 0034126478 scopus 로고    scopus 로고
    • Detection of circulating melanoma cells by RT-PCR amplification of three different melanocyte-specific mRNAs in a mouse model
    • Tsukamoto K., Hirata S., Osada A., Kitamura R., Shimada S. Detection of circulating melanoma cells by RT-PCR amplification of three different melanocyte-specific mRNAs in a mouse model. Pigment Cell Res. 13:2000;185-189.
    • (2000) Pigment Cell Res. , vol.13 , pp. 185-189
    • Tsukamoto, K.1    Hirata, S.2    Osada, A.3    Kitamura, R.4    Shimada, S.5
  • 37
    • 0035861652 scopus 로고    scopus 로고
    • Down-modulation of type 1 interferon responses by receptor cross-competition for a shared JAK kinase
    • Dondi E., Pattyn E., Lutfalla G., Van Ostade X., Uze G., Pellegrini S., Tavernier J. Down-modulation of type 1 interferon responses by receptor cross-competition for a shared JAK kinase. J. Biol. Chem. 276:2001;47004-47012.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47004-47012
    • Dondi, E.1    Pattyn, E.2    Lutfalla, G.3    Van Ostade, X.4    Uze, G.5    Pellegrini, S.6    Tavernier, J.7
  • 38
    • 0011404008 scopus 로고
    • DT-Diaphorase: Its structure, function, regulation and its role in antioxidant defence and cancer chemotherapy
    • Yagi K, editor. Tokyo, Japan: Sc Sco Press
    • Ernster L. DT-Diaphorase: its structure, function, regulation and its role in antioxidant defence and cancer chemotherapy. In: Yagi K, editor. Pathophysiology of lipid peroxides and related free radicals. Tokyo, Japan: Sc Sco Press, 1967. p. 1-24.
    • (1967) Pathophysiology of Lipid Peroxides and Related Free Radicals , pp. 1-24
    • Ernster, L.1
  • 40
    • 0028918334 scopus 로고
    • Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
    • Burdon R.H. Superoxide and hydrogen peroxide in relation to mammalian cell proliferation. Free Radic. Biol. Med. 18:1995;775-794.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 775-794
    • Burdon, R.H.1
  • 41
    • 0029019124 scopus 로고
    • N-Methyl salsolinol produces hydroxyl radicals: Involvement to neurotoxicity
    • Maruyama W., Dostert P., Matsubara K., Naoi M. N-Methyl salsolinol produces hydroxyl radicals: involvement to neurotoxicity. Free Radic. Biol. Med. 19:1995;67-75.
    • (1995) Free Radic. Biol. Med. , vol.19 , pp. 67-75
    • Maruyama, W.1    Dostert, P.2    Matsubara, K.3    Naoi, M.4
  • 42
    • 0028988538 scopus 로고
    • Dopamine-derived 1-methyl-6,7-dihydroxyisoquinolines as hydroxyl radical promoters and scavengers in rat brain: In vivo and in vitro studies
    • Maruyama W., Dostert P., Naoi M. Dopamine-derived 1-methyl-6,7-dihydroxyisoquinolines as hydroxyl radical promoters and scavengers in rat brain: in vivo and in vitro studies. J. Neurochem. 64:1995;2635-2643.
    • (1995) J. Neurochem. , vol.64 , pp. 2635-2643
    • Maruyama, W.1    Dostert, P.2    Naoi, M.3
  • 43
    • 0032710672 scopus 로고    scopus 로고
    • Contrasting effects of catecholic and O-methylated tetrahydroisoquinolines on hydroxyl radical production
    • Nappi A.J., Vass E., Collins M.A. Contrasting effects of catecholic and O-methylated tetrahydroisoquinolines on hydroxyl radical production. Biochim. Biophys. Acta. 1434:1999;64-73.
    • (1999) Biochim. Biophys. Acta , vol.1434 , pp. 64-73
    • Nappi, A.J.1    Vass, E.2    Collins, M.A.3
  • 44
    • 0028834192 scopus 로고
    • L-Dopa cytotoxicity to PC12 cells in culture is via its autoxidation
    • Basma A.N., Morris E.J., Nicklas W.J., Geller H.M. L-Dopa cytotoxicity to PC12 cells in culture is via its autoxidation. J. Neurochem. 64:1995;825-832.
    • (1995) J. Neurochem. , vol.64 , pp. 825-832
    • Basma, A.N.1    Morris, E.J.2    Nicklas, W.J.3    Geller, H.M.4
  • 45
    • 0030758614 scopus 로고    scopus 로고
    • Comparative studies of enhanced iron-mediated production of hydroxyl radical by glutathione, cysteine, ascorbic acid, and selected catechols
    • Nappi A.J., Vass E. Comparative studies of enhanced iron-mediated production of hydroxyl radical by glutathione, cysteine, ascorbic acid, and selected catechols. Biochim. Biophys. Acta. 1336:1997;295-302.
    • (1997) Biochim. Biophys. Acta , vol.1336 , pp. 295-302
    • Nappi, A.J.1    Vass, E.2
  • 46
    • 0035877035 scopus 로고    scopus 로고
    • Oxidative DNA damage and cytotoxicity induced by copper-stimulated redox cycling of salsolinol, a neurotoxic tetrahydroisoquinoline alkaloid
    • Jung Y., Surh Y. Oxidative DNA damage and cytotoxicity induced by copper-stimulated redox cycling of salsolinol, a neurotoxic tetrahydroisoquinoline alkaloid. Free Radic. Biol. Med. 30:2001;1407-1417.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1407-1417
    • Jung, Y.1    Surh, Y.2
  • 47
    • 0025110602 scopus 로고
    • Alteration of glutathione level in human melanoma cells: Effect of N-acetyl-L-cysteine and its analogues
    • Karg E., Tunek A., Brotell H., Rosengren E., Rorsman H. Alteration of glutathione level in human melanoma cells: effect of N-acetyl-L-cysteine and its analogues. Pigment Cell Res. 3:1990;11-15.
    • (1990) Pigment Cell Res. , vol.3 , pp. 11-15
    • Karg, E.1    Tunek, A.2    Brotell, H.3    Rosengren, E.4    Rorsman, H.5
  • 48
    • 0028215392 scopus 로고
    • Effects of L-cysteine on the oxidation chemistry of dopamine: New reaction pathways of potential relevance to idiopathic Parkinson's disease
    • Zhang F., Dryhurst G. Effects of L-cysteine on the oxidation chemistry of dopamine: new reaction pathways of potential relevance to idiopathic Parkinson's disease. J. Med. Chem. 37:1994;1084-1098.
    • (1994) J. Med. Chem. , vol.37 , pp. 1084-1098
    • Zhang, F.1    Dryhurst, G.2
  • 50
    • 0023914114 scopus 로고
    • Positive regulation of melanin pigmentation by two key substrates of the melanogenic pathway, L-tyrosine and L-dopa
    • Slominski A., Moellmann G., Kuklinska E., Bomirski A., Pawelek J. Positive regulation of melanin pigmentation by two key substrates of the melanogenic pathway, L-tyrosine and L-dopa. J. Cell Sci. 89:1988;287-296.
    • (1988) J. Cell Sci. , vol.89 , pp. 287-296
    • Slominski, A.1    Moellmann, G.2    Kuklinska, E.3    Bomirski, A.4    Pawelek, J.5
  • 51
    • 0026015177 scopus 로고
    • Pigment content of cultured human melanocytes does not correlate with tyrosinase message level
    • Naeyaert J.M., Eller M., Gordon P.R., Park H.Y., Gilchrest B.A. Pigment content of cultured human melanocytes does not correlate with tyrosinase message level. Br. J. Dermatol. 125:1991;297-303.
    • (1991) Br. J. Dermatol. , vol.125 , pp. 297-303
    • Naeyaert, J.M.1    Eller, M.2    Gordon, P.R.3    Park, H.Y.4    Gilchrest, B.A.5
  • 52
    • 0034047660 scopus 로고    scopus 로고
    • Downregulation of tyrosinase activity in human melanocyte cell cultures by yohimbine
    • Fuller B.B., Drake M.A., Spaulding D.T., Chaudhry F. Downregulation of tyrosinase activity in human melanocyte cell cultures by yohimbine. J. Invest. Dermatol. 114:2000;268-276.
    • (2000) J. Invest. Dermatol. , vol.114 , pp. 268-276
    • Fuller, B.B.1    Drake, M.A.2    Spaulding, D.T.3    Chaudhry, F.4
  • 53
    • 0025807858 scopus 로고
    • Studies on the reactions between human tyrosinase, superoxide anion, hydrogen peroxide and thiols
    • Wood J.M., Schallreuter K.U. Studies on the reactions between human tyrosinase, superoxide anion, hydrogen peroxide and thiols. Biochim. Biophys. Acta. 1074:1991;378-385.
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 378-385
    • Wood, J.M.1    Schallreuter, K.U.2
  • 54
    • 0029805691 scopus 로고    scopus 로고
    • Tyrosinase may protect human melanocytes from the cytotoxic effects of the superoxide anion
    • Valverde P., Manning P., Todd C., McNeil C.J., Thody A.J. Tyrosinase may protect human melanocytes from the cytotoxic effects of the superoxide anion. Exp. Dermatol. 5:1996;247-253.
    • (1996) Exp. Dermatol. , vol.5 , pp. 247-253
    • Valverde, P.1    Manning, P.2    Todd, C.3    McNeil, C.J.4    Thody, A.J.5
  • 55
    • 0030115075 scopus 로고    scopus 로고
    • Activation of tyrosinase reduces the cytotoxic effects of the superoxide anion in B16 mouse melanoma cells
    • Valverde P., Manning P., McNeil C.J., Thody A.J. Activation of tyrosinase reduces the cytotoxic effects of the superoxide anion in B16 mouse melanoma cells. Pigment Cell Res. 9:1996;77-84.
    • (1996) Pigment Cell Res. , vol.9 , pp. 77-84
    • Valverde, P.1    Manning, P.2    McNeil, C.J.3    Thody, A.J.4
  • 56
    • 0028989810 scopus 로고
    • Inhibition of alpha-ketoglutarate dehydrogenase by isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine (MPTP)
    • McNaught K.S., Altomare C., Cellamare S., Carotti A., Thull U., Carrupt P.A., Testa B., Jenner P., Marsden C.D. Inhibition of alpha-ketoglutarate dehydrogenase by isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine (MPTP). Neuroreport. 6:1995;1105-1108.
    • (1995) Neuroreport , vol.6 , pp. 1105-1108
    • McNaught, K.S.1    Altomare, C.2    Cellamare, S.3    Carotti, A.4    Thull, U.5    Carrupt, P.A.6    Testa, B.7    Jenner, P.8    Marsden, C.D.9
  • 57
    • 0028857498 scopus 로고
    • L-Dopa inhibits complex IV of the electron transport chain in catecholamine-rich human neuroblastoma NB69 cells
    • Pardo B., Mena M.A., de Yebenes J.G. L-Dopa inhibits complex IV of the electron transport chain in catecholamine-rich human neuroblastoma NB69 cells. J. Neurochem. 64:1995;576-582.
    • (1995) J. Neurochem. , vol.64 , pp. 576-582
    • Pardo, B.1    Mena, M.A.2    De Yebenes, J.G.3
  • 59
    • 0033958942 scopus 로고    scopus 로고
    • 1-Methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline (salsolinol) is toxic to dopaminergic neuroblastoma SH-SY5Y cells via impairment of cellular energy metabolism
    • Storch A., Kaftan A., Burkhardt K., Schwarz J. 1-Methyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline (salsolinol) is toxic to dopaminergic neuroblastoma SH-SY5Y cells via impairment of cellular energy metabolism. Brain Res. 855:2000;67-75.
    • (2000) Brain Res. , vol.855 , pp. 67-75
    • Storch, A.1    Kaftan, A.2    Burkhardt, K.3    Schwarz, J.4
  • 60
    • 0030840624 scopus 로고    scopus 로고
    • Isoquinoline neurotoxins in the brain and Parkinson's disease
    • Nagatsu T. Isoquinoline neurotoxins in the brain and Parkinson's disease. Neurosci. Res. 29:1997;99-111.
    • (1997) Neurosci. Res. , vol.29 , pp. 99-111
    • Nagatsu, T.1
  • 61
    • 0016599714 scopus 로고
    • Biosynthesis of tetrahydroisoquinoline alkaloids in brain and other tissues of ethanol-intoxicated rats
    • Collins M.A., Bidgeli M.G. Biosynthesis of tetrahydroisoquinoline alkaloids in brain and other tissues of ethanol-intoxicated rats. Adv. Exp. Med. Biol. 59:1975;79-91.
    • (1975) Adv. Exp. Med. Biol. , vol.59 , pp. 79-91
    • Collins, M.A.1    Bidgeli, M.G.2
  • 62
    • 0023690768 scopus 로고
    • Dopamine-derived alkaloids in alcoholism and in Parkinson's and Huntington's diseases
    • Dostert P., Strolin Benedetti M., Dordain G. Dopamine-derived alkaloids in alcoholism and in Parkinson's and Huntington's diseases. J. Neural. Transm. 74:1988;61-74.
    • (1988) J. Neural. Transm. , vol.74 , pp. 61-74
    • Dostert, P.1    Strolin Benedetti, M.2    Dordain, G.3
  • 64
    • 0020024217 scopus 로고
    • Salsolinol and catecholamines in human brain and their relation to alcoholism
    • Sjoquist B., Eriksson A., Winblad B. Salsolinol and catecholamines in human brain and their relation to alcoholism. Prog. Clin. Biol. Res. 90:1982;57-67.
    • (1982) Prog. Clin. Biol. Res. , vol.90 , pp. 57-67
    • Sjoquist, B.1    Eriksson, A.2    Winblad, B.3
  • 65
    • 0034666297 scopus 로고    scopus 로고
    • Dopaminergic neurotoxins 6,7-dihydroxy-1-(3′,4′-dihydroxybenzyl)-isoquinolines, cause different types of cell death in SH-SY5Y cells: Apoptosis was induced by oxidized papaverolines and necrosis by reduced tetrahydropapaverolines
    • Maruyama W., Sango K., Iwasa K., Minami C., Dostert P., Kawai M., Moriyasu M., Naoi M. Dopaminergic neurotoxins 6,7-dihydroxy-1-(3′,4′-dihydroxybenzyl)-isoquinolines, cause different types of cell death in SH-SY5Y cells: apoptosis was induced by oxidized papaverolines and necrosis by reduced tetrahydropapaverolines. Neurosci. Lett. 291:2000;89-92.
    • (2000) Neurosci. Lett. , vol.291 , pp. 89-92
    • Maruyama, W.1    Sango, K.2    Iwasa, K.3    Minami, C.4    Dostert, P.5    Kawai, M.6    Moriyasu, M.7    Naoi, M.8
  • 68
    • 0032504657 scopus 로고    scopus 로고
    • Role of mitochondria in oxidative stress ad ageing
    • Lenaz G. Role of mitochondria in oxidative stress ad ageing. Biochim. Biophys. Acta. 1366:1998;53-67.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 53-67
    • Lenaz, G.1
  • 69
    • 0028032254 scopus 로고
    • Different prooxidant levels stimulate growth, trigger apoptosis, or produce necrosis of insulin-secreting RINm5F cells. The role of intracellular polyamines
    • Dypbukt J.M., Ankarcrona M., Burkitt M., Sjoholm A., Strom K., Orrenius S., Nicotera P. Different prooxidant levels stimulate growth, trigger apoptosis, or produce necrosis of insulin-secreting RINm5F cells. The role of intracellular polyamines. J. Biol. Chem. 269:1994;30553-30560.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30553-30560
    • Dypbukt, J.M.1    Ankarcrona, M.2    Burkitt, M.3    Sjoholm, A.4    Strom, K.5    Orrenius, S.6    Nicotera, P.7


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