메뉴 건너뛰기




Volumn 90, Issue 1, 2013, Pages 35-42

Ascorbic acid efficiently enhances neuronal synthesis of norepinephrine from dopamine

Author keywords

Dopamine; Dopamine hydroxylase; Norepinephrine; Oxidative stress; SH SY5Y neuroblastoma cells

Indexed keywords

ASCORBIC ACID; DOPAMINE; DOPAMINE BETA MONOOXYGENASE; NORADRENALIN; SUPEROXIDE;

EID: 84870525092     PISSN: 03619230     EISSN: 18732747     Source Type: Journal    
DOI: 10.1016/j.brainresbull.2012.09.009     Document Type: Article
Times cited : (58)

References (49)
  • 1
    • 33645802571 scopus 로고    scopus 로고
    • Identification of a novel regulatory mechanism for norepinephrine transporter activity by the IP3 receptor
    • Amano T., Aoki S., Setsuie R., Sakurai M., Wada K., Noda M. Identification of a novel regulatory mechanism for norepinephrine transporter activity by the IP3 receptor. European Journal of Pharmacology 2006, 536:62-68.
    • (2006) European Journal of Pharmacology , vol.536 , pp. 62-68
    • Amano, T.1    Aoki, S.2    Setsuie, R.3    Sakurai, M.4    Wada, K.5    Noda, M.6
  • 2
    • 0013925243 scopus 로고
    • A quantitative study on the nigro-neostriatal dopamine neuron system in the rat
    • Anden N.E., Hfuxe K., Hamberger B., Hokfelt T. A quantitative study on the nigro-neostriatal dopamine neuron system in the rat. Acta Physiologica Scandinavica 1966, 67:306-312.
    • (1966) Acta Physiologica Scandinavica , vol.67 , pp. 306-312
    • Anden, N.E.1    Hfuxe, K.2    Hamberger, B.3    Hokfelt, T.4
  • 3
    • 0023188570 scopus 로고
    • Monoamine oxidase, hydrogen peroxide, and Parkinson's disease
    • Cohen G. Monoamine oxidase, hydrogen peroxide, and Parkinson's disease. Advances in Neurology 1987, 45:119-125.
    • (1987) Advances in Neurology , vol.45 , pp. 119-125
    • Cohen, G.1
  • 4
    • 0024423253 scopus 로고
    • Ascorbic acid within chromaffin granules. In situ kinetics of norepinephrine biosynthesis
    • Dhariwal K.R., Washko P., Hartzell W.O., Levine M. Ascorbic acid within chromaffin granules. In situ kinetics of norepinephrine biosynthesis. Journal of Biological Chemistry 1989, 264:15404-15409.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 15404-15409
    • Dhariwal, K.R.1    Washko, P.2    Hartzell, W.O.3    Levine, M.4
  • 7
  • 10
    • 39149111608 scopus 로고    scopus 로고
    • Inhibition of vesicular monoamine transporter-2 activity in alpha-synuclein stably transfected SH-SY5Y cells
    • Guo J.T., Chen A.Q., Kong Q., Zhu H., Ma C.M., Qin C. Inhibition of vesicular monoamine transporter-2 activity in alpha-synuclein stably transfected SH-SY5Y cells. Cellular and Molecular Neurobiology 2008, 28:35-47.
    • (2008) Cellular and Molecular Neurobiology , vol.28 , pp. 35-47
    • Guo, J.T.1    Chen, A.Q.2    Kong, Q.3    Zhu, H.4    Ma, C.M.5    Qin, C.6
  • 11
    • 60449102448 scopus 로고    scopus 로고
    • Vitamin C function in the brain: vital role of the ascorbate transporter (SVCT2)
    • Harrison F.E., May J.M. Vitamin C function in the brain: vital role of the ascorbate transporter (SVCT2). Free Radical Biology and Medicine 2009, 45:719-730.
    • (2009) Free Radical Biology and Medicine , vol.45 , pp. 719-730
    • Harrison, F.E.1    May, J.M.2
  • 12
    • 0017064979 scopus 로고
    • A fluorometric method for determination of oxidized and reduced glutathione in tissues
    • Hissin P.J., Hilf R. A fluorometric method for determination of oxidized and reduced glutathione in tissues. Analytical Biochemistry 1976, 74:214-226.
    • (1976) Analytical Biochemistry , vol.74 , pp. 214-226
    • Hissin, P.J.1    Hilf, R.2
  • 13
    • 0032476697 scopus 로고    scopus 로고
    • Ascorbate prevents the interaction of superoxide and nitric oxide only at very high physiological concentrations
    • Jackson T.S., Xu A.M., Vita J.A., Keaney J.F. Ascorbate prevents the interaction of superoxide and nitric oxide only at very high physiological concentrations. Circulation Research 1998, 83:916-922.
    • (1998) Circulation Research , vol.83 , pp. 916-922
    • Jackson, T.S.1    Xu, A.M.2    Vita, J.A.3    Keaney, J.F.4
  • 14
    • 52249094382 scopus 로고    scopus 로고
    • Extracellular dopamine induces the oxidative toxicity of SH-SY5Y cells
    • Jiang Y., Pei L., Li S., Wang M., Liu F. Extracellular dopamine induces the oxidative toxicity of SH-SY5Y cells. Synapse 2008, 62:797-803.
    • (2008) Synapse , vol.62 , pp. 797-803
    • Jiang, Y.1    Pei, L.2    Li, S.3    Wang, M.4    Liu, F.5
  • 16
    • 0031042677 scopus 로고    scopus 로고
    • 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
    • Lai C.T., Yu P.H. 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. Biochemical Pharmacology 1997, 53:363-372.
    • (1997) Biochemical Pharmacology , vol.53 , pp. 363-372
    • Lai, C.T.1    Yu, P.H.2
  • 17
    • 0001602130 scopus 로고
    • Studies on the enzyme catalyzing the conversion of 3,4-dihydroxyphenylethylamine to norepinephrine
    • Levin E.Y., Kaufman S. Studies on the enzyme catalyzing the conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. Journal of Biological Chemistry 1961, 236:2043-2049.
    • (1961) Journal of Biological Chemistry , vol.236 , pp. 2043-2049
    • Levin, E.Y.1    Kaufman, S.2
  • 18
    • 0001136504 scopus 로고
    • The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine
    • Levin E.Y., Levenberg B., Kaufman S. The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. Journal of Biological Chemistry 1960, 235:2080-2086.
    • (1960) Journal of Biological Chemistry , vol.235 , pp. 2080-2086
    • Levin, E.Y.1    Levenberg, B.2    Kaufman, S.3
  • 19
    • 0022916814 scopus 로고
    • Ascorbic acid specifically enhances dopamine beta-monooxygenase activity in resting and stimulated chromaffin cells
    • Levine M. Ascorbic acid specifically enhances dopamine beta-monooxygenase activity in resting and stimulated chromaffin cells. Journal of Biological Chemistry 1986, 261:7347-7356.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 7347-7356
    • Levine, M.1
  • 20
    • 0022350362 scopus 로고
    • Enhancement of norepinephrine biosynthesis by ascorbic acid in cultured bovine chromaffin cells
    • Levine M., Morita K., Pollard H. Enhancement of norepinephrine biosynthesis by ascorbic acid in cultured bovine chromaffin cells. Journal of Biological Chemistry 1985, 260:12942-12947.
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 12942-12947
    • Levine, M.1    Morita, K.2    Pollard, H.3
  • 21
    • 0038578532 scopus 로고    scopus 로고
    • Ascorbic acid spares alpha-tocopherol and decreases lipid peroxidation in neuronal cells
    • Li X., Huang J., May J.M. Ascorbic acid spares alpha-tocopherol and decreases lipid peroxidation in neuronal cells. Biochemical and Biophysical Research Communications 2003, 305:656-661.
    • (2003) Biochemical and Biophysical Research Communications , vol.305 , pp. 656-661
    • Li, X.1    Huang, J.2    May, J.M.3
  • 23
    • 0029031835 scopus 로고
    • Reverse transcriptase-polymerase chain reaction (RT-PCR) analysis of monoamine transporters in neuroblastoma cell lines: correlations to meta-iodobenzylguanidine (MIBG) uptake and tyrosine hydroxylase gene expression
    • Lode H.N., Bruchelt G., Seitz G., Gebhardt S., Gekeler V., Niethammer D., Beck J. Reverse transcriptase-polymerase chain reaction (RT-PCR) analysis of monoamine transporters in neuroblastoma cell lines: correlations to meta-iodobenzylguanidine (MIBG) uptake and tyrosine hydroxylase gene expression. European Journal of Cancer 1995, 31A:586-590.
    • (1995) European Journal of Cancer , vol.31 A , pp. 586-590
    • Lode, H.N.1    Bruchelt, G.2    Seitz, G.3    Gebhardt, S.4    Gekeler, V.5    Niethammer, D.6    Beck, J.7
  • 25
    • 0029968464 scopus 로고    scopus 로고
    • The TiPS/TINS lecture. catecholamines: from gene regulation to neuropsychiatric disorders
    • Mallet J. The TiPS/TINS lecture. catecholamines: from gene regulation to neuropsychiatric disorders. Trends in Neurosciences 1996, 19:191-196.
    • (1996) Trends in Neurosciences , vol.19 , pp. 191-196
    • Mallet, J.1
  • 26
    • 0032518172 scopus 로고    scopus 로고
    • Protection and recycling of a-tocopherol in human erythrocytes by intracellular ascorbic acid
    • May J.M., Qu Z.-C., Mendiratta S. Protection and recycling of a-tocopherol in human erythrocytes by intracellular ascorbic acid. Archives of Biochemistry and Biophysics 1998, 349:281-289.
    • (1998) Archives of Biochemistry and Biophysics , vol.349 , pp. 281-289
    • May, J.M.1    Qu, Z.-C.2    Mendiratta, S.3
  • 27
    • 33746383473 scopus 로고    scopus 로고
    • Ascorbate transport and recycling by SH-SY5Y neuroblastoma cells: Response to glutamate toxicity
    • May J.M., Li L., Hayslett K., Qu Z.C. Ascorbate transport and recycling by SH-SY5Y neuroblastoma cells: Response to glutamate toxicity. Neurochemical Research 2006, 31:785-794.
    • (2006) Neurochemical Research , vol.31 , pp. 785-794
    • May, J.M.1    Li, L.2    Hayslett, K.3    Qu, Z.C.4
  • 28
    • 0022972685 scopus 로고
    • Role of ascorbic acid in dopamine beta-hydroxylation. The endogenous enzyme cofactor and putative electron donor for cofactor regeneration
    • Menniti F.S., Knoth J., Diliberto E.J. Role of ascorbic acid in dopamine beta-hydroxylation. The endogenous enzyme cofactor and putative electron donor for cofactor regeneration. Journal of Biological Chemistry 1986, 261:16901-16908.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 16901-16908
    • Menniti, F.S.1    Knoth, J.2    Diliberto, E.J.3
  • 29
    • 0023217527 scopus 로고
    • The in situ kinetics of dopamine beta-hydroxylase in bovine adrenomedullary chromaffin cells. Intravesicular compartmentation reduces apparent affinity for the cofactor ascorbate
    • Menniti F.S., Knoth J., Peterson D.S., Diliberto E.J. The in situ kinetics of dopamine beta-hydroxylase in bovine adrenomedullary chromaffin cells. Intravesicular compartmentation reduces apparent affinity for the cofactor ascorbate. Journal of Biological Chemistry 1987, 262:7651-7657.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 7651-7657
    • Menniti, F.S.1    Knoth, J.2    Peterson, D.S.3    Diliberto, E.J.4
  • 30
    • 84870520475 scopus 로고    scopus 로고
    • Rapid and specific measurements of superoxide using fluorescence spectroscopy
    • Nazarewicz R., Bikineyeva A., Harrison D.G., Dikalov S. Rapid and specific measurements of superoxide using fluorescence spectroscopy. FASEB Journal 2012, 26:578.3.
    • (2012) FASEB Journal , vol.26
    • Nazarewicz, R.1    Bikineyeva, A.2    Harrison, D.G.3    Dikalov, S.4
  • 31
    • 0026040772 scopus 로고
    • Multiple forms of human dopamine beta-hydroxylase in SH-SY5Y neuroblastoma cells
    • Oyarce A.M., Fleming P.J. Multiple forms of human dopamine beta-hydroxylase in SH-SY5Y neuroblastoma cells. Archives of Biochemistry and Biophysics 1991, 290:503-510.
    • (1991) Archives of Biochemistry and Biophysics , vol.290 , pp. 503-510
    • Oyarce, A.M.1    Fleming, P.J.2
  • 32
    • 0027268723 scopus 로고
    • Ascorbic acid protects against levodopa-induced neurotoxicity on a catecholamine-rich human neuroblastoma cell line
    • Pardo B., Mena M.A., Fahn S., Garcia de Y.J. Ascorbic acid protects against levodopa-induced neurotoxicity on a catecholamine-rich human neuroblastoma cell line. Movement Disorders 1993, 8:278-284.
    • (1993) Movement Disorders , vol.8 , pp. 278-284
    • Pardo, B.1    Mena, M.A.2    Fahn, S.3    Garcia de, Y.J.4
  • 33
    • 34147223962 scopus 로고    scopus 로고
    • Ascorbate transport by primary cultured neurons and its role in neuronal function and protection against excitotoxicity
    • Qiu S., Li L., Weeber E.J., May J.M. Ascorbate transport by primary cultured neurons and its role in neuronal function and protection against excitotoxicity. Journal of Neuroscience Research 2007, 85:1046-1056.
    • (2007) Journal of Neuroscience Research , vol.85 , pp. 1046-1056
    • Qiu, S.1    Li, L.2    Weeber, E.J.3    May, J.M.4
  • 34
    • 0028142763 scopus 로고
    • A vitamin as neuromodulator: ascorbate release into the extracellular fluid of the brain regulates dopaminergic and glutamatergic transmission
    • Rebec G.V., Pierce R.C. A vitamin as neuromodulator: ascorbate release into the extracellular fluid of the brain regulates dopaminergic and glutamatergic transmission. Progress in Neurobiology 1994, 43:537-565.
    • (1994) Progress in Neurobiology , vol.43 , pp. 537-565
    • Rebec, G.V.1    Pierce, R.C.2
  • 35
    • 0027279397 scopus 로고
    • Ascorbate concentration in human cerebrospinal fluid (CSF) and serum. Intrathecal accumulation and CSF flow rate
    • Reiber H., Ruff M., Uhr M. Ascorbate concentration in human cerebrospinal fluid (CSF) and serum. Intrathecal accumulation and CSF flow rate. Clinica Chimica Acta 1993, 217:163-173.
    • (1993) Clinica Chimica Acta , vol.217 , pp. 163-173
    • Reiber, H.1    Ruff, M.2    Uhr, M.3
  • 36
    • 0022524575 scopus 로고
    • Human neuroblastoma cell lines as models of catechol uptake
    • Richards M.L., Sadee W. Human neuroblastoma cell lines as models of catechol uptake. Brain Research 1986, 384:132-137.
    • (1986) Brain Research , vol.384 , pp. 132-137
    • Richards, M.L.1    Sadee, W.2
  • 38
    • 0032489542 scopus 로고    scopus 로고
    • Ascorbic acid stimulates DOPA synthesis and tyrosine hydroxylase gene expression in the human neuroblastoma cell line SK-N-SH
    • Seitz G., Gebhardt S., Beck J.F., Bohm W., Lode H.N., Niethammer D., Bruchelt G. Ascorbic acid stimulates DOPA synthesis and tyrosine hydroxylase gene expression in the human neuroblastoma cell line SK-N-SH. Neuroscience Letters 1998, 244:33-36.
    • (1998) Neuroscience Letters , vol.244 , pp. 33-36
    • Seitz, G.1    Gebhardt, S.2    Beck, J.F.3    Bohm, W.4    Lode, H.N.5    Niethammer, D.6    Bruchelt, G.7
  • 40
    • 0029761452 scopus 로고    scopus 로고
    • Dopamine-induced apoptosis in human neuronal cells: inhibition by nucleic acids antisense to the dopamine transporter
    • Simantov R., Blinder E., Ratovitski T., Tauber M., Gabbay M., Porat S. Dopamine-induced apoptosis in human neuronal cells: inhibition by nucleic acids antisense to the dopamine transporter. Neuroscience 1996, 74:39-50.
    • (1996) Neuroscience , vol.74 , pp. 39-50
    • Simantov, R.1    Blinder, E.2    Ratovitski, T.3    Tauber, M.4    Gabbay, M.5    Porat, S.6
  • 42
    • 0023664896 scopus 로고
    • Characterization of alternate reductant binding and electron transfer in the dopamine beta-monooxygenase reaction
    • Stewart L.C., Klinman J.P. Characterization of alternate reductant binding and electron transfer in the dopamine beta-monooxygenase reaction. Biochemistry 1987, 26:5302-5309.
    • (1987) Biochemistry , vol.26 , pp. 5302-5309
    • Stewart, L.C.1    Klinman, J.P.2
  • 43
    • 0025955430 scopus 로고
    • Cooperativity in the dopamine beta-monooxygenase reaction. Evidence for ascorbate regulation of enzyme activity
    • Stewart L.C., Klinman J.P. Cooperativity in the dopamine beta-monooxygenase reaction. Evidence for ascorbate regulation of enzyme activity. Journal of Biological Chemistry 1991, 266:11537-11543.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 11537-11543
    • Stewart, L.C.1    Klinman, J.P.2
  • 44
    • 0015591248 scopus 로고
    • The effect of l-ascorbate on catecholamine biosynthesis
    • Stone K.J., Townsley B.H. The effect of l-ascorbate on catecholamine biosynthesis. Biochemical Journal 1973, 131:611-613.
    • (1973) Biochemical Journal , vol.131 , pp. 611-613
    • Stone, K.J.1    Townsley, B.H.2
  • 45
    • 0001906829 scopus 로고
    • Dehydroascorbic acid
    • American Chemical Society, Washington, DC, P.A. Seib, B.M. Tolbert (Eds.)
    • Tolbert B.M., Ward J.B. Dehydroascorbic acid. Ascorbic Acid: Chemistry, Metabolism, and Uses 1982, 101-123. American Chemical Society, Washington, DC. P.A. Seib, B.M. Tolbert (Eds.).
    • (1982) Ascorbic Acid: Chemistry, Metabolism, and Uses , pp. 101-123
    • Tolbert, B.M.1    Ward, J.B.2
  • 46
    • 0018395103 scopus 로고
    • The uptake of ascorbic acid and dehydroascorbic acid by chromaffin granules of the adrenal medulla
    • Tirrell J.G., Westhead E.W. The uptake of ascorbic acid and dehydroascorbic acid by chromaffin granules of the adrenal medulla. Neuroscience 1979, 4:181-186.
    • (1979) Neuroscience , vol.4 , pp. 181-186
    • Tirrell, J.G.1    Westhead, E.W.2
  • 47
    • 23944482400 scopus 로고    scopus 로고
    • Regulation of vitamin C transport
    • Wilson J.X. Regulation of vitamin C transport. Annual Review of Nutrition 2005, 25:105-125.
    • (2005) Annual Review of Nutrition , vol.25 , pp. 105-125
    • Wilson, J.X.1
  • 48
    • 79959573043 scopus 로고    scopus 로고
    • Vesicular monoamine transporters: structure-function, pharmacology, and medicinal chemistry
    • Wimalasena K. Vesicular monoamine transporters: structure-function, pharmacology, and medicinal chemistry. Medicinal Research Reviews 2011, 31:483-519.
    • (2011) Medicinal Research Reviews , vol.31 , pp. 483-519
    • Wimalasena, K.1
  • 49
    • 0038368985 scopus 로고    scopus 로고
    • Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: potential implications in intracellular fluorescence detection of superoxide
    • Zhao H., Kalivendi S., Zhang H., Joseph J., Nithipatikom K., Vasquez-Vivar J., Kalyanaraman B. Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: potential implications in intracellular fluorescence detection of superoxide. Free Radical Biology and Medicine 2003, 34:1359-1368.
    • (2003) Free Radical Biology and Medicine , vol.34 , pp. 1359-1368
    • Zhao, H.1    Kalivendi, S.2    Zhang, H.3    Joseph, J.4    Nithipatikom, K.5    Vasquez-Vivar, J.6    Kalyanaraman, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.