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Volumn 19, Issue 11, 2008, Pages 746-753

Niacin deficiency causes oxidative stress in rat bone marrow cells but not through decreased NADPH or glutathione status

Author keywords

Bone marrow; DNA; Glutathione; NADPH; Niacin; Oxidative stress; Protein; Rat

Indexed keywords

2,4 DINITROPHENYLHYDRAZINE; 8 HYDROXYDEOXYGUANOSINE; DNA; GLUTATHIONE; GLUTATHIONE DISULFIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PYRIDINE NUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 53149136711     PISSN: 09552863     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jnutbio.2007.10.003     Document Type: Article
Times cited : (21)

References (40)
  • 1
    • 33644891347 scopus 로고    scopus 로고
    • Tocotrienols: vitamin E beyond tocopherols
    • Sen C.K., Khanna S., and Roy S. Tocotrienols: vitamin E beyond tocopherols. Life Sci 78 (2006) 2088-2098
    • (2006) Life Sci , vol.78 , pp. 2088-2098
    • Sen, C.K.1    Khanna, S.2    Roy, S.3
  • 2
    • 33646762858 scopus 로고    scopus 로고
    • A combined deficiency of vitamins E and C causes severe central nervous system damage in guinea pigs
    • Burk R.F., Christensen J.M., Maguire M.J., Austin L.M., Whetsell Jr. W.O., May J.M., et al. A combined deficiency of vitamins E and C causes severe central nervous system damage in guinea pigs. J Nutr 136 (2006) 1576-1581
    • (2006) J Nutr , vol.136 , pp. 1576-1581
    • Burk, R.F.1    Christensen, J.M.2    Maguire, M.J.3    Austin, L.M.4    Whetsell Jr., W.O.5    May, J.M.6
  • 3
    • 1842423444 scopus 로고    scopus 로고
    • Assessment of requirements for selenium and adequacy of selenium status: a review
    • Thomson C.D. Assessment of requirements for selenium and adequacy of selenium status: a review. Eur J Clin Nutr 58 (2004) 391-402
    • (2004) Eur J Clin Nutr , vol.58 , pp. 391-402
    • Thomson, C.D.1
  • 5
    • 0034254665 scopus 로고    scopus 로고
    • On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids
    • Prutz W.A., Kissner R., Koppenol W.H., and Ruegger H. On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids. Arch Biochem Biophys 380 (2000) 181-191
    • (2000) Arch Biochem Biophys , vol.380 , pp. 181-191
    • Prutz, W.A.1    Kissner, R.2    Koppenol, W.H.3    Ruegger, H.4
  • 6
    • 0030269977 scopus 로고    scopus 로고
    • Enzymatic and molecular aspects of the antioxidant effect of menadione in hepatic microsomes
    • Tampo Y., and Yonaha M. Enzymatic and molecular aspects of the antioxidant effect of menadione in hepatic microsomes. Arch Biochem Biophys 334 (1996) 163-174
    • (1996) Arch Biochem Biophys , vol.334 , pp. 163-174
    • Tampo, Y.1    Yonaha, M.2
  • 7
    • 0019804120 scopus 로고
    • Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation
    • Kappus H., and 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
  • 8
    • 0001264584 scopus 로고
    • Role of quinones, active oxygen species and metals in the genotoxicity of 1,2,4-benzenetriol, a metabolite of benzene
    • Nohl H., Esterbauer H., and Rice-Evans C. (Eds), Richelieu Press, London
    • Zhang L., Smith M.T., Bandy B., Tamaki S.J., and Davison A.J. Role of quinones, active oxygen species and metals in the genotoxicity of 1,2,4-benzenetriol, a metabolite of benzene. In: Nohl H., Esterbauer H., and Rice-Evans C. (Eds). Free Radicals in the Environment, Medicine and Toxicology vol. 8 (1994), Richelieu Press, London 521-562
    • (1994) Free Radicals in the Environment, Medicine and Toxicology , vol.8 , pp. 521-562
    • Zhang, L.1    Smith, M.T.2    Bandy, B.3    Tamaki, S.J.4    Davison, A.J.5
  • 9
    • 0037082112 scopus 로고    scopus 로고
    • Inhibition of NADH/NADPH oxidase affects signal transduction by growth factor receptors in normal fibroblasts
    • Ammendola R., Ruocchio M.R., Chirico G., Russo L., De Felice C., Esposito F., et al. Inhibition of NADH/NADPH oxidase affects signal transduction by growth factor receptors in normal fibroblasts. Arch Biochem Biophys 397 (2002) 253-257
    • (2002) Arch Biochem Biophys , vol.397 , pp. 253-257
    • Ammendola, R.1    Ruocchio, M.R.2    Chirico, G.3    Russo, L.4    De Felice, C.5    Esposito, F.6
  • 10
    • 0032189081 scopus 로고    scopus 로고
    • Secondary leukemias induced by topoisomerase-targeted drugs
    • Felix C.A. Secondary leukemias induced by topoisomerase-targeted drugs. Biochim Biophys Acta 1400 (1998) 233-255
    • (1998) Biochim Biophys Acta , vol.1400 , pp. 233-255
    • Felix, C.A.1
  • 11
    • 0036137968 scopus 로고    scopus 로고
    • Niacin deficiency decreases bone marrow poly(ADP-ribose) and the latency of ethylnitrosourea-induced carcinogenesis in rats
    • Boyonoski A.C., Spronck J.C., Gallacher L.M., Jacobs R.M., Shah G.M., Poirier G.G., et al. Niacin deficiency decreases bone marrow poly(ADP-ribose) and the latency of ethylnitrosourea-induced carcinogenesis in rats. J Nutr 132 (2002) 108-114
    • (2002) J Nutr , vol.132 , pp. 108-114
    • Boyonoski, A.C.1    Spronck, J.C.2    Gallacher, L.M.3    Jacobs, R.M.4    Shah, G.M.5    Poirier, G.G.6
  • 12
    • 0037206611 scopus 로고    scopus 로고
    • Niacin deficiency increases spontaneous and etoposide-induced chromosomal instability in rat bone marrow cells in vivo
    • Spronck J.C., and Kirkland J.B. Niacin deficiency increases spontaneous and etoposide-induced chromosomal instability in rat bone marrow cells in vivo. Mutat Res 508 (2002) 83-97
    • (2002) Mutat Res , vol.508 , pp. 83-97
    • Spronck, J.C.1    Kirkland, J.B.2
  • 13
    • 35548963303 scopus 로고    scopus 로고
    • Niacin deficiency delays DNA excision repair and increases spontaneous and nitrosourea-induced chromosomal instability in rat bone marrow
    • Kostecki L.M., Thomas M., Linford G., Lizottee M., Toxopeus L., Bartleman A.P., et al. Niacin deficiency delays DNA excision repair and increases spontaneous and nitrosourea-induced chromosomal instability in rat bone marrow. Mutat Res 625 (2007) 50-61
    • (2007) Mutat Res , vol.625 , pp. 50-61
    • Kostecki, L.M.1    Thomas, M.2    Linford, G.3    Lizottee, M.4    Toxopeus, L.5    Bartleman, A.P.6
  • 14
    • 0034053990 scopus 로고    scopus 로고
    • Niacin deficiency in rats increases the severity of ethylnitrosourea-induced anemia and leukopenia
    • Boyonoski A.C., Gallacher L.M., ApSimon M.M., Jacobs R.M., Shah G.M., Poirier G.G., et al. Niacin deficiency in rats increases the severity of ethylnitrosourea-induced anemia and leukopenia. J Nutr 130 (2000) 1102-1107
    • (2000) J Nutr , vol.130 , pp. 1102-1107
    • Boyonoski, A.C.1    Gallacher, L.M.2    ApSimon, M.M.3    Jacobs, R.M.4    Shah, G.M.5    Poirier, G.G.6
  • 15
    • 41449091343 scopus 로고    scopus 로고
    • Niacin supplementation decreases the incidence of alkylation-induced non-lymphocytic leukemia in Long-Evans rats
    • [in press]
    • Bartleman A.P., Jacob R.A., and Kirkland J.B. Niacin supplementation decreases the incidence of alkylation-induced non-lymphocytic leukemia in Long-Evans rats. Nutr Cancer (2008) [in press]
    • (2008) Nutr Cancer
    • Bartleman, A.P.1    Jacob, R.A.2    Kirkland, J.B.3
  • 16
    • 34249907589 scopus 로고    scopus 로고
    • Niacin deficiency alters p53 expression and impairs etoposide-induced cell cycle arrest and apoptosis in rat bone marrow cells
    • Spronck J.C., Nickerson J.L., and Kirkland J.B. Niacin deficiency alters p53 expression and impairs etoposide-induced cell cycle arrest and apoptosis in rat bone marrow cells. Nutr Cancer 57 (2007) 88-99
    • (2007) Nutr Cancer , vol.57 , pp. 88-99
    • Spronck, J.C.1    Nickerson, J.L.2    Kirkland, J.B.3
  • 17
    • 34547991087 scopus 로고    scopus 로고
    • Niacin
    • Rucker R., Zempleni J., Suttie J.W., et al. (Eds), Taylor and Francis, New York, NY
    • Kirkland J.B. Niacin. In: Rucker R., Zempleni J., Suttie J.W., et al. (Eds). Handbook of Vitamins, Fourth Edition. 4th ed (2007), Taylor and Francis, New York, NY 191-232
    • (2007) Handbook of Vitamins, Fourth Edition. 4th ed , pp. 191-232
    • Kirkland, J.B.1
  • 18
    • 0028143826 scopus 로고
    • Differential susceptibility of plasma proteins to oxidative modification: examination by western blot immunoassay
    • Shacter E., Williams J.A., Lim M., and Levine R.L. Differential susceptibility of plasma proteins to oxidative modification: examination by western blot immunoassay. Free Radic Biol Med 17 (1994) 429-437
    • (1994) Free Radic Biol Med , vol.17 , pp. 429-437
    • Shacter, E.1    Williams, J.A.2    Lim, M.3    Levine, R.L.4
  • 19
    • 0346100521 scopus 로고    scopus 로고
    • Recent advances in the analysis of oxidized proteins
    • Requena J.R., Levine R.L., and Stadtman E.R. Recent advances in the analysis of oxidized proteins. Amino Acids 25 (2003) 221-226
    • (2003) Amino Acids , vol.25 , pp. 221-226
    • Requena, J.R.1    Levine, R.L.2    Stadtman, E.R.3
  • 20
    • 33644754088 scopus 로고    scopus 로고
    • Recognition of oxidatively modified bases within the biotin-binding site of avidin
    • Conners R., Hooley E., Clarke A.R., Thomas S., and Brady R.L. Recognition of oxidatively modified bases within the biotin-binding site of avidin. J Mol Biol 357 (2006) 263-274
    • (2006) J Mol Biol , vol.357 , pp. 263-274
    • Conners, R.1    Hooley, E.2    Clarke, A.R.3    Thomas, S.4    Brady, R.L.5
  • 21
    • 0031984418 scopus 로고    scopus 로고
    • Direct detection of 8-oxodeoxyguanosine and 8-oxoguanine by avidin and its analogues
    • Struthers L., Patel R., Clark J., and Thomas S. Direct detection of 8-oxodeoxyguanosine and 8-oxoguanine by avidin and its analogues. Anal Biochem 255 (1998) 20-31
    • (1998) Anal Biochem , vol.255 , pp. 20-31
    • Struthers, L.1    Patel, R.2    Clark, J.3    Thomas, S.4
  • 22
    • 0028828562 scopus 로고
    • Heme degradation in the presence of glutathione. A proposed mechanism to account for the high levels of non-heme iron found in the membranes of hemoglobinopathic red blood cells
    • Atamna H., and Ginsburg H. Heme degradation in the presence of glutathione. A proposed mechanism to account for the high levels of non-heme iron found in the membranes of hemoglobinopathic red blood cells. J Biol Chem 270 (1995) 24876-24883
    • (1995) J Biol Chem , vol.270 , pp. 24876-24883
    • Atamna, H.1    Ginsburg, H.2
  • 24
    • 0029028545 scopus 로고
    • Methods for biochemical study of poly(ADP-ribose) metabolism in vitro and in vivo
    • Shah G.M., Poirier D., Duchaine C., Brochu G., Desnoyers S., Lagueux J., et al. Methods for biochemical study of poly(ADP-ribose) metabolism in vitro and in vivo. Anal Biochem 227 (1995) 1-13
    • (1995) Anal Biochem , vol.227 , pp. 1-13
    • Shah, G.M.1    Poirier, D.2    Duchaine, C.3    Brochu, G.4    Desnoyers, S.5    Lagueux, J.6
  • 25
    • 0017072120 scopus 로고
    • Pyridine nucleotide levels as a function of growth in normal and transformed 3T3 cells
    • Jacobson E.L., and Jacobson M.K. Pyridine nucleotide levels as a function of growth in normal and transformed 3T3 cells. Arch Biochem Biophys 175 (1976) 627-634
    • (1976) Arch Biochem Biophys , vol.175 , pp. 627-634
    • Jacobson, E.L.1    Jacobson, M.K.2
  • 26
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulfide in biological samples
    • Anderson M.E. Determination of glutathione and glutathione disulfide in biological samples. Methods Enzymol 113 (1985) 548-555
    • (1985) Methods Enzymol , vol.113 , pp. 548-555
    • Anderson, M.E.1
  • 27
    • 0019167355 scopus 로고
    • Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine
    • Griffith O.W. Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Anal Biochem 106 (1980) 207-212
    • (1980) Anal Biochem , vol.106 , pp. 207-212
    • Griffith, O.W.1
  • 28
    • 0033008869 scopus 로고    scopus 로고
    • Decreased hemolysis and lipid peroxidation in blood during storage in the presence of nicotinic acid
    • Arun P., Padmakumaran Nair K.G., Manojkumar V., Deepadevi K.V., Lakshmi L.R., and Kurup P.A. Decreased hemolysis and lipid peroxidation in blood during storage in the presence of nicotinic acid. Vox Sang 76 (1999) 220-225
    • (1999) Vox Sang , vol.76 , pp. 220-225
    • Arun, P.1    Padmakumaran Nair, K.G.2    Manojkumar, V.3    Deepadevi, K.V.4    Lakshmi, L.R.5    Kurup, P.A.6
  • 30
    • 20544443964 scopus 로고    scopus 로고
    • Decreasing the oxidant stress from paraquat in isolated perfused rat lung using captopril and niacin
    • Ghazi-Khansari M., Nasiri G., and Honarjoo M. Decreasing the oxidant stress from paraquat in isolated perfused rat lung using captopril and niacin. Arch Toxicol 79 (2005) 341-345
    • (2005) Arch Toxicol , vol.79 , pp. 341-345
    • Ghazi-Khansari, M.1    Nasiri, G.2    Honarjoo, M.3
  • 31
    • 0018906390 scopus 로고
    • (ADP-ribose)n participates in DNA excision repair
    • Durkacz B.W., Omidiji O., Gray D.A., and Shall S. (ADP-ribose)n participates in DNA excision repair. Nature 283 (1980) 593-596
    • (1980) Nature , vol.283 , pp. 593-596
    • Durkacz, B.W.1    Omidiji, O.2    Gray, D.A.3    Shall, S.4
  • 32
  • 34
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer F.Q., and Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30 (2001) 1191-1212
    • (2001) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 35
    • 0035919479 scopus 로고    scopus 로고
    • Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
    • Rutter J., Reick M., Wu L.C., and McKnight S.L. Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors. Science 293 (2001) 510-514
    • (2001) Science , vol.293 , pp. 510-514
    • Rutter, J.1    Reick, M.2    Wu, L.C.3    McKnight, S.L.4
  • 36
    • 0037040581 scopus 로고    scopus 로고
    • Regulation of corepressor function by nuclear NADH
    • Zhang Q., Piston D.W., and Goodman R.H. Regulation of corepressor function by nuclear NADH. Science 295 (2002) 1895-1897
    • (2002) Science , vol.295 , pp. 1895-1897
    • Zhang, Q.1    Piston, D.W.2    Goodman, R.H.3
  • 37
    • 33748329644 scopus 로고    scopus 로고
    • Cooperative activity of Ref-1/APE and ERp57 in reductive activation of transcription factors
    • Grillo C., D'Ambrosio C., Scaloni A., Maceroni M., Merluzzi S., Turano C., et al. Cooperative activity of Ref-1/APE and ERp57 in reductive activation of transcription factors. Free Radic Biol Med 41 (2006) 1113-1123
    • (2006) Free Radic Biol Med , vol.41 , pp. 1113-1123
    • Grillo, C.1    D'Ambrosio, C.2    Scaloni, A.3    Maceroni, M.4    Merluzzi, S.5    Turano, C.6
  • 38
    • 53149138743 scopus 로고    scopus 로고
    • Vitamin-Dependent Modifications of Chromatin: Epigenetic Events and Genomic Stability
    • Rucker R.B., Zempleni J., Suttie J.W., et al. (Eds), Taylor and Francis, New York, NY
    • Kirkland J.B., Zempleni J., Buckles L.K., and Christman J.K. Vitamin-Dependent Modifications of Chromatin: Epigenetic Events and Genomic Stability. In: Rucker R.B., Zempleni J., Suttie J.W., et al. (Eds). Handbook of vitamins. 4th ed. (2007), Taylor and Francis, New York, NY 521-544
    • (2007) Handbook of vitamins. 4th ed. , pp. 521-544
    • Kirkland, J.B.1    Zempleni, J.2    Buckles, L.K.3    Christman, J.K.4
  • 39
    • 0344197087 scopus 로고    scopus 로고
    • Niacin and carcinogenesis
    • Kirkland J.B. Niacin and carcinogenesis. Nutr Cancer 46 (2003) 110-118
    • (2003) Nutr Cancer , vol.46 , pp. 110-118
    • Kirkland, J.B.1
  • 40
    • 34347257042 scopus 로고    scopus 로고
    • Nox enzymes, ROS, and chronic disease: an example of antagonistic pleiotropy
    • Lambeth J.D. Nox enzymes, ROS, and chronic disease: an example of antagonistic pleiotropy. Free Radic Biol Med 43 (2007) 332-347
    • (2007) Free Radic Biol Med , vol.43 , pp. 332-347
    • Lambeth, J.D.1


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