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Volumn 44, Issue 10-11, 2011, Pages 873-883

Analysis of the effects of iron and vitamin C co-supplementation on oxidative damage, antioxidant response and inflammation in THP-1 macrophages

Author keywords

Antioxidant enzymes; Lipid peroxidation; NF B; PUFA; Redox status; TNF

Indexed keywords

3,4 METHYLENEDIOXYAMPHETAMINE; ACETYLCYSTEINE; ALPHA TOCOPHEROL; ANTIOXIDANT; ASCORBIC ACID; BUTYLCRESOL; CATALASE; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; HYDROGEN PEROXIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IRON; MALONALDEHYDE; POLYUNSATURATED FATTY ACID; SUPEROXIDE DISMUTASE; TROLOX C; TUMOR NECROSIS FACTOR ALPHA;

EID: 79958829836     PISSN: 00099120     EISSN: 18732933     Source Type: Journal    
DOI: 10.1016/j.clinbiochem.2011.04.012     Document Type: Article
Times cited : (17)

References (60)
  • 3
    • 0242349764 scopus 로고    scopus 로고
    • Oxidative stress and cardiovascular injury: Part II: animal and human studies
    • Griendling K.K., FitzGerald G.A. Oxidative stress and cardiovascular injury: Part II: animal and human studies. Circulation 2003, 108:2034-2040.
    • (2003) Circulation , vol.108 , pp. 2034-2040
    • Griendling, K.K.1    FitzGerald, G.A.2
  • 4
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • Sen C.K., Packer L. Antioxidant and redox regulation of gene transcription. FASEB J 1996, 10:709-720.
    • (1996) FASEB J , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.2
  • 5
    • 0026687504 scopus 로고
    • Increased susceptibility to activation and increased uptake of low density lipoprotein by cholesterol-loaded macrophages
    • Oiknine J., Aviram M. Increased susceptibility to activation and increased uptake of low density lipoprotein by cholesterol-loaded macrophages. Arterioscler Thromb 1992, 12:745-753.
    • (1992) Arterioscler Thromb , vol.12 , pp. 745-753
    • Oiknine, J.1    Aviram, M.2
  • 6
    • 0037115158 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling
    • Forman H.J., Torres M. Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling. Am J Respir Crit Care Med 2002, 166:S4-S8.
    • (2002) Am J Respir Crit Care Med , vol.166
    • Forman, H.J.1    Torres, M.2
  • 7
    • 0032102148 scopus 로고    scopus 로고
    • Colocalization of iron and ceroid in human atherosclerotic lesions
    • Lee F.Y., Lee T.S., Pan C.C., Huang A.L., Chau L.Y. Colocalization of iron and ceroid in human atherosclerotic lesions. Atherosclerosis 1998, 138:281-288.
    • (1998) Atherosclerosis , vol.138 , pp. 281-288
    • Lee, F.Y.1    Lee, T.S.2    Pan, C.C.3    Huang, A.L.4    Chau, L.Y.5
  • 8
    • 33751069000 scopus 로고    scopus 로고
    • Oxidative stress influences cholesterol efflux in THP-1 macrophages: role of ATP-binding cassette A1 and nuclear factors
    • Marcil V., Delvin E., Sane A.T., Tremblay A., Levy E. Oxidative stress influences cholesterol efflux in THP-1 macrophages: role of ATP-binding cassette A1 and nuclear factors. Cardiovasc Res 2006, 72:473-482.
    • (2006) Cardiovasc Res , vol.72 , pp. 473-482
    • Marcil, V.1    Delvin, E.2    Sane, A.T.3    Tremblay, A.4    Levy, E.5
  • 9
    • 0142151011 scopus 로고    scopus 로고
    • Inflammatory reaction without endogenous antioxidant response in Caco-2 cells exposed to iron/ascorbate-mediated lipid peroxidation
    • Bernotti S., Seidman E., Sinnett D., Brunet S., Dionne S., Delvin E., et al. Inflammatory reaction without endogenous antioxidant response in Caco-2 cells exposed to iron/ascorbate-mediated lipid peroxidation. Am J Physiol Gastrointest Liver Physiol 2003, 285:G898-G906.
    • (2003) Am J Physiol Gastrointest Liver Physiol , vol.285
    • Bernotti, S.1    Seidman, E.2    Sinnett, D.3    Brunet, S.4    Dionne, S.5    Delvin, E.6
  • 11
    • 37749045357 scopus 로고    scopus 로고
    • Development of an in vitro assay for the investigation of metabolism-induced drug hepatotoxicity
    • Otto M., Hansen S.H., Dalgaard L., Dubois J., Badolo L. Development of an in vitro assay for the investigation of metabolism-induced drug hepatotoxicity. Cell Biol Toxicol 2008, 24:87-99.
    • (2008) Cell Biol Toxicol , vol.24 , pp. 87-99
    • Otto, M.1    Hansen, S.H.2    Dalgaard, L.3    Dubois, J.4    Badolo, L.5
  • 12
    • 0027754135 scopus 로고
    • Caco-2 cell metabolism of oxygen-derived radicals
    • Baker S.S., Baker R.D. Caco-2 cell metabolism of oxygen-derived radicals. Dig Dis Sci 1993, 38:2273-2280.
    • (1993) Dig Dis Sci , vol.38 , pp. 2273-2280
    • Baker, S.S.1    Baker, R.D.2
  • 13
    • 0036237349 scopus 로고    scopus 로고
    • Simultaneous analysis of oxidized and reduced glutathione in cell extracts by capillary zone electrophoresis
    • Yang Q., Krautmacher C., Schilling D., Pittelkow M.R., Naylor S. Simultaneous analysis of oxidized and reduced glutathione in cell extracts by capillary zone electrophoresis. Biomed Chromatogr 2002, 16:224-228.
    • (2002) Biomed Chromatogr , vol.16 , pp. 224-228
    • Yang, Q.1    Krautmacher, C.2    Schilling, D.3    Pittelkow, M.R.4    Naylor, S.5
  • 14
    • 0024458253 scopus 로고
    • Direct transesterification of plasma fatty acids for the diagnosis of essential fatty acid deficiency in cystic fibrosis
    • Lepage G., Levy E., Ronco N., Smith L., Galeano N., Roy C.C. Direct transesterification of plasma fatty acids for the diagnosis of essential fatty acid deficiency in cystic fibrosis. J Lipid Res 1989, 30:1483-1490.
    • (1989) J Lipid Res , vol.30 , pp. 1483-1490
    • Lepage, G.1    Levy, E.2    Ronco, N.3    Smith, L.4    Galeano, N.5    Roy, C.C.6
  • 15
    • 0032246473 scopus 로고    scopus 로고
    • Regulatory antioxidant enzymes
    • Humana, NJ, A.D. Clifton (Ed.) Free Radical and Antioxidant Protocols
    • Pippenger C.E., Armstrong D. Regulatory antioxidant enzymes. Methods in Molecular Biology 1998, 299-313. Humana, NJ. A.D. Clifton (Ed.).
    • (1998) Methods in Molecular Biology , pp. 299-313
    • Pippenger, C.E.1    Armstrong, D.2
  • 16
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: an update
    • Babior B.M. NADPH oxidase: an update. Blood 1999, 93:1464-1476.
    • (1999) Blood , vol.93 , pp. 1464-1476
    • Babior, B.M.1
  • 17
    • 0030900931 scopus 로고    scopus 로고
    • Direct copper reduction by macrophages. Its role in low density lipoprotein oxidation
    • Garner B., van R.D., Dean R.T., Jessup W. Direct copper reduction by macrophages. Its role in low density lipoprotein oxidation. J Biol Chem 1997, 272:6927-6935.
    • (1997) J Biol Chem , vol.272 , pp. 6927-6935
    • Garner, B.1    van, R.D.2    Dean, R.T.3    Jessup, W.4
  • 18
    • 0033570271 scopus 로고    scopus 로고
    • Oxidative stress as a regulator of gene expression in the vasculature
    • Kunsch C., Medford R.M. Oxidative stress as a regulator of gene expression in the vasculature. Circ Res 1999, 85:753-766.
    • (1999) Circ Res , vol.85 , pp. 753-766
    • Kunsch, C.1    Medford, R.M.2
  • 20
    • 0002986150 scopus 로고
    • The role of iron in enzymatic lipid peroxidation
    • Academic Press, New York, W.A. Pryor (Ed.)
    • Aust S.D., Svingen B.A. The role of iron in enzymatic lipid peroxidation. Free Radicals in Biology 1982, 1-28. Academic Press, New York. W.A. Pryor (Ed.).
    • (1982) Free Radicals in Biology , pp. 1-28
    • Aust, S.D.1    Svingen, B.A.2
  • 21
    • 0033984036 scopus 로고    scopus 로고
    • Modulation of endoplasmic reticulum-bound cholesterol regulatory enzymes by iron/ascorbate-mediated lipid peroxidation
    • Brunet S., Thibault L., Lepage G., Seidman E.G., Dube N., Levy E. Modulation of endoplasmic reticulum-bound cholesterol regulatory enzymes by iron/ascorbate-mediated lipid peroxidation. Free Radic Biol Med 2000, 28:46-54.
    • (2000) Free Radic Biol Med , vol.28 , pp. 46-54
    • Brunet, S.1    Thibault, L.2    Lepage, G.3    Seidman, E.G.4    Dube, N.5    Levy, E.6
  • 22
    • 0021917237 scopus 로고
    • Variations in dietary triacylglycerol saturation alter the lipid composition and fluidity of rat intestinal plasma membranes
    • Brasitus T.A., Davidson N.O., Schachter D. Variations in dietary triacylglycerol saturation alter the lipid composition and fluidity of rat intestinal plasma membranes. Biochim Biophys Acta 1985, 812:460-472.
    • (1985) Biochim Biophys Acta , vol.812 , pp. 460-472
    • Brasitus, T.A.1    Davidson, N.O.2    Schachter, D.3
  • 23
    • 0023937941 scopus 로고
    • Ascorbate-enhanced lipid peroxidation in photooxidized cell membranes: cholesterol product analysis as a probe of reaction mechanism
    • Bachowski G.J., Thomas J.P., Girotti A.W. Ascorbate-enhanced lipid peroxidation in photooxidized cell membranes: cholesterol product analysis as a probe of reaction mechanism. Lipids 1988, 23:580-586.
    • (1988) Lipids , vol.23 , pp. 580-586
    • Bachowski, G.J.1    Thomas, J.P.2    Girotti, A.W.3
  • 24
    • 0027190587 scopus 로고
    • Lipid peroxidation of the brush-border membrane: membrane physical properties and glucose transport
    • Jourd'Heuil D., Vaananen P., Meddings J.B. Lipid peroxidation of the brush-border membrane: membrane physical properties and glucose transport. Am J Physiol 1993, 264:G1009-G1015.
    • (1993) Am J Physiol , vol.264
    • Jourd'Heuil, D.1    Vaananen, P.2    Meddings, J.B.3
  • 25
    • 77950626737 scopus 로고    scopus 로고
    • Change in the fatty acid pattern of erythrocyte membrane phospholipids after oral supplementation of specific fatty acids in patients with gastrointestinal diseases
    • Siener R., Alteheld B., Terjung B., Junghans B., Bitterlich N., Stehle P., et al. Change in the fatty acid pattern of erythrocyte membrane phospholipids after oral supplementation of specific fatty acids in patients with gastrointestinal diseases. Eur J Clin Nutr 2010, 64:410-418.
    • (2010) Eur J Clin Nutr , vol.64 , pp. 410-418
    • Siener, R.1    Alteheld, B.2    Terjung, B.3    Junghans, B.4    Bitterlich, N.5    Stehle, P.6
  • 26
    • 79251522887 scopus 로고    scopus 로고
    • Impact of the omega-3 to omega-6 polyunsaturated fatty acid ratio on cytokine release in human alveolar cells
    • Cotogni P., Muzio G., Trombetta A., Ranieri V.M., Canuto R.A. Impact of the omega-3 to omega-6 polyunsaturated fatty acid ratio on cytokine release in human alveolar cells. JPEN J Parenter Enteral Nutr 2011, 35:114-121.
    • (2011) JPEN J Parenter Enteral Nutr , vol.35 , pp. 114-121
    • Cotogni, P.1    Muzio, G.2    Trombetta, A.3    Ranieri, V.M.4    Canuto, R.A.5
  • 27
    • 34250636650 scopus 로고    scopus 로고
    • Colon cancer therapy: new perspectives of nutritional manipulations using polyunsaturated fatty acids
    • Dupertuis Y.M., Meguid M.M., Pichard C. Colon cancer therapy: new perspectives of nutritional manipulations using polyunsaturated fatty acids. Curr Opin Clin Nutr Metab Care 2007, 10:427-432.
    • (2007) Curr Opin Clin Nutr Metab Care , vol.10 , pp. 427-432
    • Dupertuis, Y.M.1    Meguid, M.M.2    Pichard, C.3
  • 28
    • 56649092631 scopus 로고    scopus 로고
    • Poorly controlled type 1 diabetes is associated with altered glutathione homeostasis in adolescents: apparent resistance to N-acetylcysteine supplementation
    • Darmaun D., Smith S.D., Sweeten S., Hartman B.K., Welch S., Mauras N. Poorly controlled type 1 diabetes is associated with altered glutathione homeostasis in adolescents: apparent resistance to N-acetylcysteine supplementation. Pediatr Diabetes 2008, 9:577-582.
    • (2008) Pediatr Diabetes , vol.9 , pp. 577-582
    • Darmaun, D.1    Smith, S.D.2    Sweeten, S.3    Hartman, B.K.4    Welch, S.5    Mauras, N.6
  • 29
    • 77950789625 scopus 로고    scopus 로고
    • Effect of alpha-tocopherol and beta-carotene supplementation on macrovascular complications and total mortality from diabetes: results of the ATBC Study
    • Kataja-Tuomola M.K., Kontto J.P., Mannisto S., Albanes D., Virtamo J.R. Effect of alpha-tocopherol and beta-carotene supplementation on macrovascular complications and total mortality from diabetes: results of the ATBC Study. Ann Med 2010, 42:178-186.
    • (2010) Ann Med , vol.42 , pp. 178-186
    • Kataja-Tuomola, M.K.1    Kontto, J.P.2    Mannisto, S.3    Albanes, D.4    Virtamo, J.R.5
  • 30
    • 0018195287 scopus 로고
    • The glutathione status of cells
    • Kosower N.S., Kosower E.M. The glutathione status of cells. Int Rev Cytol 1978, 54:109-160.
    • (1978) Int Rev Cytol , vol.54 , pp. 109-160
    • Kosower, N.S.1    Kosower, E.M.2
  • 32
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister A. Glutathione metabolism and its selective modification. J Biol Chem 1988, 263:17205-17208.
    • (1988) J Biol Chem , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 33
    • 0036372619 scopus 로고    scopus 로고
    • Redox potential of GSH/GSSG couple: assay and biological significance
    • Jones D.P. Redox potential of GSH/GSSG couple: assay and biological significance. Methods Enzymol 2002, 348:93-112.
    • (2002) Methods Enzymol , vol.348 , pp. 93-112
    • Jones, D.P.1
  • 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., Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 2001, 30:1191-1212.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 35
    • 33749372482 scopus 로고    scopus 로고
    • The effects of glutaredoxin and copper activation pathways on the disulfide and stability of Cu, Zn superoxide dismutase
    • Carroll M.C., Outten C.E., Proescher J.B., Rosenfeld L., Watson W.H., Whitson L.J., et al. The effects of glutaredoxin and copper activation pathways on the disulfide and stability of Cu, Zn superoxide dismutase. J Biol Chem 2006, 281:28648-28656.
    • (2006) J Biol Chem , vol.281 , pp. 28648-28656
    • Carroll, M.C.1    Outten, C.E.2    Proescher, J.B.3    Rosenfeld, L.4    Watson, W.H.5    Whitson, L.J.6
  • 36
    • 33644853318 scopus 로고    scopus 로고
    • Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form
    • Banci L., Bertini I., Cantini F., D'Amelio N., Gaggelli E. Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. J Biol Chem 2006, 281:2333-2337.
    • (2006) J Biol Chem , vol.281 , pp. 2333-2337
    • Banci, L.1    Bertini, I.2    Cantini, F.3    D'Amelio, N.4    Gaggelli, E.5
  • 37
    • 33744948516 scopus 로고    scopus 로고
    • Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase
    • Caruano-Yzermans A.L., Bartnikas T.B., Gitlin J.D. Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase. J Biol Chem 2006, 281:13581-13587.
    • (2006) J Biol Chem , vol.281 , pp. 13581-13587
    • Caruano-Yzermans, A.L.1    Bartnikas, T.B.2    Gitlin, J.D.3
  • 38
    • 1842782787 scopus 로고    scopus 로고
    • Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu, Zn superoxide dismutase
    • Brown N.M., Torres A.S., Doan P.E., O'Halloran T.V. Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu, Zn superoxide dismutase. Proc Nat Acad Sci U S A 2004, 101:5518-5523.
    • (2004) Proc Nat Acad Sci U S A , vol.101 , pp. 5518-5523
    • Brown, N.M.1    Torres, A.S.2    Doan, P.E.3    O'Halloran, T.V.4
  • 39
    • 9144261759 scopus 로고    scopus 로고
    • The unusually stable quaternary structure of human Cu, Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status
    • Arnesano F., Banci L., Bertini I., Martinelli M., Furukawa Y., O'Halloran TV. The unusually stable quaternary structure of human Cu, Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. J Biol Chem 2004, 279:47998-48003.
    • (2004) J Biol Chem , vol.279 , pp. 47998-48003
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Martinelli, M.4    Furukawa, Y.5    O'Halloran, T.V.6
  • 40
    • 33745946535 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein correlates positively with toll-like receptor 2 and interferon regulatory factor-1 and inversely with superoxide dismutase-1 expression: studies in hypercholesterolemic swine and THP-1 cells
    • Holvoet P., Davey P.C., De K.D., Doukoure M., Deridder E., Bochaton-Piallat M.L., et al. Oxidized low-density lipoprotein correlates positively with toll-like receptor 2 and interferon regulatory factor-1 and inversely with superoxide dismutase-1 expression: studies in hypercholesterolemic swine and THP-1 cells. Arterioscler Thromb Vasc Biol 2006, 26:1558-1565.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 1558-1565
    • Holvoet, P.1    Davey, P.C.2    De, K.D.3    Doukoure, M.4    Deridder, E.5    Bochaton-Piallat, M.L.6
  • 42
    • 3042533553 scopus 로고    scopus 로고
    • Gender differences in myogenic tone in superoxide dismutase knockout mouse: animal model of oxidative stress
    • Veerareddy S., Cooke C.L., Baker P.N., Davidge S.T. Gender differences in myogenic tone in superoxide dismutase knockout mouse: animal model of oxidative stress. Am J Physiol Heart Circ Physiol 2004, 287:H40-H45.
    • (2004) Am J Physiol Heart Circ Physiol , vol.287
    • Veerareddy, S.1    Cooke, C.L.2    Baker, P.N.3    Davidge, S.T.4
  • 43
    • 6344241908 scopus 로고    scopus 로고
    • Structure of cerebral arterioles in mice deficient in expression of the gene for endothelial nitric oxide synthase
    • Baumbach G.L., Sigmund C.D., Faraci F.M. Structure of cerebral arterioles in mice deficient in expression of the gene for endothelial nitric oxide synthase. Circ Res 2004, 95:822-829.
    • (2004) Circ Res , vol.95 , pp. 822-829
    • Baumbach, G.L.1    Sigmund, C.D.2    Faraci, F.M.3
  • 44
    • 3943073829 scopus 로고    scopus 로고
    • Vascular protection: superoxide dismutase isoforms in the vessel wall
    • Faraci F.M., Didion S.P. Vascular protection: superoxide dismutase isoforms in the vessel wall. Arterioscler Thromb Vasc Biol 2004, 24:1367-1373.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 1367-1373
    • Faraci, F.M.1    Didion, S.P.2
  • 46
    • 17644375510 scopus 로고    scopus 로고
    • Role of antioxidant-1 in extracellular superoxide dismutase function and expression
    • Jeney V., Itoh S., Wendt M., Gradek Q., Ushio-Fukai M., Harrison D.G., et al. Role of antioxidant-1 in extracellular superoxide dismutase function and expression. Circ Res 2005, 96:723-729.
    • (2005) Circ Res , vol.96 , pp. 723-729
    • Jeney, V.1    Itoh, S.2    Wendt, M.3    Gradek, Q.4    Ushio-Fukai, M.5    Harrison, D.G.6
  • 47
    • 0021280371 scopus 로고
    • Properties of extracellular superoxide dismutase from human lung
    • Marklund S.L. Properties of extracellular superoxide dismutase from human lung. Biochem J 1984, 220:269-272.
    • (1984) Biochem J , vol.220 , pp. 269-272
    • Marklund, S.L.1
  • 48
    • 0036736747 scopus 로고    scopus 로고
    • Peroxidase properties of extracellular superoxide dismutase: role of uric acid in modulating in vivo activity
    • Hink H.U., Santanam N., Dikalov S., McCann L., Nguyen A.D., Parthasarathy S., et al. Peroxidase properties of extracellular superoxide dismutase: role of uric acid in modulating in vivo activity. Arterioscler Thromb Vasc Biol 2002, 22:1402-1408.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 1402-1408
    • Hink, H.U.1    Santanam, N.2    Dikalov, S.3    McCann, L.4    Nguyen, A.D.5    Parthasarathy, S.6
  • 49
    • 0027618650 scopus 로고
    • Regulation of the NF-kappa B/rel transcription factor and I kappa B inhibitor system
    • Liou H.C., Baltimore D. Regulation of the NF-kappa B/rel transcription factor and I kappa B inhibitor system. Curr Opin Cell Biol 1993, 5:477-487.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 477-487
    • Liou, H.C.1    Baltimore, D.2
  • 50
    • 0028174061 scopus 로고
    • Function and activation of NF-kappa B in the immune system
    • Baeuerle P.A., Henkel T. Function and activation of NF-kappa B in the immune system. Annu Rev Immunol 1994, 12:141-179.
    • (1994) Annu Rev Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 51
    • 0032529475 scopus 로고    scopus 로고
    • Butylated hydroxytoluene and N-acetylcysteine attenuates tumor necrosis factor-alpha (TNF-alpha) secretion and TNF-alpha mRNA expression in alveolar macrophages from human lung transplant recipients in vitro
    • Hulten L.M., Lindmark H., Schersten H., Wiklund O., Nilsson FN, Riise G.C. Butylated hydroxytoluene and N-acetylcysteine attenuates tumor necrosis factor-alpha (TNF-alpha) secretion and TNF-alpha mRNA expression in alveolar macrophages from human lung transplant recipients in vitro. Transplantation 1998, 66:364-369.
    • (1998) Transplantation , vol.66 , pp. 364-369
    • Hulten, L.M.1    Lindmark, H.2    Schersten, H.3    Wiklund, O.4    Nilsson, F.N.5    Riise, G.C.6
  • 52
    • 62349116866 scopus 로고    scopus 로고
    • Vascular NAD(P)H oxidase activation in diabetes: a double-edged sword in redox signalling
    • Gao L., Mann G.E. Vascular NAD(P)H oxidase activation in diabetes: a double-edged sword in redox signalling. Cardiovasc Res 2009, 82:9-20.
    • (2009) Cardiovasc Res , vol.82 , pp. 9-20
    • Gao, L.1    Mann, G.E.2
  • 53
    • 79952362120 scopus 로고    scopus 로고
    • Augmented NADPH oxidase activity and p22phox expression in monocytes underlie oxidative stress of patients with type 2 diabetes mellitus
    • Huang X., Sun M., Li D., Liu J., Guo H., Dong Y., et al. Augmented NADPH oxidase activity and p22phox expression in monocytes underlie oxidative stress of patients with type 2 diabetes mellitus. Diabetes Res Clin Pract 2011.
    • (2011) Diabetes Res Clin Pract
    • Huang, X.1    Sun, M.2    Li, D.3    Liu, J.4    Guo, H.5    Dong, Y.6
  • 54
    • 58849107536 scopus 로고    scopus 로고
    • Sensory neurons and schwann cells respond to oxidative stress by increasing antioxidant defense mechanisms
    • Vincent A.M., Kato K., McLean L.L., Soules M.E., Feldman E.L. Sensory neurons and schwann cells respond to oxidative stress by increasing antioxidant defense mechanisms. Antioxid Redox Signal 2009, 11:425-438.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 425-438
    • Vincent, A.M.1    Kato, K.2    McLean, L.L.3    Soules, M.E.4    Feldman, E.L.5
  • 55
    • 33646359960 scopus 로고    scopus 로고
    • Coronary heart disease risk equivalence in diabetes depends on concomitant risk factors
    • Howard B.V., Best L.G., Galloway J.M., Howard W.J., Jones K., Lee E.T., et al. Coronary heart disease risk equivalence in diabetes depends on concomitant risk factors. Diabetes Care 2006, 29:391-397.
    • (2006) Diabetes Care , vol.29 , pp. 391-397
    • Howard, B.V.1    Best, L.G.2    Galloway, J.M.3    Howard, W.J.4    Jones, K.5    Lee, E.T.6
  • 56
    • 33644696797 scopus 로고    scopus 로고
    • Type 2 diabetes as a "coronary heart disease equivalent": an 18-year prospective population-based study in Finnish subjects
    • Juutilainen A., Lehto S., Ronnemaa T., Pyorala K., Laakso M. Type 2 diabetes as a "coronary heart disease equivalent": an 18-year prospective population-based study in Finnish subjects. Diabetes Care 2005, 28:2901-2907.
    • (2005) Diabetes Care , vol.28 , pp. 2901-2907
    • Juutilainen, A.1    Lehto, S.2    Ronnemaa, T.3    Pyorala, K.4    Laakso, M.5
  • 57
    • 17644394616 scopus 로고    scopus 로고
    • Smoldering and polarized inflammation in the initiation and promotion of malignant disease
    • Balkwill F., Charles K.A., Mantovani A. Smoldering and polarized inflammation in the initiation and promotion of malignant disease. Cancer Cell 2005, 7:211-217.
    • (2005) Cancer Cell , vol.7 , pp. 211-217
    • Balkwill, F.1    Charles, K.A.2    Mantovani, A.3
  • 60
    • 78650898208 scopus 로고    scopus 로고
    • Fruit and vegetables and cancer risk
    • Key T.J. Fruit and vegetables and cancer risk. Br J Cancer 2011, 104:6-11.
    • (2011) Br J Cancer , vol.104 , pp. 6-11
    • Key, T.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.