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Volumn 58, Issue 13, 2010, Pages 7624-7633

Egg yolk peptides up-regulate glutathione synthesis and antioxidant enzyme activities in a porcine model of intestinal oxidative stress

Author keywords

; glutamylcysteine synthetase; Antioxidant enzymes; Egg yolk peptides; Glutathione; Hydrogen peroxide; Oxidative stress

Indexed keywords

ANTIOXIDANT; CATALASE; EGG PROTEIN; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; PEPTIDE; SUPEROXIDE DISMUTASE;

EID: 77954545552     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf1011598     Document Type: Article
Times cited : (67)

References (57)
  • 1
    • 0000092645 scopus 로고    scopus 로고
    • Molecular and cellular responses to oxidative stress and changes in oxidation-reduction imbalance in the intestine
    • Aw, T. Y. Molecular and cellular responses to oxidative stress and changes in oxidation-reduction imbalance in the intestine. Am. J. Clin. Nutr. 1999, 70, 557-565.
    • (1999) Am. J. Clin. Nutr. , vol.70 , pp. 557-565
    • Aw, T.Y.1
  • 2
    • 34547851729 scopus 로고    scopus 로고
    • Oxidative stress and pathogenesis of inflammatory bowel disease: An epiphenomenon or the cause?
    • Rezaie, A.; Parker, R. D.; Abdollahi, M. Oxidative stress and pathogenesis of inflammatory bowel disease: an epiphenomenon or the cause? Div. Dis. Sci 2007, 52, 2015-2021.
    • (2007) Div. Dis. Sci , vol.52 , pp. 2015-2021
    • Rezaie, A.1    Parker, R.D.2    Abdollahi, M.3
  • 4
    • 0034468847 scopus 로고    scopus 로고
    • The gastrointestinal tract: A maior site of antioxidant action?
    • Halliwell, B.; Zhao, K.; Whiteman, M. The gastrointestinal tract: a maior site of antioxidant action? Free Radical Res. 2000, 33, 819-830.
    • (2000) Free Radical Res. , vol.33 , pp. 819-830
    • Halliwell, B.1    Zhao, K.2    Whiteman, M.3
  • 5
    • 0025069762 scopus 로고
    • How to characterize a biological, antioxidant
    • Halliwell, B. How to characterize a biological, antioxidant. Free Radical Res. Commun. 1990, 9, 1-32.
    • (1990) Free Radical Res. Commun. , vol.9 , pp. 1-32
    • Halliwell, B.1
  • 6
    • 34250359779 scopus 로고    scopus 로고
    • Emerging role of Nrf2 in protecting against hepatic and gastrointestinal, disease
    • Aleksunes, L. M.; Manautou, J. E. Emerging role of Nrf2 in protecting against hepatic and gastrointestinal, disease. Toxicol. Pathol. 2007, 35, 459-473.
    • (2007) Toxicol. Pathol. , vol.35 , pp. 459-473
    • Aleksunes, L.M.1    Manautou, J.E.2
  • 7
    • 0029058780 scopus 로고
    • Oxidation of parenteral lipid, emulsion by ambient and phototherapy lights: Potential toxicity of routine parenteral feeding
    • Neuzil, J.; Darlow, B. A.; Inder, T. E.; Sluis, K. B.; Winterbourn, C. C.; Stocker, R. Oxidation of parenteral lipid, emulsion by ambient and phototherapy lights: potential toxicity of routine parenteral feeding. J. Pediatr. 1995, 126, 785-790.
    • (1995) J. Pediatr. , vol.126 , pp. 785-790
    • Neuzil, J.1    Darlow, B.A.2    Inder, T.E.3    Sluis, K.B.4    Winterbourn, C.C.5    Stocker, R.6
  • 8
    • 34848928166 scopus 로고    scopus 로고
    • Chronic treatment with resveratrol induces redox stress- And, ataxia telangiectasia-mutated (ATM)-dependent senescence in p53-positive cancer cells
    • Heiss, E. H.; Schilder, Y. D.; Dirsch, V. M. Chronic treatment with resveratrol induces redox stress- and, ataxia telangiectasia-mutated (ATM)-dependent senescence in p53-positive cancer cells. J. Biol. Chem. 2007, 282, 26759-26766.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26759-26766
    • Heiss, E.H.1    Schilder, Y.D.2    Dirsch, V.M.3
  • 9
    • 0036489186 scopus 로고    scopus 로고
    • Flavonoids increase the intracellular glutathione level by transactivation of the γ-glutamylcysteine synthetase catalytical subunit promoter
    • Myhrstad, M. C.; Carlsen, H.; Nordstrom, O.; Blomhoff, R.; Moskaug, J. O. Flavonoids increase the intracellular glutathione level by transactivation of the γ-glutamylcysteine synthetase catalytical subunit promoter. Free Radical Biol. Med. 2002, 32, 386-393.
    • (2002) Free Radical Biol. Med. , vol.32 , pp. 386-393
    • Myhrstad, M.C.1    Carlsen, H.2    Nordstrom, O.3    Blomhoff, R.4    Moskaug, J.O.5
  • 10
    • 1842425919 scopus 로고    scopus 로고
    • Extra virgin olive oil biophenols inhibit cell-mediated oxidation of LDL by increasing the mRNA transcription of glutathione-related enzymes
    • Masella, R.; Vari, R.; D'Archivio, M.; Di Benedetto, R.; Matarrese, P.; Malorni, W.; Scazzocchio, B.; Giovannini, C. Extra virgin olive oil biophenols inhibit cell-mediated oxidation of LDL by increasing the mRNA transcription of glutathione-related enzymes. J. Nutr. 2004, 134, 785-791.
    • (2004) J. Nutr. , vol.134 , pp. 785-791
    • Masella, R.1    Vari, R.2    D'Archivio, M.3    Di Benedetto, R.4    Matarrese, P.5    Malorni, W.6    Scazzocchio, B.7    Giovannini, C.8
  • 11
    • 13244289773 scopus 로고    scopus 로고
    • Curcumin induces glutathione biosynthesis and inhibits NF-KB activation and interleukin-8 release in alveolar epithelial cells: Mechanism of free radical scavenging activity
    • Biswas, S. K.; McClure, D.; Jimenez, L. A.; Megson, I. L.; Rahman, I. Curcumin induces glutathione biosynthesis and inhibits NF-KB activation and interleukin-8 release in alveolar epithelial cells: mechanism of free radical scavenging activity. Antioxid. Redox Simal. 2005, 7, 32-41.
    • (2005) Antioxid. Redox Simal. , vol.7 , pp. 32-41
    • Biswas, S.K.1    McClure, D.2    Jimenez, L.A.3    Megson, I.L.4    Rahman, I.5
  • 12
    • 1542436560 scopus 로고    scopus 로고
    • A flavonoid antioxidant, prevents and protects against ethanolinduced oxidative stress in mouse liver
    • Molina, M. F.; Sanchez-Reus, I.; Iglesias, I.; Benedi, J. Quercetin, a flavonoid antioxidant, prevents and protects against ethanolinduced oxidative stress in mouse liver. Biol. Pharm. Bull. 2003, 26, 1398-1402.
    • (2003) Biol. Pharm. Bull. , vol.26 , pp. 1398-1402
    • Molina, M.F.1    Sanchez-Reus, I.2    Iglesias, I.3    Quercetin, B.J.4
  • 13
    • 27744488160 scopus 로고    scopus 로고
    • Upregulation of endogenous antioxidants and phase 2 enzymes by the red wine polyphenol, resveratrol in cultured aortic smooth, muscle cells leads to cytoprotection against oxidative and electrophilic stress
    • Li, Y.; Cao, Z.; Zhu, H. Upregulation of endogenous antioxidants and phase 2 enzymes by the red wine polyphenol, resveratrol in cultured aortic smooth, muscle cells leads to cytoprotection against oxidative and electrophilic stress. Pharmacol, Res. 2006, 53, 6-15.
    • (2006) Pharmacol, Res. , vol.53 , pp. 6-15
    • Li, Y.1    Cao, Z.2    Zhu, H.3
  • 14
    • 0028902218 scopus 로고
    • Dairy proteins protect against dimethylhydrazine-induced intestinal cancers in rats
    • Mcintosh, G. H.; Regester, G. O.; Le Leu, R. K.; Royle, P. J.; Smithers, G. W. Dairy proteins protect against dimethylhydrazine-induced intestinal cancers in rats. J. Nutr. 1995, 125, 809-816.
    • (1995) J. Nutr. , vol.125 , pp. 809-816
    • Mcintosh, G.H.1    Regester, G.O.2    Le Leu, R.K.3    Royle, P.J.4    Smithers, G.W.5
  • 15
    • 33745727051 scopus 로고    scopus 로고
    • Plant originated glycoprotein has anti-oxidative and anti-inflammatory effects on dextran sulfate sodium-induced colitis in mouse
    • Oh, P.S.; Lim, K. T. Plant originated glycoprotein has anti-oxidative and anti-inflammatory effects on dextran sulfate sodium-induced colitis in mouse. J. Biomed. Sci. 2006, 13, 549-560.
    • (2006) J. Biomed. Sci. , vol.13 , pp. 549-560
    • Oh, P.S.1    Lim, K.T.2
  • 16
    • 34247594808 scopus 로고    scopus 로고
    • Oligophosphopeptides derived from egg yolk phosvitin up-regulate γ-glutamylcysteine synthetase and antioxidant enzymes against oxidative stress in Caco-2 cells
    • Katayama, S.; Ishikawa, S.; Fan, M. Z.; Mine, Y. Oligophosphopeptides derived from egg yolk phosvitin up-regulate γ-glutamylcysteine synthetase and antioxidant enzymes against oxidative stress in Caco-2 cells. J., Agric, Food Chem. 2007, 55, 2829-2835.
    • (2007) J., Agric, Food Chem. , vol.55 , pp. 2829-2835
    • Katayama, S.1    Ishikawa, S.2    Fan, M.Z.3    Mine, Y.4
  • 17
    • 33244465570 scopus 로고    scopus 로고
    • Antioxidative stress activity of oligophosphopeptides derived from hen egg yolk, phosvitin in Caco-2 cells
    • Katayama, S.; Xu, X.; Fan, M. Z.; Mine, Y. Antioxidative stress activity of oligophosphopeptides derived from hen egg yolk, phosvitin in Caco-2 cells. J. Aeric. Food Chem. 2006, 54, 773-778.
    • (2006) J. Aeric. Food Chem. , vol.54 , pp. 773-778
    • Katayama, S.1    Xu, X.2    Fan, M.Z.3    Mine, Y.4
  • 18
    • 0025731084 scopus 로고
    • Relationship between surface hydrophilicity of a protein and its stability against denaturation by organic solvents
    • Khmelnitsky, Y. L.; Belova, A. B.; Levashov, A. V.; Mozhaev, V. V. Relationship between surface hydrophilicity of a protein and its stability against denaturation by organic solvents. FEBS Lett, 1991, 284, 267-269.
    • (1991) FEBS Lett , vol.284 , pp. 267-269
    • Khmelnitsky, Y.L.1    Belova, A.B.2    Levashov, A.V.3    Mozhaev, V.V.4
  • 20
    • 62449115988 scopus 로고    scopus 로고
    • Egg yolk protein modification by controlled enzymatic hydrolysis for improved functionalities
    • 44
    • Wang, G.; Wang, T. Egg yolk protein modification by controlled enzymatic hydrolysis for improved functionalities. Int. J. Food Sci. Technol. 2009, 44, 44 (4) 763-769.
    • (2009) Int. J. Food Sci. Technol. , vol.44 , Issue.4 , pp. 763-769
    • Wang, G.1    Wang, T.2
  • 21
    • 0035358387 scopus 로고    scopus 로고
    • Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin-free egg yolk
    • Park, P. J.; Jung, W. K.; Nam, K. S.; Shahidi, F.; Kim, S. K. Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin-free egg yolk. J. Am. Oil Chem. Soc. 2001, 78, 651-656.
    • (2001) J. Am. Oil Chem. Soc. , vol.78 , pp. 651-656
    • Park, P.J.1    Jung, W.K.2    Nam, K.S.3    Shahidi, F.4    Kim, S.K.5
  • 22
    • 1042289377 scopus 로고    scopus 로고
    • Antioxidant activity of egg-yolk protein hydrolysates in a linoleic acid oxidation system
    • Sakanaka, S.; Tachibana, Y.; Ishihara, N.; Juneja, L. R. Antioxidant activity of egg-yolk protein hydrolysates in a linoleic acid oxidation system. Food Chem. 2004, 86, 99-103.
    • (2004) Food Chem. , vol.86 , pp. 99-103
    • Sakanaka, S.1    Tachibana, Y.2    Ishihara, N.3    Juneja, L.R.4
  • 23
    • 0038000513 scopus 로고    scopus 로고
    • Combined effect of hydrogen peroxide induced, oxidative stress and, IL-I α on IL-8 production in CaCo-2 cells (a human colon carcinoma cell line) and normal, intestinal, epithelial, cells
    • Yamamoto, K.; Kushima, R.; Kisaki, O.; Fujiyama, Y.; Okabe, H. Combined effect of hydrogen peroxide induced, oxidative stress and, IL-I α on IL-8 production in CaCo-2 cells (a human colon carcinoma cell line) and normal, intestinal, epithelial, cells. Inflammation 2003, 27, 123-128.
    • (2003) Inflammation , vol.27 , pp. 123-128
    • Yamamoto, K.1    Kushima, R.2    Kisaki, O.3    Fujiyama, Y.4    Okabe, H.5
  • 24
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay, J. A.; Chin, S. M.; Linn, S. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 1988, 240, 640-642.
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 25
    • 0024448109 scopus 로고
    • Hydrogen peroxide enteritis: The "snow white" sign
    • Bilotta, J. J.; Waye, J. D. Hydrogen peroxide enteritis: the "snow white" sign. Gastrointest, Endoc. 1989, 35, 428-430.
    • (1989) Gastrointest, Endoc. , vol.35 , pp. 428-430
    • Bilotta, J.J.1    Waye, J.D.2
  • 26
    • 0023081945 scopus 로고    scopus 로고
    • The pig as a model for human nutrition
    • Miller, E. R.; Ullrey, D. E. The pig as a model for human nutrition. Annu. Rev. Nutr. 87, 7, 361-382.
    • Annu. Rev. Nutr. , vol.87 , Issue.7 , pp. 361-382
    • Miller, E.R.1    Ullrey, D.E.2
  • 27
    • 0036913250 scopus 로고    scopus 로고
    • A comparison of the Kjeldahl and Dumas methods for the determination of protein in foods, using data from a proficiency testing scheme
    • Thompson, M.; Owen, L.; Wilkinson, K.; Wood, R.; Damant, A. A comparison of the Kjeldahl and Dumas methods for the determination of protein in foods, using data from a proficiency testing scheme. Analyst 2002, 127, 1666-1668.
    • (2002) Analyst , vol.127 , pp. 1666-1668
    • Thompson, M.1    Owen, L.2    Wilkinson, K.3    Wood, R.4    Damant, A.5
  • 28
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G. R. Phosphorus assay in column chromatography, J. Biol. Chem. 1959, 234, 466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 29
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen, J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J. Aeric. Food Chem. 1979, 27, 1256-1262.
    • (1979) J. Aeric. Food Chem. , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 30
    • 0034697387 scopus 로고    scopus 로고
    • Superoxide produced by activated neutrophils efficiently reduces the tetrazolium salt, WST-I to produce a soluble formazan: A simple colorimetric assay for measuring respiratory burst activation and for screening anti-inflammatory agents
    • Tan, A. S.; Berridge, M. V. Superoxide produced by activated neutrophils efficiently reduces the tetrazolium salt, WST-I to produce a soluble formazan: a simple colorimetric assay for measuring respiratory burst activation and for screening anti-inflammatory agents. J. Immunol. Method, 2000, 238, 59-68.
    • (2000) J. Immunol. Method , vol.238 , pp. 59-68
    • Tan, A.S.1    Berridge, M.V.2
  • 31
    • 0021154370 scopus 로고
    • The energy equivalents of ATP and the energy values of food proteins and, fats
    • Livesey, G. The energy equivalents of ATP and the energy values of food proteins and, fats. Br. J. Nutr. 1984, 51, 15-28.
    • (1984) Br. J. Nutr. , vol.51 , pp. 15-28
    • Livesey, G.1
  • 32
    • 0034426765 scopus 로고    scopus 로고
    • Kinetic microassay for glutathione in cells plated on 96-well microtiter plates
    • Allen, S.; Shea, J. M.; Felmet, T.; Gadra, J.; Dehn, P. F. A, kinetic microassay for glutathione in cells plated on 96-well microtiter plates. methods Cell Sci. 2000, 22, 305-312.
    • (2000) Methods Cell Sci. , vol.22 , pp. 305-312
    • Allen, S.1    Shea, J.M.2    Felmet, T.3    Gadra, J.4    Dehn, P.F.A.5
  • 33
    • 0022300420 scopus 로고
    • Glutathione biosynthesis; γ-glutamylcysteine synthetase from, rat kidney
    • Seelig, G. F.; Meister, A. Glutathione biosynthesis; γ- glutamylcysteine synthetase from, rat kidney. Methods Enzymol, 1985, 113, 379-390.
    • (1985) Methods Enzymol , vol.113 , pp. 379-390
    • Seelig, G.F.1    Meister, A.2
  • 34
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • Krawetz, S., Misener, S., Eds.; Humana Press: Totowa, NJ
    • Rozen, S.; Skaletsky, H. J. Primer3 on the WWW for general users and for biologist programmers. In Bioinformatics Methods and Protocols: Methods in Molecular Biology; Krawetz, S., Misener, S., Eds.; Humana Press: Totowa, NJ, 2000; pp 365-386.
    • (2000) Bioinformatics Methods and Protocols: Methods in Molecular Biology , pp. 365-386
    • Rozen, S.1    Skaletsky, H.J.2
  • 35
    • 0023692586 scopus 로고
    • A spectrophotometric method for determination of catalase activity in small tissue samples
    • Johansson, L. H.; Borg, L. A. A spectrophotometric method for determination of catalase activity in small tissue samples. Anal. Biochem. 1988, 774, 331-336.
    • (1988) Anal. Biochem. , vol.774 , pp. 331-336
    • Johansson, L.H.1    Borg, L.A.2
  • 36
    • 0019740344 scopus 로고    scopus 로고
    • Glutathione peroxidase
    • Wendel, A. Glutathione peroxidase. Methods Enzumol. 77, 325-333.
    • Methods Enzumol. , vol.77 , pp. 325-333
    • Wendel, A.1
  • 38
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig, W. H.; Pabst, M. J.; Jakoby, W. B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 1974, 249, 7130-7139.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 39
    • 0025697262 scopus 로고
    • Malondialdehyde and thiobarbituric acid-reactivity as diagnostic indices of lipid peroxidation and peroxidative tissue injury
    • Janero, D. R. Malondialdehyde and thiobarbituric acid-reactivity as diagnostic indices of lipid peroxidation and peroxidative tissue injury. Free Radical biol. Med. 1990, 9, 515-540.
    • (1990) Free Radical Biol. Med. , vol.9 , pp. 515-540
    • Janero, D.R.1
  • 40
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine, R. L.; Williams, J. A.; Stadtman, E. R.; Shacter, E. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzvmol. 1994, 233, 346-357.
    • (1994) Methods Enzvmol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 41
    • 0015937146 scopus 로고
    • Alkyl isocyanates as active-site-specific reagents for serine proteases. Identification of the active-site serine as the site of reaction
    • Brown, W. E.; Wold, F. Alkyl isocyanates as active-site-specific reagents for serine proteases. Identification of the active-site serine as the site of reaction. Biochemistry 1973, 12, 835-840.
    • (1973) Biochemistry , vol.12 , pp. 835-840
    • Brown, W.E.1    Wold, F.2
  • 42
    • 0030933267 scopus 로고    scopus 로고
    • Response of pigs to bitter-tasting compounds
    • Nelson, S. L.; Sanregret, J. D. Response of pigs to bitter-tasting compounds. Chem. Senses 1997, 22, 129-132.
    • (1997) Chem. Senses , vol.22 , pp. 129-132
    • Nelson, S.L.1    Sanregret, J.D.2
  • 45
    • 0033231162 scopus 로고    scopus 로고
    • Biologic and pharmacologic regulation of mammalian glutathione synthesis
    • Griffith, O. W. Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radical Biol. Med. 1999, 27, 922-935.
    • (1999) Free Radical Biol. Med. , vol.27 , pp. 922-935
    • Griffith, O.W.1
  • 46
    • 17444424206 scopus 로고    scopus 로고
    • Intestinal glutathione: Determinant of mucosal peroxide transport, metabolism, and oxidative susceptibility
    • Aw, T. Y. Intestinal glutathione: determinant of mucosal peroxide transport, metabolism, and oxidative susceptibility. Toxicol, Appl. Pharmacol. 2005, 204, 320-328.
    • (2005) Toxicol, Appl. Pharmacol. , vol.204 , pp. 320-328
    • Aw, T.Y.1
  • 47
    • 0021187188 scopus 로고
    • Glutathione and GSH-dcpendent enzymes in the tumorous and nontumorous mucosa of the human colon and rectum
    • Siegers, C. P.; Bose-Younes, H.; Thies, E.; Hoppenkamps, R.; Younes, M. Glutathione and GSH-dcpendent enzymes in the tumorous and nontumorous mucosa of the human colon and rectum. J. Cancer. Res. Clin. Oncol. 1984, 107, 238-241.
    • (1984) J. Cancer. Res. Clin. Oncol. , vol.107 , pp. 238-241
    • Siegers, C.P.1    Bose-Younes, H.2    Thies, E.3    Hoppenkamps, R.4    Younes, M.5
  • 48
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge, W. Free radicals in the physiological control of cell function. Physiol. Rev. 2002, 82, 47-95.
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 49
    • 60849116096 scopus 로고    scopus 로고
    • Reactive species and disease: Fact, fiction, or filibuster?
    • Halliwell, B., Gutteridge, J. M. C., Eds.; Oxford University Press: New York
    • Halliwell, B.; Gutteridge, J. M. C. Reactive species and disease: fact, fiction, or filibuster? In Free Radicals in Biology and Medicine; Halliwell, B., Gutteridge, J. M. C., Eds.; Oxford University Press: New York, 2007; pp 488-613.
    • (2007) Free Radicals in Biology and Medicine , pp. 488-613
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 50
    • 0033643459 scopus 로고    scopus 로고
    • Antioxidant regulation of genes encoding enzymes that detoxify xenobiotics and carcinogens
    • Dhakshinamoorthy, S.; Long, D. J., 2nd; Jaiswal, A. K. Antioxidant regulation of genes encoding enzymes that detoxify xenobiotics and carcinogens. Curr. Ton. Cell, Regul, 2000, 36, 201-216.
    • (2000) Curr. Ton. Cell, Regul , vol.36 , pp. 201-216
    • Dhakshinamoorthy, S.1    Long II, D.J.2    Jaiswal, A.K.3
  • 51
    • 0034573074 scopus 로고    scopus 로고
    • Activation of antioxidant-response element (ARE), mitogen-activated protein kinases (MAPKs) and caspases by major green tea polyphenol components during cell survival and death
    • Chen, C.; Yu, R.; Owuor, E. D.; Kong, A. N. Activation of antioxidant-response element (ARE), mitogen-activated protein kinases (MAPKs) and caspases by major green tea polyphenol components during cell survival and death. Arch, Pharm. Res. 2000, 23, 605-612.
    • (2000) Arch, Pharm. Res. , vol.23 , pp. 605-612
    • Chen, C.1    Yu, R.2    Owuor, E.D.3    Kong, A.N.4
  • 52
    • 25144482448 scopus 로고    scopus 로고
    • Novel mechanisms of natural antioxidant compounds in biological systems: Involvement of glutathione and glutathione-related enzymes
    • Masella, R.; Di Benedetto, R.; Vari, R.; Filesi, C.; Giovannini, C. Novel mechanisms of natural antioxidant compounds in biological systems: involvement of glutathione and glutathione-related enzymes. J. Nutr. Biochem. 2005, 16, 577-586.
    • (2005) J. Nutr. Biochem. , vol.16 , pp. 577-586
    • Masella, R.1    Di Benedetto, R.2    Vari, R.3    Filesi, C.4    Giovannini, C.5
  • 53
    • 48349127906 scopus 로고    scopus 로고
    • Malondialdehyde and protein carbonyl as biomarkers for oxidative stress and disease progression in patients with chronic myeloid leukemia
    • Ahmad, R.; Tripathi, A. K.; Tripathi, P.; Singh, S.; Singh, R.; Singh, R. K. Malondialdehyde and protein carbonyl as biomarkers for oxidative stress and disease progression in patients with chronic myeloid leukemia. In Vivo 2008, 22, 525-528.
    • (2008) In Vivo , vol.22 , pp. 525-528
    • Ahmad, R.1    Tripathi, A.K.2    Tripathi, P.3    Singh, S.4    Singh, R.5    Singh, R.K.6
  • 54
    • 1342264317 scopus 로고    scopus 로고
    • Role of intestine in postsurgical complications: Involvement of free radicals
    • Thomas, S.; Balasubramanian, K. A. Role of intestine in postsurgical complications: involvement of free radicals. Free Radical Biol. Med. 2004, 36, 745-756.
    • (2004) Free Radical Biol. Med. , vol.36 , pp. 745-756
    • Thomas, S.1    Balasubramanian, K.A.2
  • 56
    • 2342644210 scopus 로고    scopus 로고
    • Molecular and integrative physiology of intestinal peptide transport
    • Daniel, H. Molecular and integrative physiology of intestinal peptide transport. Annu. Rev. Phvsiol. 2004, 66, 361-384.
    • (2004) Annu. Rev. Phvsiol. , vol.66 , pp. 361-384
    • Daniel, H.1
  • 57
    • 0033007311 scopus 로고    scopus 로고
    • Effect of chain length on absorption of biologically active peptides from, the gastrointestinal tract
    • Roberts, P. R.; Burney, J. D.; Black, K. W.; Zaloga, G. P. Effect of chain length on absorption of biologically active peptides from, the gastrointestinal tract. Digestion 1999, 60, 332-337.
    • (1999) Digestion , vol.60 , pp. 332-337
    • Roberts, P.R.1    Burney, J.D.2    Black, K.W.3    Zaloga, G.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.