메뉴 건너뛰기




Volumn 43, Issue 10, 2007, Pages 1439-1452

Cytoprotective properties of α-tocopherol are related to gene regulation in cultured d-galactosamine-treated human hepatocytes

Author keywords

Cell death; CPT1; CYP3A4; Free radicals; Hepatocytes; NF B; NOS 2; PPAR ; PXR; Tocopherol

Indexed keywords

ALPHA TOCOPHEROL; CARNITINE PALMITOYLTRANSFERASE; COLLAGENASE; GALACTOSAMINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; KETOCONAZOLE; NITRIC OXIDE SYNTHASE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; PREGNANE X RECEPTOR; RIFAMPICIN;

EID: 35148863166     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2007.07.023     Document Type: Article
Times cited : (24)

References (66)
  • 2
    • 0015963597 scopus 로고
    • Selective uridine triphosphate deficiency induced by d-galactosamine in liver and reversed by pyrimidine nucleotide precursors: effect on ribonucleic acid synthesis
    • Keppler D.O., Pausch J., and Decker K. Selective uridine triphosphate deficiency induced by d-galactosamine in liver and reversed by pyrimidine nucleotide precursors: effect on ribonucleic acid synthesis. J. Biol. Chem. 249 (1974) 211-216
    • (1974) J. Biol. Chem. , vol.249 , pp. 211-216
    • Keppler, D.O.1    Pausch, J.2    Decker, K.3
  • 4
    • 0016772868 scopus 로고
    • Early, reversible plasma membrane injury in galactosamine-induced liver cell death
    • El Mofty S.K., Scrutton M.C., Serroni A., Nicolini C., and Farber J.L. Early, reversible plasma membrane injury in galactosamine-induced liver cell death. Am. J. Pathol. 79 (1975) 579-595
    • (1975) Am. J. Pathol. , vol.79 , pp. 579-595
    • El Mofty, S.K.1    Scrutton, M.C.2    Serroni, A.3    Nicolini, C.4    Farber, J.L.5
  • 5
    • 0028008599 scopus 로고
    • Hepatic injury and lethal shock in galactosamine-sensitized mice induced by the superantigen staphylococcal enterotoxin B
    • Nagaki M., Muto Y., Ohnishi H., Yasuda S., Sano K., Naito T., Maeda T., Yamada T., and Moriwaki H. Hepatic injury and lethal shock in galactosamine-sensitized mice induced by the superantigen staphylococcal enterotoxin B. Gastroenterology 106 (1994) 450-458
    • (1994) Gastroenterology , vol.106 , pp. 450-458
    • Nagaki, M.1    Muto, Y.2    Ohnishi, H.3    Yasuda, S.4    Sano, K.5    Naito, T.6    Maeda, T.7    Yamada, T.8    Moriwaki, H.9
  • 9
    • 0037212020 scopus 로고    scopus 로고
    • Evaluation of oxidative stress during apoptosis and necrosis caused by d-galactosamine in rat liver
    • Sun F., Hamagawa E., Tsutsui C., Sakaguchi N., Kakuta Y., Tokumaru S., and Kojo S. Evaluation of oxidative stress during apoptosis and necrosis caused by d-galactosamine in rat liver. Biochem. Pharmacol. 65 (2003) 101-107
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 101-107
    • Sun, F.1    Hamagawa, E.2    Tsutsui, C.3    Sakaguchi, N.4    Kakuta, Y.5    Tokumaru, S.6    Kojo, S.7
  • 10
    • 0030052324 scopus 로고    scopus 로고
    • Protective effect of S-adenosyl-l-methionine on bromobenzene- and d-galactosamine-induced toxicity to isolated rat hepatocytes
    • Wu J., Soderbergh H., Karlsson K., and Danielsson A. Protective effect of S-adenosyl-l-methionine on bromobenzene- and d-galactosamine-induced toxicity to isolated rat hepatocytes. Hepatology 23 (1996) 359-365
    • (1996) Hepatology , vol.23 , pp. 359-365
    • Wu, J.1    Soderbergh, H.2    Karlsson, K.3    Danielsson, A.4
  • 11
    • 0032736328 scopus 로고    scopus 로고
    • Involvement of oxidative DNA damage and apoptosis in antitumor actions of aminosugars
    • Hiraku Y., and Kawanishi S. Involvement of oxidative DNA damage and apoptosis in antitumor actions of aminosugars. Free Radic. Res. 31 (1999) 389-403
    • (1999) Free Radic. Res. , vol.31 , pp. 389-403
    • Hiraku, Y.1    Kawanishi, S.2
  • 12
  • 13
    • 10644242646 scopus 로고    scopus 로고
    • PGE1-induced NO reduces apoptosis by d-galactosamine through attenuation of NF-kappaB and NOS-2 expression in rat hepatocytes
    • Siendones E., Fouad D., Diaz-Guerra M.J., De la Mata M., Bosca L., and Muntane J. PGE1-induced NO reduces apoptosis by d-galactosamine through attenuation of NF-kappaB and NOS-2 expression in rat hepatocytes. Hepatology 40 (2004) 1295-1303
    • (2004) Hepatology , vol.40 , pp. 1295-1303
    • Siendones, E.1    Fouad, D.2    Diaz-Guerra, M.J.3    De la Mata, M.4    Bosca, L.5    Muntane, J.6
  • 16
    • 0027292287 scopus 로고
    • Molecular pharmacology of vitamin E: structural aspects of antioxidant activity
    • van Acker S.A., Koymans L.M., and Bast A. Molecular pharmacology of vitamin E: structural aspects of antioxidant activity. Free Radic. Biol. Med. 15 (1993) 311-328
    • (1993) Free Radic. Biol. Med. , vol.15 , pp. 311-328
    • van Acker, S.A.1    Koymans, L.M.2    Bast, A.3
  • 17
    • 0242363202 scopus 로고    scopus 로고
    • Role of lipid peroxidation as a mechanism of liver injury after acetaminophen overdose in mice
    • Knight T.R., Fariss M.W., Farhood A., and Jaeschke H. Role of lipid peroxidation as a mechanism of liver injury after acetaminophen overdose in mice. Toxicol. Sci. 76 (2003) 229-236
    • (2003) Toxicol. Sci. , vol.76 , pp. 229-236
    • Knight, T.R.1    Fariss, M.W.2    Farhood, A.3    Jaeschke, H.4
  • 19
    • 0032416487 scopus 로고    scopus 로고
    • Effect of dietary vitamin E on antioxidant status and antioxidant enzyme activities in Sprague-Dawley rats
    • Lii C.K., Ko Y.J., Chiang M.T., Sung W.C., and Chen H.W. Effect of dietary vitamin E on antioxidant status and antioxidant enzyme activities in Sprague-Dawley rats. Nutr. Cancer 32 (1998) 95-100
    • (1998) Nutr. Cancer , vol.32 , pp. 95-100
    • Lii, C.K.1    Ko, Y.J.2    Chiang, M.T.3    Sung, W.C.4    Chen, H.W.5
  • 21
    • 0031976862 scopus 로고    scopus 로고
    • Human plasma and tissue alpha-tocopherol concentrations in response to supplementation with deuterated natural and synthetic vitamin E
    • Burton G.W., Traber M.G., Acuff R.V., Walters D.N., Kayden H., Hughes L., and Ingold K.U. Human plasma and tissue alpha-tocopherol concentrations in response to supplementation with deuterated natural and synthetic vitamin E. Am. J. Clin. Nutr. 67 (1998) 669-684
    • (1998) Am. J. Clin. Nutr. , vol.67 , pp. 669-684
    • Burton, G.W.1    Traber, M.G.2    Acuff, R.V.3    Walters, D.N.4    Kayden, H.5    Hughes, L.6    Ingold, K.U.7
  • 22
    • 0019941886 scopus 로고
    • First proof that vitamin E is major lipid-soluble, chain-breaking antioxidant in human blood plasma
    • Burton G.W., Joyce A., and Ingold K.U. First proof that vitamin E is major lipid-soluble, chain-breaking antioxidant in human blood plasma. Lancet 2 (1982) 327
    • (1982) Lancet , vol.2 , pp. 327
    • Burton, G.W.1    Joyce, A.2    Ingold, K.U.3
  • 25
    • 0037067711 scopus 로고    scopus 로고
    • Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism: novel mechanism of regulation of vitamin E status
    • Sontag T.J., and Parker R.S. Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism: novel mechanism of regulation of vitamin E status. J. Biol. Chem. 277 (2002) 25290-25296
    • (2002) J. Biol. Chem. , vol.277 , pp. 25290-25296
    • Sontag, T.J.1    Parker, R.S.2
  • 26
    • 0036791124 scopus 로고    scopus 로고
    • Identities and differences in the metabolism of tocotrienols and tocopherols in HepG2 cells
    • Birringer M., Pfluger P., Kluth D., Landes N., and Brigelius-Flohe R. Identities and differences in the metabolism of tocotrienols and tocopherols in HepG2 cells. J. Nutr. 132 (2002) 3113-3118
    • (2002) J. Nutr. , vol.132 , pp. 3113-3118
    • Birringer, M.1    Pfluger, P.2    Kluth, D.3    Landes, N.4    Brigelius-Flohe, R.5
  • 28
    • 0027146004 scopus 로고
    • Effect of vitamin E dietary intake on in vitro activation of aflatoxin B1
    • Cassand P., Decoudu S., Leveque F., Daubeze M., and Narbonne J.F. Effect of vitamin E dietary intake on in vitro activation of aflatoxin B1. Mutat. Res. 319 (1993) 309-316
    • (1993) Mutat. Res. , vol.319 , pp. 309-316
    • Cassand, P.1    Decoudu, S.2    Leveque, F.3    Daubeze, M.4    Narbonne, J.F.5
  • 30
    • 0028585920 scopus 로고
    • Sequence of the 5′-flanking region of CYP3A5: comparative analysis with CYP3A4 and CYP3A7
    • Jounaidi Y., Guzelian P.S., Maurel P., and Vilarem M.J. Sequence of the 5′-flanking region of CYP3A5: comparative analysis with CYP3A4 and CYP3A7. Biochem. Biophys. Res. Commun. 205 (1994) 1741-1747
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1741-1747
    • Jounaidi, Y.1    Guzelian, P.S.2    Maurel, P.3    Vilarem, M.J.4
  • 33
    • 0033983850 scopus 로고    scopus 로고
    • A rapid method for the extraction and determination of vitamin E metabolites in human urine
    • Lodge J.K., Traber M.G., Elsner A., and Brigelius-Flohé R. A rapid method for the extraction and determination of vitamin E metabolites in human urine. J. Lipid Res. 41 (2000) 148-154
    • (2000) J. Lipid Res. , vol.41 , pp. 148-154
    • Lodge, J.K.1    Traber, M.G.2    Elsner, A.3    Brigelius-Flohé, R.4
  • 35
    • 0036791124 scopus 로고    scopus 로고
    • Identities and differences in the metabolism of tocotrienols and tocopherols in HepG2 cells
    • Birringer M., Pfluger P., Kluth D., Landes N., and Brigelius-Flohé R. Identities and differences in the metabolism of tocotrienols and tocopherols in HepG2 cells. J. Nutr. 132 (2002) 3113-3118
    • (2002) J. Nutr. , vol.132 , pp. 3113-3118
    • Birringer, M.1    Pfluger, P.2    Kluth, D.3    Landes, N.4    Brigelius-Flohé, R.5
  • 36
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(- Delta Delta C(T)) method
    • Livak K.J., and Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(- Delta Delta C(T)) method. Methods 25 (2001) 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 37
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells
    • Schreiber E., Matthias P., Muller M.M., and Schaffner W. Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. Nucleic Acids Res. 17 (1989) 6419
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 38
    • 0036293621 scopus 로고    scopus 로고
    • Reduced glutathione depletion causes necrosis and sensitization to tumor necrosis factor-alpha-induced apoptosis in cultured mouse hepatocytes
    • Nagai H., Matsumaru K., Feng G., and Kaplowitz N. Reduced glutathione depletion causes necrosis and sensitization to tumor necrosis factor-alpha-induced apoptosis in cultured mouse hepatocytes. Hepatology 36 (2002) 55-64
    • (2002) Hepatology , vol.36 , pp. 55-64
    • Nagai, H.1    Matsumaru, K.2    Feng, G.3    Kaplowitz, N.4
  • 39
    • 3142754211 scopus 로고    scopus 로고
    • Role of NF-kappaB activation and nitric oxide expression during PGE protection against d-galactosamine-induced cell death in cultured rat hepatocytes
    • Fouad D., Siendones E., Costan G., and Muntane J. Role of NF-kappaB activation and nitric oxide expression during PGE protection against d-galactosamine-induced cell death in cultured rat hepatocytes. Liver Int. 24 (2004) 227-236
    • (2004) Liver Int. , vol.24 , pp. 227-236
    • Fouad, D.1    Siendones, E.2    Costan, G.3    Muntane, J.4
  • 40
    • 0035879776 scopus 로고    scopus 로고
    • Tocopherols are metabolized in HepG2 cells by side chain omega-oxidation and consecutive beta-oxidation
    • Birringer M., Drogan D., and Brigelius-Flohe R. Tocopherols are metabolized in HepG2 cells by side chain omega-oxidation and consecutive beta-oxidation. Free Radic. Biol. Med. 31 (2001) 226-232
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 226-232
    • Birringer, M.1    Drogan, D.2    Brigelius-Flohe, R.3
  • 41
    • 0034597750 scopus 로고    scopus 로고
    • Cytochrome P4503A-dependent metabolism of tocopherols and inhibition by sesamin
    • Parker R.S., Sontag T.J., and Swanson J.E. Cytochrome P4503A-dependent metabolism of tocopherols and inhibition by sesamin. Biochem. Biophys. Res. Commun. 277 (2000) 531-534
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , pp. 531-534
    • Parker, R.S.1    Sontag, T.J.2    Swanson, J.E.3
  • 42
    • 33750722500 scopus 로고    scopus 로고
    • A temporal study on the histopathological, biochemical and molecular responses of CCl(4)-induced hepatotoxicity in Cyp2e1-null mice
    • Avasarala S., Yang L., Sun Y., Leung A.W., Chan W.Y., Cheung W.T., and Lee S.S. A temporal study on the histopathological, biochemical and molecular responses of CCl(4)-induced hepatotoxicity in Cyp2e1-null mice. Toxicology 228 (2006) 310-322
    • (2006) Toxicology , vol.228 , pp. 310-322
    • Avasarala, S.1    Yang, L.2    Sun, Y.3    Leung, A.W.4    Chan, W.Y.5    Cheung, W.T.6    Lee, S.S.7
  • 45
    • 0016772868 scopus 로고
    • Early, reversible plasma membrane injury in galactosamine-induced liver cell death
    • El-Mofty S.K., Scrutton M.C., Serroni A., Nicolini C., and Farber J.L. Early, reversible plasma membrane injury in galactosamine-induced liver cell death. Am. J. Pathol. 79 (1975) 579-595
    • (1975) Am. J. Pathol. , vol.79 , pp. 579-595
    • El-Mofty, S.K.1    Scrutton, M.C.2    Serroni, A.3    Nicolini, C.4    Farber, J.L.5
  • 46
    • 0028008599 scopus 로고
    • Hepatic injury and lethal shock in galactosamine-sensitized mice induced by the superantigen staphylococcal enterotoxin B
    • Nagaki M., Muto Y., Ohnishi H., Yasuda S., Sano K., Naito T., Maeda T., Yamada T., and Moriwaki H. Hepatic injury and lethal shock in galactosamine-sensitized mice induced by the superantigen staphylococcal enterotoxin B. Gastroenterology 106 (1994) 450-458
    • (1994) Gastroenterology , vol.106 , pp. 450-458
    • Nagaki, M.1    Muto, Y.2    Ohnishi, H.3    Yasuda, S.4    Sano, K.5    Naito, T.6    Maeda, T.7    Yamada, T.8    Moriwaki, H.9
  • 47
    • 0021995204 scopus 로고
    • Toxicity of d-galactosamine for rat hepatocytes in monolayer culture
    • Tran-Thi T.A., Phillips J., Falk H., and Decker K. Toxicity of d-galactosamine for rat hepatocytes in monolayer culture. Exp. Mol. Pathol. 42 (1985) 89-116
    • (1985) Exp. Mol. Pathol. , vol.42 , pp. 89-116
    • Tran-Thi, T.A.1    Phillips, J.2    Falk, H.3    Decker, K.4
  • 48
    • 0033230646 scopus 로고    scopus 로고
    • Attenuation of endogenous oxidative stress-induced cell death by cytochrome P450 inhibitors in primary cultures of rat hepatocytes
    • Shiba D., and Shimamoto N. Attenuation of endogenous oxidative stress-induced cell death by cytochrome P450 inhibitors in primary cultures of rat hepatocytes. Free Radic. Biol. Med. 27 (1999) 1019-1026
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 1019-1026
    • Shiba, D.1    Shimamoto, N.2
  • 49
    • 0028788763 scopus 로고
    • Role of oxidative stress generated from the mitochondrial electron transport chain and mitochondrial glutathione status in loss of mitochondrial function and activation of transcription factor nuclear factor-kappa B: studies with isolated mitochondria and rat hepatocytes
    • Garcia-Ruiz C., Colell A., Morales A., Kaplowitz N., and Fernandez-Checa J.C. Role of oxidative stress generated from the mitochondrial electron transport chain and mitochondrial glutathione status in loss of mitochondrial function and activation of transcription factor nuclear factor-kappa B: studies with isolated mitochondria and rat hepatocytes. Mol. Pharmacol. 48 (1995) 825-834
    • (1995) Mol. Pharmacol. , vol.48 , pp. 825-834
    • Garcia-Ruiz, C.1    Colell, A.2    Morales, A.3    Kaplowitz, N.4    Fernandez-Checa, J.C.5
  • 50
    • 0035078341 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) mediates the mitochondrial-dependent apoptosis induced by transforming growth factor (beta) in fetal hepatocytes
    • Herrera B., Alvarez A.M., Sanchez A., Fernandez M., Roncero C., Benito M., and Fabregat I. Reactive oxygen species (ROS) mediates the mitochondrial-dependent apoptosis induced by transforming growth factor (beta) in fetal hepatocytes. FASEB J. 15 (2001) 741-751
    • (2001) FASEB J. , vol.15 , pp. 741-751
    • Herrera, B.1    Alvarez, A.M.2    Sanchez, A.3    Fernandez, M.4    Roncero, C.5    Benito, M.6    Fabregat, I.7
  • 51
    • 0035129976 scopus 로고    scopus 로고
    • Bile acid-induced rat hepatocyte apoptosis is inhibited by antioxidants and blockers of the mitochondrial permeability transition
    • Yerushalmi B., Dahl R., Devereaux M.W., Gumpricht E., and Sokol R.J. Bile acid-induced rat hepatocyte apoptosis is inhibited by antioxidants and blockers of the mitochondrial permeability transition. Hepatology 33 (2001) 616-626
    • (2001) Hepatology , vol.33 , pp. 616-626
    • Yerushalmi, B.1    Dahl, R.2    Devereaux, M.W.3    Gumpricht, E.4    Sokol, R.J.5
  • 52
    • 0032054683 scopus 로고    scopus 로고
    • The role of nitric oxide in hepatic metabolism
    • Alexander B. The role of nitric oxide in hepatic metabolism. Nutrition 14 (1998) 376-390
    • (1998) Nutrition , vol.14 , pp. 376-390
    • Alexander, B.1
  • 53
    • 0033027841 scopus 로고    scopus 로고
    • Nitric oxide in liver injury
    • Clemens M.G. Nitric oxide in liver injury. Hepatology 30 (1999) 1-5
    • (1999) Hepatology , vol.30 , pp. 1-5
    • Clemens, M.G.1
  • 54
    • 0032528866 scopus 로고    scopus 로고
    • alpha-Tocopherol specifically inactivates cellular protein kinase C alpha by changing its phosphorylation state
    • Ricciarelli R., Tasinato A., Clement S., Ozer N.K., Boscoboinik D., and Azzi A. alpha-Tocopherol specifically inactivates cellular protein kinase C alpha by changing its phosphorylation state. Biochem. J. 334 (1998) 243-249
    • (1998) Biochem. J. , vol.334 , pp. 243-249
    • Ricciarelli, R.1    Tasinato, A.2    Clement, S.3    Ozer, N.K.4    Boscoboinik, D.5    Azzi, A.6
  • 55
    • 0032484209 scopus 로고    scopus 로고
    • alpha-Tocopherol inhibits the respiratory burst in human monocytes: attenuation of p47(phox) membrane translocation and phosphorylation
    • Cachia O., Benna J.E., Pedruzzi E., Descomps B., Gougerot-Pocidalo M.A., and Leger C.L. alpha-Tocopherol inhibits the respiratory burst in human monocytes: attenuation of p47(phox) membrane translocation and phosphorylation. J. Biol. Chem. 273 (1998) 32801-32805
    • (1998) J. Biol. Chem. , vol.273 , pp. 32801-32805
    • Cachia, O.1    Benna, J.E.2    Pedruzzi, E.3    Descomps, B.4    Gougerot-Pocidalo, M.A.5    Leger, C.L.6
  • 56
    • 0033594810 scopus 로고    scopus 로고
    • PPARalpha activators inhibit cytokine-induced vascular cell adhesion molecule-1 expression in human endothelial cells
    • Marx N., Sukhova G.K., Collins T., Libby P., and Plutzky J. PPARalpha activators inhibit cytokine-induced vascular cell adhesion molecule-1 expression in human endothelial cells. Circulation 99 (1999) 3125-3131
    • (1999) Circulation , vol.99 , pp. 3125-3131
    • Marx, N.1    Sukhova, G.K.2    Collins, T.3    Libby, P.4    Plutzky, J.5
  • 57
    • 0030922247 scopus 로고    scopus 로고
    • Repression of interleukin-6 gene expression by 17 beta-estradiol: inhibition of the DNA-binding activity of the transcription factors NF-IL6 and NF-kappa B by the estrogen receptor
    • Ray P., Ghosh S.K., Zhang D.H., and Ray A. Repression of interleukin-6 gene expression by 17 beta-estradiol: inhibition of the DNA-binding activity of the transcription factors NF-IL6 and NF-kappa B by the estrogen receptor. FEBS Lett. 409 (1997) 79-85
    • (1997) FEBS Lett. , vol.409 , pp. 79-85
    • Ray, P.1    Ghosh, S.K.2    Zhang, D.H.3    Ray, A.4
  • 59
    • 0034034671 scopus 로고    scopus 로고
    • Central role of peroxisome proliferator-activated receptors in the actions of peroxisome proliferators
    • Corton J.C., Anderson S.P., and Stauber A. Central role of peroxisome proliferator-activated receptors in the actions of peroxisome proliferators. Annu. Rev. Pharmacol. Toxicol. 40 (2000) 491-518
    • (2000) Annu. Rev. Pharmacol. Toxicol. , vol.40 , pp. 491-518
    • Corton, J.C.1    Anderson, S.P.2    Stauber, A.3
  • 60
    • 0024509605 scopus 로고
    • Biochemical mechanisms of induction of hepatic peroxisome proliferation
    • Lock E.A., Mitchell A.M., and Elcombe C.R. Biochemical mechanisms of induction of hepatic peroxisome proliferation. Annu. Rev. Pharmacol. Toxicol. 29 (1989) 145-163
    • (1989) Annu. Rev. Pharmacol. Toxicol. , vol.29 , pp. 145-163
    • Lock, E.A.1    Mitchell, A.M.2    Elcombe, C.R.3
  • 61
    • 0031819433 scopus 로고    scopus 로고
    • Evidence for the suppression of apoptosis by the peroxisome proliferator activated receptor alpha (PPAR alpha)
    • Roberts R.A., James N.H., Woodyatt N.J., Macdonald N., and Tugwood J.D. Evidence for the suppression of apoptosis by the peroxisome proliferator activated receptor alpha (PPAR alpha). Carcinogenesis 19 (1998) 43-48
    • (1998) Carcinogenesis , vol.19 , pp. 43-48
    • Roberts, R.A.1    James, N.H.2    Woodyatt, N.J.3    Macdonald, N.4    Tugwood, J.D.5
  • 62
    • 0031695507 scopus 로고    scopus 로고
    • Regulation of apoptosis in mouse hepatocytes and alteration of apoptosis by nongenotoxic carcinogens
    • Christensen J.G., Gonzales A.J., Cattley R.C., and Goldsworthy T.L. Regulation of apoptosis in mouse hepatocytes and alteration of apoptosis by nongenotoxic carcinogens. Cell Growth Differ. 9 (1998) 815-825
    • (1998) Cell Growth Differ. , vol.9 , pp. 815-825
    • Christensen, J.G.1    Gonzales, A.J.2    Cattley, R.C.3    Goldsworthy, T.L.4
  • 65
    • 0032169485 scopus 로고    scopus 로고
    • The human orphan nuclear receptor PXR is activated by compounds that regulate CYP3A4 gene expression and cause drug interactions
    • Lehmann J.M., McKee D.D., Watson M.A., Willson T.M., Moore J.T., and Kliewer S.A. The human orphan nuclear receptor PXR is activated by compounds that regulate CYP3A4 gene expression and cause drug interactions. J. Clin. Invest. 102 (1998) 1016-1023
    • (1998) J. Clin. Invest. , vol.102 , pp. 1016-1023
    • Lehmann, J.M.1    McKee, D.D.2    Watson, M.A.3    Willson, T.M.4    Moore, J.T.5    Kliewer, S.A.6
  • 66
    • 0033499242 scopus 로고    scopus 로고
    • Improving the nutrient composition of plants to enhance human nutrition and health
    • Grusak M.A., and DellaPenna D. Improving the nutrient composition of plants to enhance human nutrition and health. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50 (1999) 133-161
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 133-161
    • Grusak, M.A.1    DellaPenna, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.