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Volumn 39, Issue 5, 2006, Pages 479-491

Heme oxygenase-1 as a potential therapeutic target for hepatoprotection

Author keywords

Chemoprevention; Heme oxygenase 1; Hepatoprotective agents; Hepatotoxicants; Liver damage; Transcription factors

Indexed keywords

MAMMALIA;

EID: 33750838526     PISSN: 12258687     EISSN: 12258687     Source Type: Journal    
DOI: 10.5483/bmbrep.2006.39.5.479     Document Type: Review
Times cited : (197)

References (146)
  • 1
    • 0034306862 scopus 로고    scopus 로고
    • Cadmium-induced mRNA expression of Hsp32 is augmented in metallothionein-I and -II knock-out mice
    • Abe, T., Yamamoto, O., Gotoh, S., Yan, Y., Todaka, N. and Higashi, K. (2000) Cadmium-induced mRNA expression of Hsp32 is augmented in metallothionein-I and -II knock-out mice. Arch. Biochem. Biophys. 382, 81-88.
    • (2000) Arch. Biochem. Biophys. , vol.382 , pp. 81-88
    • Abe, T.1    Yamamoto, O.2    Gotoh, S.3    Yan, Y.4    Todaka, N.5    Higashi, K.6
  • 2
    • 0024516371 scopus 로고
    • Transcriptional activation of the heme oxygenase gene by heme and cadmium in mouse hepatoma cells
    • Alam, J., Shibahara, S. and Smith, A. (1989) Transcriptional activation of the heme oxygenase gene by heme and cadmium in mouse hepatoma cells. J. Biol. Chem. 264, 6371-6375.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6371-6375
    • Alam, J.1    Shibahara, S.2    Smith, A.3
  • 3
    • 12344322514 scopus 로고    scopus 로고
    • Differential expression of mouse hepatic transporter genes in response to acetaminophen and carbon tetrachloride
    • Aleksunes, L. M., Slitt, A. M., Cherrington, N. J., Thibodeau, M. S., Klaassen, C. D. and Manautou, J. E. (2005) Differential expression of mouse hepatic transporter genes in response to acetaminophen and carbon tetrachloride. Toxicol. Sci. 83, 44-52.
    • (2005) Toxicol. Sci. , vol.83 , pp. 44-52
    • Aleksunes, L.M.1    Slitt, A.M.2    Cherrington, N.J.3    Thibodeau, M.S.4    Klaassen, C.D.5    Manautou, J.E.6
  • 6
    • 0030008030 scopus 로고    scopus 로고
    • Demonstration of halothane-induced hepatic lipid peroxidation in rats by quantification of F2-isoprostanes
    • nd and Franks J. J. (1996). Demonstration of halothane-induced hepatic lipid peroxidation in rats by quantification of F2-isoprostanes. Anesthesiology. 84, 910-916.
    • (1996) Anesthesiology , vol.84 , pp. 910-916
    • Awad, J.A.1    Horn, J.L.2    Roberts II, L.J.3    Franks, J.J.4
  • 9
    • 0033845823 scopus 로고    scopus 로고
    • Transcriptional activation of heme oxygenase-1 and its functional significance in acetaminophen-induced hepatitis and hepatocellular injury in the rat
    • Bauer, I., Vollmar, B., Jaeschke, H., Rensing, H., Kraemer, T., Larsen, R. and Bauer, M. (2000) Transcriptional activation of heme oxygenase-1 and its functional significance in acetaminophen-induced hepatitis and hepatocellular injury in the rat. J. Hepatol. 33, 395-406.
    • (2000) J. Hepatol. , vol.33 , pp. 395-406
    • Bauer, I.1    Vollmar, B.2    Jaeschke, H.3    Rensing, H.4    Kraemer, T.5    Larsen, R.6    Bauer, M.7
  • 12
    • 0037124078 scopus 로고    scopus 로고
    • Heme oxygenase-1-derived carbon monoxide requires the activation of transcription factor NF-kappa B to protect endothelial cells from tumor necrosis factor-alpha-mediated apoptosis
    • Brouard, S., Berberat, P. O., Tobiasch, E., Seldon, M. P., Bach, F. H. and Soares, M. P. (2002) Heme oxygenase-1-derived carbon monoxide requires the activation of transcription factor NF-kappa B to protect endothelial cells from tumor necrosis factor-alpha-mediated apoptosis. J. Biol. Chem. 277, 17950-17961.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17950-17961
    • Brouard, S.1    Berberat, P.O.2    Tobiasch, E.3    Seldon, M.P.4    Bach, F.H.5    Soares, M.P.6
  • 13
    • 0030813934 scopus 로고    scopus 로고
    • Dimethylarsenic acid treatment alters six different rat biochemical parameters: Relevance to arsenic carcinogenesis
    • Brown, J. L., Kitchin, K. T. and George M. (1997) Dimethylarsenic acid treatment alters six different rat biochemical parameters: relevance to arsenic carcinogenesis. Teratog. Carcinog. Mutagen. 17, 71-84.
    • (1997) Teratog. Carcinog. Mutagen. , vol.17 , pp. 71-84
    • Brown, J.L.1    Kitchin, K.T.2    George, M.3
  • 14
    • 0023490534 scopus 로고
    • Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase
    • Brune, B. and Ullrich, V. (1987) Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase. Mol. Pharmacol. 32, 497-504.
    • (1987) Mol. Pharmacol. , vol.32 , pp. 497-504
    • Brune, B.1    Ullrich, V.2
  • 15
    • 19744373984 scopus 로고    scopus 로고
    • Glutathione depletion and anaesthesia in mice alter heme and drug metabolizing enzymes
    • Buzaleh, A. M. and Batlle, A. M. (2005) Glutathione depletion and anaesthesia in mice alter heme and drug metabolizing enzymes. Biochim. Biophys. Acta. 1723, 128-134.
    • (2005) Biochim. Biophys. Acta , vol.1723 , pp. 128-134
    • Buzaleh, A.M.1    Batlle, A.M.2
  • 16
    • 0029858594 scopus 로고    scopus 로고
    • The tumor promoter arsenite stimulates AP-1 activity by inhibiting a JNK phosphatase
    • Cavigelli, M., Li, W. W., Lin, A., Su, B., Yoshioka, K. and Karin, M. (1996) The tumor promoter arsenite stimulates AP-1 activity by inhibiting a JNK phosphatase. EMBO J. 15, 6269-6279.
    • (1996) EMBO J. , vol.15 , pp. 6269-6279
    • Cavigelli, M.1    Li, W.W.2    Lin, A.3    Su, B.4    Yoshioka, K.5    Karin, M.6
  • 18
    • 5344220933 scopus 로고    scopus 로고
    • Induction of detoxifying enzymes by garlic organosulfur compounds through transcription factor Nrf2: Effect of chemical structure and stress signals
    • Chen, C., Pung, D., Leong, V., Hebbar, V., Shen, G., Nair, S., Li, W. and Kong, A. N. (2004) Induction of detoxifying enzymes by garlic organosulfur compounds through transcription factor Nrf2: effect of chemical structure and stress signals. Free Radic. Biol. Med. 37, 1578-1590.
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 1578-1590
    • Chen, C.1    Pung, D.2    Leong, V.3    Hebbar, V.4    Shen, G.5    Nair, S.6    Li, W.7    Kong, A.N.8
  • 19
    • 16644385572 scopus 로고    scopus 로고
    • Heme oxygenase-1 protects against apoptosis induced by tumor necrosis factor-alpha and cycloheximide in papillary thyroid carcinoma cells
    • Chen, G. G., Liu, Z. M., Vlantis, A. C, Tse, G. M., Leung, B. C. and van Hasselt, C. A. (2004) Heme oxygenase-1 protects against apoptosis induced by tumor necrosis factor-alpha and cycloheximide in papillary thyroid carcinoma cells. J. Cell. Biochem. 92, 1246-1256.
    • (2004) J. Cell. Biochem. , vol.92 , pp. 1246-1256
    • Chen, G.G.1    Liu, Z.M.2    Vlantis, A.C.3    Tse, G.M.4    Leung, B.C.5    Van Hasselt, C.A.6
  • 20
    • 0036607095 scopus 로고    scopus 로고
    • Differential induction of heme oxygenase-1 in macrophages and hepatocytes during acetaminophen-induced hepatotoxicity in the rat: Effects of hemin and biliverdin
    • Chiu, H., Brittingham, J. A. and Laskin, D. L. (2002) Differential induction of heme oxygenase-1 in macrophages and hepatocytes during acetaminophen-induced hepatotoxicity in the rat: effects of hemin and biliverdin. Toxicol. Appl. Pharmacol. 181, 106-115.
    • (2002) Toxicol. Appl. Pharmacol. , vol.181 , pp. 106-115
    • Chiu, H.1    Brittingham, J.A.2    Laskin, D.L.3
  • 21
    • 0036190993 scopus 로고    scopus 로고
    • Enhanced heme oxygenase activity increases the antioxidant defense capacity of guinea pig liver upon acute cobalt chloride loading: Comparison with rat liver
    • Christova, T. Y., Duridanova, D. B. and Setchenska, M. S. (2002) Enhanced heme oxygenase activity increases the antioxidant defense capacity of guinea pig liver upon acute cobalt chloride loading: comparison with rat liver. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 131, 177-184.
    • (2002) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.131 , pp. 177-184
    • Christova, T.Y.1    Duridanova, D.B.2    Setchenska, M.S.3
  • 23
    • 0024439390 scopus 로고
    • Cytochrome P-450, reductive metabolism, and cell injury
    • De Groot, H. and Sies, H. (1989) Cytochrome P-450, reductive metabolism, and cell injury. Drug Metab. Rev. 20, 275-284.
    • (1989) Drug Metab. Rev. , vol.20 , pp. 275-284
    • De Groot, H.1    Sies, H.2
  • 24
    • 14344252035 scopus 로고    scopus 로고
    • Heme oxygenase-1 induction in hepatocytes and non-parenchymal cells protects against liver injury during endotoxemia
    • Dorman, R. B., Bajt, M. L., Farhood, A., Mayes, J. and Jaeschke, H. (2004) Heme oxygenase-1 induction in hepatocytes and non-parenchymal cells protects against liver injury during endotoxemia. Comp. Hepatol. 3, 42.
    • (2004) Comp. Hepatol. , vol.3 , pp. 42
    • Dorman, R.B.1    Bajt, M.L.2    Farhood, A.3    Mayes, J.4    Jaeschke, H.5
  • 25
    • 14344252633 scopus 로고    scopus 로고
    • Cobalt protoporphyrin protects against hepatic parenchymal injury and microvascular dysfunction during experimental rhabdomyolysis
    • Dorman, R. B., Wunder, C. and Brock, R. W. (2005) Cobalt protoporphyrin protects against hepatic parenchymal injury and microvascular dysfunction during experimental rhabdomyolysis. Shock. 23, 275-280.
    • (2005) Shock , vol.23 , pp. 275-280
    • Dorman, R.B.1    Wunder, C.2    Brock, R.W.3
  • 26
    • 0025969686 scopus 로고
    • Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron
    • Eisenstein, R. S., Garcia-Mayol, D., Pettingell, W. and Munro, H. N. (1991) Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron. Proc. Natl. Acad. Sci. USA 88, 688-692.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 688-692
    • Eisenstein, R.S.1    Garcia-Mayol, D.2    Pettingell, W.3    Munro, H.N.4
  • 27
    • 0032502738 scopus 로고    scopus 로고
    • Mechanism of sodium arsenite-mediated induction of heme oxygenase-1 in hepatoma cells. Role of mitogenactivated protein kinases
    • Elbirt, K. K., Whitmarsh, A. J., Davis, R. J. and Bonkovsky, H. L. (1998) Mechanism of sodium arsenite-mediated induction of heme oxygenase-1 in hepatoma cells. Role of mitogenactivated protein kinases. J. Biol. Chem. 273, 8922-8931.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8922-8931
    • Elbirt, K.K.1    Whitmarsh, A.J.2    Davis, R.J.3    Bonkovsky, H.L.4
  • 28
    • 1442326158 scopus 로고    scopus 로고
    • Antiapoptotic role of heme oxygenase (HO) and the potential of HO as a target in anticancer treatment
    • Fang, J., Akaike, T. and Maeda, H. (2004) Antiapoptotic role of heme oxygenase (HO) and the potential of HO as a target in anticancer treatment. Apoptosis. 9, 27-35.
    • (2004) Apoptosis , vol.9 , pp. 27-35
    • Fang, J.1    Akaike, T.2    Maeda, H.3
  • 32
    • 0029883321 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 in LMH cells. Comparison of LMH cells to primary cultures of chick embryo liver cells
    • Gabis, K. K., Gildemeister, O. S., Pepe, J. A., Lambrecht, R. W and Bonkovsky, H. L. (1996) Induction of heme oxygenase-1 in LMH cells. Comparison of LMH cells to primary cultures of chick embryo liver cells. Biochim. Biophys. Acta 1290, 113-120.
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 113-120
    • Gabis, K.K.1    Gildemeister, O.S.2    Pepe, J.A.3    Lambrecht, R.W.4    Bonkovsky, H.L.5
  • 34
    • 1642498338 scopus 로고    scopus 로고
    • Hepatic metabolism of diallyl disulphide in rat and man
    • Germain, E., Chevalier, J., Siess, M. H. and Teyssier, C. (2003) Hepatic metabolism of diallyl disulphide in rat and man. Xenobiotica 33, 1185-1199.
    • (2003) Xenobiotica , vol.33 , pp. 1185-1199
    • Germain, E.1    Chevalier, J.2    Siess, M.H.3    Teyssier, C.4
  • 36
    • 0032005790 scopus 로고    scopus 로고
    • Distribution of heme oxygenase isoforms in rat liver. Topographic basis for carbon monoxide-mediated microvascular relaxation
    • Goda, N., Suzuki, K., Naito, M., Takeoka, S., Tsuchida, E., Ishimura, Y., Tamatani, T. and Suematsu, M. (1998) Distribution of heme oxygenase isoforms in rat liver. Topographic basis for carbon monoxide-mediated microvascular relaxation. J. Clin. Invest. 101, 604-612.
    • (1998) J. Clin. Invest. , vol.101 , pp. 604-612
    • Goda, N.1    Suzuki, K.2    Naito, M.3    Takeoka, S.4    Tsuchida, E.5    Ishimura, Y.6    Tamatani, T.7    Suematsu, M.8
  • 38
    • 7944220437 scopus 로고    scopus 로고
    • Diallyl sulfide induces heme oxygenase-1 through MAPK pathway
    • Gong, P., Hu, B. and Cederbaum, A. I. (2004) Diallyl sulfide induces heme oxygenase-1 through MAPK pathway. Arch. Biochem. Biophys. 432, 252-260.
    • (2004) Arch. Biochem. Biophys. , vol.432 , pp. 252-260
    • Gong, P.1    Hu, B.2    Cederbaum, A.I.3
  • 39
    • 21344437955 scopus 로고    scopus 로고
    • Glutamine is highly effective in preventing in vivo cobalt-induced oxidative stress in rat liver
    • Gonzales, S., Polizio, A. H., Erario, M. A. and Tomaro, M. L. (2005) Glutamine is highly effective in preventing in vivo cobalt-induced oxidative stress in rat liver. World J. Gastroenterol. 11, 3533-3538.
    • (2005) World J. Gastroenterol. , vol.11 , pp. 3533-3538
    • Gonzales, S.1    Polizio, A.H.2    Erario, M.A.3    Tomaro, M.L.4
  • 40
    • 21344437955 scopus 로고    scopus 로고
    • Glutamine is highly effective in preventing in vivo cobalt-induced oxidative stress in rat liver
    • Gonzales, S., Polizio, A. H., Erario, M. A. and Tomaro, M. L. (2005) Glutamine is highly effective in preventing in vivo cobalt-induced oxidative stress in rat liver. World J. Gastroenterol. 11, 3533-3538.
    • (2005) World J. Gastroenterol. , vol.11 , pp. 3533-3538
    • Gonzales, S.1    Polizio, A.H.2    Erario, M.A.3    Tomaro, M.L.4
  • 42
    • 0032917797 scopus 로고    scopus 로고
    • Modulation of phase II enzymes by organosulfur compounds from allium vegetables in rat tissues
    • Guyonnet, D., Siess, M. H., Le Bon, A. M. and Suschetet, M. (1999) Modulation of phase II enzymes by organosulfur compounds from allium vegetables in rat tissues. Toxicol. Appl. Pharmacol. 154, 50-58.
    • (1999) Toxicol. Appl. Pharmacol. , vol.154 , pp. 50-58
    • Guyonnet, D.1    Siess, M.H.2    Le Bon, A.M.3    Suschetet, M.4
  • 43
    • 0035877643 scopus 로고    scopus 로고
    • Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation
    • He, C. H., Gong, P., Hu, B., Stewart, D., Choi, M. E., Choi, A. M. and Alam, J. (2001) Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation. J. Biol. Chem. 276, 20858-20865.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20858-20865
    • He, C.H.1    Gong, P.2    Hu, B.3    Stewart, D.4    Choi, M.E.5    Choi, A.M.6    Alam, J.7
  • 44
    • 5144220818 scopus 로고    scopus 로고
    • Signal transduction pathways leading to cell cycle arrest and apoptosis induction in cancer cells by Allium vegetable-derived organosulfur compounds: A review
    • Herman-Antosiewicz, A. and Singh, S. V. (2004) Signal transduction pathways leading to cell cycle arrest and apoptosis induction in cancer cells by Allium vegetable-derived organosulfur compounds: a review. Mutat. Res. 555, 121-131.
    • (2004) Mutat. Res. , vol.555 , pp. 121-131
    • Herman-Antosiewicz, A.1    Singh, S.V.2
  • 47
    • 0031956516 scopus 로고    scopus 로고
    • The rat heme oxygenase-1 gene is transcriptionally induced via the protein kinase A signaling pathway in rat hepatocyte cultures
    • Immenschuh, S., Kietzmann, T., Hinke, V., Wiederhold, M., Katz, N. and Muller-Eberhard, U. (1998) The rat heme oxygenase-1 gene is transcriptionally induced via the protein kinase A signaling pathway in rat hepatocyte cultures. Mol. Pharmacol. 53, 483-491.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 483-491
    • Immenschuh, S.1    Kietzmann, T.2    Hinke, V.3    Wiederhold, M.4    Katz, N.5    Muller-Eberhard, U.6
  • 48
    • 0028818098 scopus 로고
    • Expression of the mRNA of heme-binding protein 23 is coordinated with that of heme oxygenase-1 by heme and heavy metals in primary rat hepatocytes and hepatoma cells
    • Immenschuh, S., Iwahara, S., Satoh, H., Nell, C., Katz, N. and Muller-Eberhard, U. (1995) Expression of the mRNA of heme-binding protein 23 is coordinated with that of heme oxygenase-1 by heme and heavy metals in primary rat hepatocytes and hepatoma cells. Biochemistry 34, 13407-13411.
    • (1995) Biochemistry , vol.34 , pp. 13407-13411
    • Immenschuh, S.1    Iwahara, S.2    Satoh, H.3    Nell, C.4    Katz, N.5    Muller-Eberhard, U.6
  • 53
    • 20444438012 scopus 로고    scopus 로고
    • Differential expression and stability of endogenous nuclear factor E2-related factor 2 (Nrf2) by natural chemopreventive compounds in HepG2 human hepatoma cells
    • Jeong, W. S, Keum, Y. S, Chen, C., Jain, M. R., Shen, G., Kim, J. H., Li, W. and Kong, A. N. (2005) Differential expression and stability of endogenous nuclear factor E2-related factor 2 (Nrf2) by natural chemopreventive compounds in HepG2 human hepatoma cells. J. Biochem. Mol. Biol. 38, 167-176.
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 167-176
    • Jeong, W.S.1    Keum, Y.S.2    Chen, C.3    Jain, M.R.4    Shen, G.5    Kim, J.H.6    Li, W.7    Kong, A.N.8
  • 54
    • 0035234782 scopus 로고    scopus 로고
    • Regulation of heme oxygenase activity in rat liver during oxidative stress induced by cobalt chloride and mercury chloride
    • Kaliman, P. A., Nikitchenko, I. V., Sokol, O. A. and Strel'chenko, E. V. (2001) Regulation of heme oxygenase activity in rat liver during oxidative stress induced by cobalt chloride and mercury chloride. Biochemistry (Mosc). 66, 77-82.
    • (2001) Biochemistry (Mosc) , vol.66 , pp. 77-82
    • Kaliman, P.A.1    Nikitchenko, I.V.2    Sokol, O.A.3    Strel'chenko, E.V.4
  • 58
    • 0028885949 scopus 로고
    • The organ toxicity of inhaled anesthetics
    • Kenna, J. G. and Jones, R. M. (1995) The organ toxicity of inhaled anesthetics. Anesth Analg. 81, 51-66.
    • (1995) Anesth Analg. , vol.81 , pp. 51-66
    • Kenna, J.G.1    Jones, R.M.2
  • 59
    • 0030868098 scopus 로고    scopus 로고
    • Chemoprevention by inducers of carcinogen detoxication enzymes
    • Kensler, T. W. (1997) Chemoprevention by inducers of carcinogen detoxication enzymes. Environ. Health Perspect. 105, 965-970.
    • (1997) Environ. Health Perspect. , vol.105 , pp. 965-970
    • Kensler, T.W.1
  • 60
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • Keyse, S. M. and Tyrrell, R. M. (1989) Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc. Natl. Acad. Sci. USA 86, 99-103.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 61
    • 15044345354 scopus 로고    scopus 로고
    • Effects of Cyclopentenone Prostaglandins on the Expression of Heme Oxygenase-1 in MCF-7 Cells
    • Kim, E. H., Kim, D. H., Na, H. K. and Surh, Y. J. (2004) Effects of Cyclopentenone Prostaglandins on the Expression of Heme Oxygenase-1 in MCF-7 Cells. Ann. N. Y. Acad. Sci. 1030, 493-500.
    • (2004) Ann. N. Y. Acad. Sci. , vol.1030 , pp. 493-500
    • Kim, E.H.1    Kim, D.H.2    Na, H.K.3    Surh, Y.J.4
  • 62
    • 0032746684 scopus 로고    scopus 로고
    • An integrated pharmacokinetic and pharmacodynamic study of arsenite action. 1. Heme oxygenase induction in rats
    • Kitchin, K. T., Del Razo, L. M., Brown, J. L., Anderson, W. L. and Kenyon, E. M. (1999) An integrated pharmacokinetic and pharmacodynamic study of arsenite action. 1. Heme oxygenase induction in rats. Teratog. Carcinog. Mutagen. 19, 385-402
    • (1999) Teratog. Carcinog. Mutagen. , vol.19 , pp. 385-402
    • Kitchin, K.T.1    Del Razo, L.M.2    Brown, J.L.3    Anderson, W.L.4    Kenyon, E.M.5
  • 63
    • 5144232811 scopus 로고    scopus 로고
    • Chemoprevention through the Keap1-Nrf2 signaling pathway by phase 2 enzyme inducers
    • Kwak, M. K., Wakabayashi, N. and Kensler, T. W. (2004) Chemoprevention through the Keap1-Nrf2 signaling pathway by phase 2 enzyme inducers. Mutat. Res. 555, 133-148.
    • (2004) Mutat. Res. , vol.555 , pp. 133-148
    • Kwak, M.K.1    Wakabayashi, N.2    Kensler, T.W.3
  • 65
    • 0034014663 scopus 로고    scopus 로고
    • Inhibition of human cytochrome P450 enzymes by 1,2-dithiole-3-thione, oltipraz and its derivatives, and sulforaphane
    • Langouet, S., Furge, L. L, Kerriguy, N., Nakamura, K., Guillouzo, A. and Guengerich, F. P. (2000) Inhibition of human cytochrome P450 enzymes by 1,2-dithiole-3-thione, oltipraz and its derivatives, and sulforaphane. Chem. Res. Toxicol. 13, 245-252.
    • (2000) Chem. Res. Toxicol. , vol.13 , pp. 245-252
    • Langouet, S.1    Furge, L.L.2    Kerriguy, N.3    Nakamura, K.4    Guillouzo, A.5    Guengerich, F.P.6
  • 66
    • 0028948724 scopus 로고
    • Modulation of macrophage functioning abrogates the acute hepatotoxicity of acetaminophen
    • Laskin, D. L., Gardner, C. R., Price, V. F. and Jollow, D. J. (1995) Modulation of macrophage functioning abrogates the acute hepatotoxicity of acetaminophen. Hepatology 21, 1045-1050.
    • (1995) Hepatology , vol.21 , pp. 1045-1050
    • Laskin, D.L.1    Gardner, C.R.2    Price, V.F.3    Jollow, D.J.4
  • 67
    • 0034701113 scopus 로고    scopus 로고
    • Age-dependent increase of heme oxygenase-1 gene expression in the liver mediated by NF-kappa B
    • Lavrovsky, Y., Song, C. S., Chatterjee, B. and Roy, A. K. (2000) Age-dependent increase of heme oxygenase-1 gene expression in the liver mediated by NF-kappa B. Mech. Ageing Dev. 114, 49-60.
    • (2000) Mech. Ageing Dev. , vol.114 , pp. 49-60
    • Lavrovsky, Y.1    Song, C.S.2    Chatterjee, B.3    Roy, A.K.4
  • 68
    • 19444379739 scopus 로고    scopus 로고
    • Nrf2 as a molecular target for chemoprevention
    • Lee J-S and Surh Y-J. (2005).Nrf2 as a molecular target for chemoprevention. Cancer Lett. 224, 171-184.
    • (2005) Cancer Lett. , vol.224 , pp. 171-184
    • Lee, J.-S.1    Surh, Y.-J.2
  • 70
    • 0025106189 scopus 로고
    • Regulation of heme oxygenase gene expression by cobalt in rat liver and kidney
    • Lin, J. H., Villalon, P., Martasek, P. and Abraham, N. G. (1990) Regulation of heme oxygenase gene expression by cobalt in rat liver and kidney. Eur. J. Biochem. 192, 577-582.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 577-582
    • Lin, J.H.1    Villalon, P.2    Martasek, P.3    Abraham, N.G.4
  • 71
  • 72
    • 0035877643 scopus 로고    scopus 로고
    • Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation
    • He, C. H., Gong, P., Hu, B., Stewart, D., Choi, M. E., Choi, A. M. and Alam, J. (2001) Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation. J. Biol. Chem. 276, 20858-20865.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20858-20865
    • He, C.H.1    Gong, P.2    Hu, B.3    Stewart, D.4    Choi, M.E.5    Choi, A.M.6    Alam, J.7
  • 73
    • 0842308302 scopus 로고    scopus 로고
    • Upregulation of heme oxygenase-1 and p21 confers resistance to apoptosis in human gastric cancer cells
    • Liu, Z. M., Chen, G. G., Ng, E. K., Leung, W. K., Sung, J. J. and Chung, S. C. (2004) Upregulation of heme oxygenase-1 and p21 confers resistance to apoptosis in human gastric cancer cells. Oncogene 23, 503-513.
    • (2004) Oncogene , vol.23 , pp. 503-513
    • Liu, Z.M.1    Chen, G.G.2    Ng, E.K.3    Leung, W.K.4    Sung, J.J.5    Chung, S.C.6
  • 74
    • 0029961252 scopus 로고    scopus 로고
    • Differential activation of ERK, JNK/SAPK and P38/CSBP/RK MAP kinase family members during the cellular response to arsenite
    • Liu, Y., Guyton, K. Z, Gorospe, M., Xu, Q., Lee, J. C. and Holbrook, N. J. (1996) Differential activation of ERK, JNK/SAPK and P38/CSBP/RK MAP kinase family members during the cellular response to arsenite. Free Radic. Biol. Med. 21, 771-81.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 771-781
    • Liu, Y.1    Guyton, K.Z.2    Gorospe, M.3    Xu, Q.4    Lee, J.C.5    Holbrook, N.J.6
  • 75
    • 0027933447 scopus 로고
    • Heme oxygenase and oxidative stress. Evidence of involvement of bilirubin as physiological protector against oxidative damage
    • Llesuy, S. F and Tomaro, M. L. (1994) Heme oxygenase and oxidative stress. Evidence of involvement of bilirubin as physiological protector against oxidative damage. Biochim. Biophys. Acta. 1223, 9-14.
    • (1994) Biochim. Biophys. Acta. , vol.1223 , pp. 9-14
    • Llesuy, S.F.1    Tomaro, M.L.2
  • 76
    • 0033938021 scopus 로고    scopus 로고
    • Upstream regulatory elements in chick heme oxygenase-1 promoter: A study in primary cultures of chick embryo liver cells
    • Lu, T. H, Shan, Y., Pepe, J., Lambrecht, R. W. and Bonkovsky, H. L. (2000) Upstream regulatory elements in chick heme oxygenase-1 promoter: a study in primary cultures of chick embryo liver cells. Mol. Cell. Biochem. 209, 17-27.
    • (2000) Mol. Cell. Biochem. , vol.209 , pp. 17-27
    • Lu, T.H.1    Shan, Y.2    Pepe, J.3    Lambrecht, R.W.4    Bonkovsky, H.L.5
  • 77
    • 0030738362 scopus 로고    scopus 로고
    • Regulation of expression of the human heme oxygenase-1 gene in transfected chick embryo liver cell cultures
    • Lu, T. H., Pepe, J. A., Gildemeister, O. S., Tyrrell, R. M. and Bonkovsky, H. L. (1997) Regulation of expression of the human heme oxygenase-1 gene in transfected chick embryo liver cell cultures. Biochim. Biophys. Acta. 1352, 293-302.
    • (1997) Biochim. Biophys. Acta. , vol.1352 , pp. 293-302
    • Lu, T.H.1    Pepe, J.A.2    Gildemeister, O.S.3    Tyrrell, R.M.4    Bonkovsky, H.L.5
  • 78
    • 0033938021 scopus 로고    scopus 로고
    • Upstream regulatory elements in chick heme oxygenase-1 promoter: A study in primary cultures of chick embryo liver cells
    • Lu, T. H., Shan, Y., Pepe, J., Lambrecht, R. W. and Bonkovsky, H. L. (2000) Upstream regulatory elements in chick heme oxygenase-1 promoter: a study in primary cultures of chick embryo liver cells. Mol. Cell. Biochem. 209, 17-27.
    • (2000) Mol. Cell. Biochem. , vol.209 , pp. 17-27
    • Lu, T.H.1    Shan, Y.2    Pepe, J.3    Lambrecht, R.W.4    Bonkovsky, H.L.5
  • 79
    • 0030038632 scopus 로고    scopus 로고
    • Participation of altered upstream stimulatory factor in the induction of rat heme oxygenase-1 by cadmium
    • Maeshima, H., Sato, M., Ishikawa, K., Katagata, Y. and Yoshida, T. (1996) Participation of altered upstream stimulatory factor in the induction of rat heme oxygenase-1 by cadmium. Nucleic Acids Res. 24, 2959-2965.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2959-2965
    • Maeshima, H.1    Sato, M.2    Ishikawa, K.3    Katagata, Y.4    Yoshida, T.5
  • 80
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines, M. D. (1988) Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J 2, 2557-2568.
    • (1988) FASEB J. , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 81
    • 28844432578 scopus 로고    scopus 로고
    • The heme oxygenase sytem: Update 2005
    • Maines, M. D. (2005) The heme oxygenase sytem: Update 2005. Antiox Redox Signal 7, 1761-1766.
    • (2005) Antiox Redox Signal , vol.7 , pp. 1761-1766
    • Maines, M.D.1
  • 82
    • 27544434838 scopus 로고    scopus 로고
    • 30 Some years of heme oxygenase: From a "molecular wrecking ball" to a "mesmerizing" trigger of cellular events
    • Maines, M. D. and Gibbs, P. E. (2005) 30 some years of heme oxygenase: from a "molecular wrecking ball" to a "mesmerizing" trigger of cellular events. Biochem. Biophys. Res. Commun. 338, 568-577.
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 568-577
    • Maines, M.D.1    Gibbs, P.E.2
  • 83
    • 0022632224 scopus 로고
    • Characterization of two constitutive forms of rat liver microsomal heme oxygenase. only one molecular species of the enzyme is inducible
    • Maines, M. D., Trakshel, G. M. and Kutty, R. K. (1986) Characterization of two constitutive forms of rat liver microsomal heme oxygenase. Only one molecular species of the enzyme is inducible. J. Biol. Chem. 261, 411-419.
    • (1986) J. Biol. Chem. , vol.261 , pp. 411-419
    • Maines, M.D.1    Trakshel, G.M.2    Kutty, R.K.3
  • 84
    • 0030639567 scopus 로고    scopus 로고
    • Acetaminophen-induced hepatotoxicity: Predisposing factors and treatments
    • Makin, A. J. and Williams, R. (1997) Acetaminophen-induced hepatotoxicity: predisposing factors and treatments. Adv. Intern. Med. 42, 453-483.
    • (1997) Adv. Intern. Med. , vol.42 , pp. 453-483
    • Makin, A.J.1    Williams, R.2
  • 85
    • 14844288046 scopus 로고    scopus 로고
    • Heme oxygenase-1 levels and oxidative stress-related parameters in non-alcoholic fatty liver disease patients
    • Malaguarnera, L., Madeddu, R., Palio, E., Arena, N. and Malaguarnera, M. (2005) Heme oxygenase-1 levels and oxidative stress-related parameters in non-alcoholic fatty liver disease patients . J. Hepatol. 42, 585-591.
    • (2005) J. Hepatol. , vol.42 , pp. 585-591
    • Malaguarnera, L.1    Madeddu, R.2    Palio, E.3    Arena, N.4    Malaguarnera, M.5
  • 88
    • 10244220962 scopus 로고    scopus 로고
    • Remote liver injury is attenuated by adenovirus-mediated gene transfer of heme oxygenase-1 during the systemic inflammatory response syndrome
    • McCarter, S. D., Badhwar, A., Scott, J. R., Akyea, T. G., Bihari, A., Dungey, A. A., Harris, K. A. and Potter, R. F. (2004) Remote liver injury is attenuated by adenovirus-mediated gene transfer of heme oxygenase-1 during the systemic inflammatory response syndrome. Microcirculation 11, 587-595.
    • (2004) Microcirculation , vol.11 , pp. 587-595
    • McCarter, S.D.1    Badhwar, A.2    Scott, J.R.3    Akyea, T.G.4    Bihari, A.5    Dungey, A.A.6    Harris, K.A.7    Potter, R.F.8
  • 89
    • 0026653813 scopus 로고
    • Human heme oxygenase-2: Characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal
    • McCoubrey, W. K Jr., Ewing, J. F. and Maines, M. D. (1992) Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch. Biochem. Biophys. 295, 13-20.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 13-20
    • McCoubrey Jr., W.K.1    Ewing, J.F.2    Maines, M.D.3
  • 90
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • McCoubrey, W. K. Jr., Huang, T. J. and Maines, M. D. (1997) Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur. J. Biochem. 247, 725-732.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 725-732
    • McCoubrey Jr., W.K.1    Huang, T.J.2    Maines, M.D.3
  • 91
    • 33644618004 scopus 로고    scopus 로고
    • Curcumin induces heme oxygenase-1 in hepatocytes and is protective in simulated cold preservation and warm reperfusion injury
    • McNally, S. J, Harrison, E. M., Ross, J. A., Garden, O. J. and Wigmore, S. J. (2006) Curcumin induces heme oxygenase-1 in hepatocytes and is protective in simulated cold preservation and warm reperfusion injury. Transplantation 81, 623-626.
    • (2006) Transplantation , vol.81 , pp. 623-626
    • McNally, S.J.1    Harrison, E.M.2    Ross, J.A.3    Garden, O.J.4    Wigmore, S.J.5
  • 92
    • 0033000310 scopus 로고    scopus 로고
    • Pretreatment of mice with macrophage inactivators decreases acetaminophen hepatotoxicity and the formation of reactive oxygen and nitrogen species
    • Michael, S. L., Pumford, N. R., Mayeux, P. R., Niesman, M. R. and Hinson, J. A. (1999) Pretreatment of mice with macrophage inactivators decreases acetaminophen hepatotoxicity and the formation of reactive oxygen and nitrogen species. Hepatology. 30, 186-195.
    • (1999) Hepatology , vol.30 , pp. 186-195
    • Michael, S.L.1    Pumford, N.R.2    Mayeux, P.R.3    Niesman, M.R.4    Hinson, J.A.5
  • 93
    • 0034921254 scopus 로고    scopus 로고
    • Mechanisms by which garlic and allyl sulfur compounds suppress carcinogen bioactivation. Garlic and carcinogenesis
    • Milner, J. A. (2001) Mechanisms by which garlic and allyl sulfur compounds suppress carcinogen bioactivation. Garlic and carcinogenesis. Adv. Exp. Med. Biol. 492, 69-81.
    • (2001) Adv. Exp. Med. Biol. , vol.492 , pp. 69-81
    • Milner, J.A.1
  • 94
    • 0025057279 scopus 로고
    • Activation of heme oxygenase and heat shock protein 70 genes by stress in human hepatoma cells
    • Mitani, K., Fujita, H., Sassa, S. and Kappas, A. (1990) Activation of heme oxygenase and heat shock protein 70 genes by stress in human hepatoma cells. Biochem. Biophys. Res. Commun. 166, 1429-1434.
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 1429-1434
    • Mitani, K.1    Fujita, H.2    Sassa, S.3    Kappas, A.4
  • 96
    • 0034607632 scopus 로고    scopus 로고
    • Endothelial heme oxygenase-1 induction by hypoxia. Modulation by inducible nitric-oxide synthase and S-nitrosothiols
    • Motterlini, R., Foresti, R., Bassi, R., Calabrese, V., Clark, J. E. and Green, C. J. (2000) Endothelial heme oxygenase-1 induction by hypoxia. Modulation by inducible nitric-oxide synthase and S-nitrosothiols. J. Biol. Chem. 275, 13613-13620.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13613-13620
    • Motterlini, R.1    Foresti, R.2    Bassi, R.3    Calabrese, V.4    Clark, J.E.5    Green, C.J.6
  • 97
    • 1842588301 scopus 로고    scopus 로고
    • Induction of phase II detoxification enzymes in rats by plant-derived isothiocyanates: Comparison of allyl isothiocyanate with sulforaphane and related compounds
    • Munday, R. and Munday, C. M. (2004) Induction of phase II detoxification enzymes in rats by plant-derived isothiocyanates: comparison of allyl isothiocyanate with sulforaphane and related compounds. J. Agric. Food Chem. 52, 1867-1871.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1867-1871
    • Munday, R.1    Munday, C.M.2
  • 99
    • 0038537298 scopus 로고    scopus 로고
    • PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells
    • Nakaso K., Yano, H., Fukuhara, Y., Takeshima, T., Wada-Isoe, K. and Nakashima, K. (2003) PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells. FEBS Lett 546, 181-184.
    • (2003) FEBS Lett. , vol.546 , pp. 181-184
    • Nakaso, K.1    Yano, H.2    Fukuhara, Y.3    Takeshima, T.4    Wada-Isoe, K.5    Nakashima, K.6
  • 100
    • 0025694879 scopus 로고
    • Molecular mechanisms of the hepatotoxicity caused by acetaminophen
    • Nelson, S. D. (1990) Molecular mechanisms of the hepatotoxicity caused by acetaminophen. Semin Liver Dis. 10, 267-278.
    • (1990) Semin Liver Dis. , vol.10 , pp. 267-278
    • Nelson, S.D.1
  • 102
    • 0041742490 scopus 로고    scopus 로고
    • A typical protein kinase C mediates activation of NF-E2-related factor 2 in response to oxidative stress
    • Numazawa, S., Ishikawa, M., Yoshida, A., Tanaka, S. and Yoshida, T. (2003) A typical protein kinase C mediates activation of NF-E2-related factor 2 in response to oxidative stress. Am. J. Physiol. Cell. Physiol. 285, 334-342.
    • (2003) Am. J. Physiol. Cell. Physiol. , vol.285 , pp. 334-342
    • Numazawa, S.1    Ishikawa, M.2    Yoshida, A.3    Tanaka, S.4    Yoshida, T.5
  • 104
    • 0032571164 scopus 로고    scopus 로고
    • Heme oxygenase induction by UVA radiation. A response to oxidative stress in rat liver
    • Ossola, J. O. and Tomaro, M. L. (1998) Heme oxygenase induction by UVA radiation. A response to oxidative stress in rat liver. Int. J. Biochem. Cell. Biol. 30, 285-292.
    • (1998) Int. J. Biochem. Cell. Biol. , vol.30 , pp. 285-292
    • Ossola, J.O.1    Tomaro, M.L.2
  • 105
    • 0031568222 scopus 로고    scopus 로고
    • Relationship between oxidative stress and heme oxygenase induction by copper sulfate
    • Ossola, J. O., Groppa, M. D. and Tomaro, M. L. (1997) Relationship between oxidative stress and heme oxygenase induction by copper sulfate. Arch. Biochem. Biophys. 337, 332-337.
    • (1997) Arch. Biochem. Biophys. , vol.337 , pp. 332-337
    • Ossola, J.O.1    Groppa, M.D.2    Tomaro, M.L.3
  • 106
    • 0030976644 scopus 로고    scopus 로고
    • Mechanism of hemoglobin-induced protection against endotoxemia in rats: A ferritinin-dependent pathway
    • Otterbein, L., Chin, B. Y., Otterbein, S. L., Lowe, V. C., Fessler, H. E. and Choi, A. M. (1997) Mechanism of hemoglobin-induced protection against endotoxemia in rats: a ferritinin-dependent pathway. Am. J. Physiol. 272, 268-275.
    • (1997) Am. J. Physiol. , vol.272 , pp. 268-275
    • Otterbein, L.1    Chin, B.Y.2    Otterbein, S.L.3    Lowe, V.C.4    Fessler, H.E.5    Choi, A.M.6
  • 107
    • 0043268709 scopus 로고    scopus 로고
    • Heme oxygenase-1: Unleashing the protective properties of heme
    • Otterbein, L. E., Soares, M. P., Yamashita, K. and Bach, F. H. (2003) Heme oxygenase-1: unleashing the protective properties of heme. Trends Immunol. 24, 449-455.
    • (2003) Trends Immunol. , vol.24 , pp. 449-455
    • Otterbein, L.E.1    Soares, M.P.2    Yamashita, K.3    Bach, F.H.4
  • 108
    • 0032531163 scopus 로고    scopus 로고
    • Protective role of endogenous carbon monoxide in hepatic microcirculatory dysfunction after hemorrhagic shock in rats
    • Pannen, B. H., Kohler, N., Hole, B., Bauer, M., Clemens, M. G. and Geiger, K. K. (1998) Protective role of endogenous carbon monoxide in hepatic microcirculatory dysfunction after hemorrhagic shock in rats. J. Clin. Invest. 102, 1220-1228.
    • (1998) J. Clin. Invest. , vol.102 , pp. 1220-1228
    • Pannen, B.H.1    Kohler, N.2    Hole, B.3    Bauer, M.4    Clemens, M.G.5    Geiger, K.K.6
  • 109
    • 0032531163 scopus 로고    scopus 로고
    • Protective role of endogenous carbon monoxide in hepatic microcirculatory dysfunction after hemorrhagic shock in rats
    • Pannen, B. H., Kohler, N., Hole, B., Bauer, M., Clemens, M. G., and Geiger, K. K. (1998) Protective role of endogenous carbon monoxide in hepatic microcirculatory dysfunction after hemorrhagic shock in rats. J. Clin. Invest. 102, 1220-1228.
    • (1998) J. Clin. Invest. , vol.102 , pp. 1220-1228
    • Pannen, B.H.1    Kohler, N.2    Hole, B.3    Bauer, M.4    Clemens, M.G.5    Geiger, K.K.6
  • 112
    • 0034063564 scopus 로고    scopus 로고
    • Heme oxygenase-1 is a cGMP-inducible endothelial protein and mediates the cytoprotective action of nitric oxide
    • Polte, T., Abate, A., Dennery, P. A. and Schroder, H. (2000) Heme oxygenase-1 is a cGMP-inducible endothelial protein and mediates the cytoprotective action of nitric oxide. Arterioscler Thromb. Vasc. Biol. 20, 1209-1215.
    • (2000) Arterioscler Thromb. Vasc. Biol. , vol.20 , pp. 1209-1215
    • Polte, T.1    Abate, A.2    Dennery, P.A.3    Schroder, H.4
  • 113
    • 0031443801 scopus 로고    scopus 로고
    • The nitric oxide donor SIN-1 protects endothelial cells from tumor necrosis factor-alpha-mediated cytotoxicity: Possible role for cyclic GMP and heme oxygenase
    • Polte, T., Oberle, S. and Schroder, H. (1997) The nitric oxide donor SIN-1 protects endothelial cells from tumor necrosis factor-alpha-mediated cytotoxicity: possible role for cyclic GMP and heme oxygenase. J. Mol. Cell. Cardiol. 29, 3305-3310.
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 3305-3310
    • Polte, T.1    Oberle, S.2    Schroder, H.3
  • 114
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1-deficient cells
    • Poss, K. D. and Tonegawa, S. (1997) Reduced stress defense in heme oxygenase 1-deficient cells. Proc. Natl. Acad. Sci. USA 94, 10925-10930.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10925-10930
    • Poss, K.D.1    Tonegawa, S.2
  • 115
    • 28844446987 scopus 로고    scopus 로고
    • Molecular basis of heme oxygenase-1 induction: Implications for chemoprevention and chemoprotection
    • Prawan A., Kundu, J. K. and Surh A. J. (2005) Molecular basis of heme oxygenase-1 induction: implications for chemoprevention and chemoprotection. Antioxid Redox Signal 7, 1688-1703.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 1688-1703
    • Prawan, A.1    Kundu, J.K.2    Surh, A.J.3
  • 116
    • 0029830816 scopus 로고    scopus 로고
    • Induction of hepatic heme oxygenase-1 and ferritin in rats by cancer chemopreventive dithiolethiones
    • Primiano, T., Kensler, T. W., Kuppusamy, P., Zweier, J. L. and Sutter, T. R. (1996) Induction of hepatic heme oxygenase-1 and ferritin in rats by cancer chemopreventive dithiolethiones. Carcinogenesis 17, 2291-2296.
    • (1996) Carcinogenesis , vol.17 , pp. 2291-2296
    • Primiano, T.1    Kensler, T.W.2    Kuppusamy, P.3    Zweier, J.L.4    Sutter, T.R.5
  • 118
    • 0038529681 scopus 로고    scopus 로고
    • Nerve growth factor protects against 6-hydroxydopamine-induced oxidative stress by increasing expression of heme oxygenase-1 in a phosphatidylinositol 3-kinase-dependent manner
    • Salinas, M., Diaz, R., Abraham, N. G., Ruiz de Galarreta, C. M. and Cuadrado, A. (2003) Nerve growth factor protects against 6-hydroxydopamine- induced oxidative stress by increasing expression of heme oxygenase-1 in a phosphatidylinositol 3-kinase-dependent manner. J. Biol. Chem. 278, 13898-13904.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13898-13904
    • Salinas, M.1    Diaz, R.2    Abraham, N.G.3    Ruiz De Galarreta, C.M.4    Cuadrado, A.5
  • 121
    • 7044269687 scopus 로고    scopus 로고
    • Cooperative effect of biliverdin and carbon monoxide on survival of mice in immune-mediated liver injury
    • Sass, G., Seyfried, S., Parreira Soares, M., Yamashita, K., Kaczmarek, E., Neuhuber, W. L. and Tiegs, G. (2004) Cooperative effect of biliverdin and carbon monoxide on survival of mice in immune-mediated liver injury. Hepatology 40, 1128-1135.
    • (2004) Hepatology , vol.40 , pp. 1128-1135
    • Sass, G.1    Seyfried, S.2    Parreira Soares, M.3    Yamashita, K.4    Kaczmarek, E.5    Neuhuber, W.L.6    Tiegs, G.7
  • 123
    • 23044459608 scopus 로고    scopus 로고
    • Carbon monoxide-releasing molecules (CO-RMs) attenuate the inflammatory response elicited by lipopolysaccharide in RAW264.7 murine macrophages
    • Sawle, P., Foresti, R., Mann, B. E., Johnson, T. R., Green, C. J. and Motterlini, R. (2005) Carbon monoxide-releasing molecules (CO-RMs) attenuate the inflammatory response elicited by lipopolysaccharide in RAW264.7 murine macrophages. Br. J. Pharmacol. 145, 800-810.
    • (2005) Br. J. Pharmacol. , vol.145 , pp. 800-810
    • Sawle, P.1    Foresti, R.2    Mann, B.E.3    Johnson, T.R.4    Green, C.J.5    Motterlini, R.6
  • 124
    • 0030772692 scopus 로고    scopus 로고
    • Gene expression in liver after toxic injury: Analysis of heat shock response and oxidative stress-inducible genes
    • Schiaffonati, L. and Tiberio L. (1997) Gene expression in liver after toxic injury: analysis of heat shock response and oxidative stress-inducible genes. Liver 17, 183-191.
    • (1997) Liver , vol.17 , pp. 183-191
    • Schiaffonati, L.1    Tiberio, L.2
  • 125
    • 7244259196 scopus 로고    scopus 로고
    • Isoflurane pretreatment lowers portal venous resistance by increasing hepatic heme oxygenase activity in the rat liver in vivo
    • Schmidt, R., Hoetzel, A., Baechle, T., Loop, T., Humar, M., Bauer, M., Pahl, H. L., Geiger, K. K. and Pannen, B. H. (2004) Isoflurane pretreatment lowers portal venous resistance by increasing hepatic heme oxygenase activity in the rat liver in vivo. J. Hepatol. 41, 706-713.
    • (2004) J. Hepatol. , vol.41 , pp. 706-713
    • Schmidt, R.1    Hoetzel, A.2    Baechle, T.3    Loop, T.4    Humar, M.5    Bauer, M.6    Pahl, H.L.7    Geiger, K.K.8    Pannen, B.H.9
  • 126
    • 0036250653 scopus 로고    scopus 로고
    • Acute sodium arsenite treatment induces Cyp2a5 but not Cyp1a1 in the C57Bl/6 mouse in a tissue (kidney) selective manner
    • Seubert, J. M., Webb, C. D. and Bend, J. R. (2002) Acute sodium arsenite treatment induces Cyp2a5 but not Cyp1a1 in the C57Bl/6 mouse in a tissue (kidney) selective manner. J. Biochem. Mol. Toxicol. 16, 96-106.
    • (2002) J. Biochem. Mol. Toxicol. , vol.16 , pp. 96-106
    • Seubert, J.M.1    Webb, C.D.2    Bend, J.R.3
  • 127
    • 3543141161 scopus 로고    scopus 로고
    • Identification of key elements that are responsible for heme-mediated induction of the avian heme oxygenase-1 gene
    • Shan, Y., Lambrecht, R. W. and Bonkovsky, H. L. (2004) Identification of key elements that are responsible for heme-mediated induction of the avian heme oxygenase-1 gene. Biochim. Biophys. Acta 1679, 87-94.
    • (2004) Biochim. Biophys. Acta , vol.1679 , pp. 87-94
    • Shan, Y.1    Lambrecht, R.W.2    Bonkovsky, H.L.3
  • 128
    • 0033500043 scopus 로고    scopus 로고
    • Effects of garlic oil and its organosulfur compounds on the activities of hepatic drug-metabolizing and antioxidant enzymes in rats fed high- and low-fat diets
    • Sheen, L. Y., Chen, H. W., Kung, Y. L, Liu, C. T. and Lii, C. K. (1999) Effects of garlic oil and its organosulfur compounds on the activities of hepatic drug-metabolizing and antioxidant enzymes in rats fed high- and low-fat diets. Nutr. Cancer 35, 160-166.
    • (1999) Nutr. Cancer , vol.35 , pp. 160-166
    • Sheen, L.Y.1    Chen, H.W.2    Kung, Y.L.3    Liu, C.T.4    Lii, C.K.5
  • 130
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker, R., Yamamoto, Y., McDonagh, A. F., Glazer, A. N. and Ames, B. N. (1987) Bilirubin is an antioxidant of possible physiological importance. Science 235, 1043-1046.
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 132
    • 2942555358 scopus 로고    scopus 로고
    • Heme oxygenase-1: A novel therapeutic target in oxidative tissue injuries
    • Takahashi, T., Morita, K., Akagi, R. and Sassa, S. (2004). Heme oxygenase-1: A novel therapeutic target in oxidative tissue injuries. Curr. Med. Chem. 11, 1545-1561.
    • (2004) Curr. Med. Chem. , vol.11 , pp. 1545-1561
    • Takahashi, T.1    Morita, K.2    Akagi, R.3    Sassa, S.4
  • 134
    • 0037464355 scopus 로고    scopus 로고
    • Antiapoptotic effect of haem oxygenase-1 induced by nitric oxide in experimental solid tumour
    • Tanaka, S., Akaike, T., Fang, J., Beppu, T., Ogawa, M., Tamura, F., Miyamoto, Y. and Maeda, H. (2003) Antiapoptotic effect of haem oxygenase-1 induced by nitric oxide in experimental solid tumour. Br. J. Cancer. 88, 902-909.
    • (2003) Br. J. Cancer. , vol.88 , pp. 902-909
    • Tanaka, S.1    Akaike, T.2    Fang, J.3    Beppu, T.4    Ogawa, M.5    Tamura, F.6    Miyamoto, Y.7    Maeda, H.8
  • 135
    • 0022977615 scopus 로고
    • Purification and characterization of the major constitutive form of testicular heme oxygenase. The non inducible isoform
    • Trakshel, G. M., Kutty, R. K, and Maines, M. D. (1986) Purification and characterization of the major constitutive form of testicular heme oxygenase. The non inducible isoform. J. Biol. Chem. 261, 11131-11137.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11131-11137
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 136
    • 0027287614 scopus 로고
    • The proximal promoter region of the human heme oxygenase gene contains elements involved in stimulation of transcriptional activity by a variety of agents including oxidants
    • Tyrrell, R. M., Applegate, L. A. and Tromvoukis, Y. (1993) The proximal promoter region of the human heme oxygenase gene contains elements involved in stimulation of transcriptional activity by a variety of agents including oxidants. Carcinogenesis 14, 761-765.
    • (1993) Carcinogenesis , vol.14 , pp. 761-765
    • Tyrrell, R.M.1    Applegate, L.A.2    Tromvoukis, Y.3
  • 138
    • 21244453607 scopus 로고    scopus 로고
    • Alleviating ischemia-reperfusion injury in aged rat liver by induction of heme oxygenase-1
    • Wang, X. H., Wang, K., Zhang, F., Li, X. C., Qian, X. F., Cheng, F., Li, G. Q. and Fan Y. (2004) Alleviating ischemia-reperfusion injury in aged rat liver by induction of heme oxygenase-1. Transplant Proc. 36, 2917-2923.
    • (2004) Transplant Proc. , vol.36 , pp. 2917-2923
    • Wang, X.H.1    Wang, K.2    Zhang, F.3    Li, X.C.4    Qian, X.F.5    Cheng, F.6    Li, G.Q.7    Fan, Y.8
  • 139
    • 4544354315 scopus 로고    scopus 로고
    • Role of NF-kappaB and p38 MAP kinase signaling pathways in the lipopolysaccharide-dependent activation of heme oxygenase-1 gene expression
    • Wijayanti, N., Huber, S., Samoylenko, A., Kietzmann, T. and Immenschuh, S. (2004) Role of NF-kappaB and p38 MAP kinase signaling pathways in the lipopolysaccharide-dependent activation of heme oxygenase-1 gene expression. Antioxid. Redox Signal 6, 802-810.
    • (2004) Antioxid. Redox Signal , vol.6 , pp. 802-810
    • Wijayanti, N.1    Huber, S.2    Samoylenko, A.3    Kietzmann, T.4    Immenschuh, S.5
  • 141
    • 0036588447 scopus 로고    scopus 로고
    • Inhibition of haem oxygenase activity increases leukocyte accumulation in the liver following limb ischaemia-reperfusion in mice
    • Wunder, C., Brock, R. W., McCarter, S. D., Bihari, A., Harris, K., Eichelbronner, O and Potter, R. F. (2002) Inhibition of haem oxygenase activity increases leukocyte accumulation in the liver following limb ischaemia-reperfusion in mice. J. Physiol. 540, 1013-1021.
    • (2002) J. Physiol. , vol.540 , pp. 1013-1021
    • Wunder, C.1    Brock, R.W.2    McCarter, S.D.3    Bihari, A.4    Harris, K.5    Eichelbronner, O.6    Potter, R.F.7
  • 144
    • 0035126521 scopus 로고    scopus 로고
    • Mechanisms of inhibition of chemical toxicity and carcinogenesis by diallyl sulfide (DAS) and related compounds from garlic
    • Yang, C. S., Chhabra, S. K., Hong, J. Y. and Smith, T. J. (2001) Mechanisms of inhibition of chemical toxicity and carcinogenesis by diallyl sulfide (DAS) and related compounds from garlic. J. Nutr. 131, 1041-1045.
    • (2001) J. Nutr. , vol.131 , pp. 1041-1045
    • Yang, C.S.1    Chhabra, S.K.2    Hong, J.Y.3    Smith, T.J.4
  • 146
    • 0242580049 scopus 로고    scopus 로고
    • Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress
    • Zhang, D. D. and Hannink, M. (2003) Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol. Cell. Biol. 23, 8137-8151.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2


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