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Volumn 94, Issue 8, 2012, Pages 1821-1827

Intracellular accumulation of bilirubin as a defense mechanism against increased oxidative stress

Author keywords

Bilirubin; Heme oxygenase; Hyperbilirubinemia; Lipopolysaccharide; Oxidative stress

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; ARSENITE SODIUM; BILIRUBIN; HEME; HEME OXYGENASE 1;

EID: 84862879160     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.04.026     Document Type: Article
Times cited : (42)

References (44)
  • 1
    • 33845613215 scopus 로고    scopus 로고
    • The heme catabolic pathway and its protective effects on oxidative stress-mediated diseases
    • L. Vitek, H.A. Schwertner, The heme catabolic pathway and its protective effects on oxidative stress-mediated diseases, Adv. Clin. Chem. 43 (2007) 1-57.
    • (2007) Adv. Clin. Chem. , vol.43 , pp. 1-57
    • Vitek, L.1    Schwertner, H.A.2
  • 2
    • 41049098411 scopus 로고    scopus 로고
    • Gilbert syndrome, UGT1A1*28 allele, and cardio-vascular disease risk: Possible protective effects and therapeutic applications of bilirubin
    • H.A. Schwertner, L. Vitek, Gilbert syndrome, UGT1A1*28 allele, and cardio-vascular disease risk: possible protective effects and therapeutic applications of bilirubin, Atherosclerosis 198 (2008) 1-11.
    • (2008) Atherosclerosis , vol.198 , pp. 1-11
    • Schwertner, H.A.1    Vitek, L.2
  • 3
    • 4544386856 scopus 로고    scopus 로고
    • Antioxidant activities of bile pigments
    • R. Stocker, Antioxidant activities of bile pigments, Antioxid. Redox. Signal. 6 (2004) 841-849.
    • (2004) Antioxid. Redox. Signal. , vol.6 , pp. 841-849
    • Stocker, R.1
  • 4
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • R. Stocker, Y. Yamamoto, A.F. McDonagh, A.N. Glazer, B.N. Ames, Bilirubin is an antioxidant of possible physiological importance, Science 235 (1987) 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
  • 6
    • 34247121549 scopus 로고    scopus 로고
    • The anti-mutagenic and antioxidant effects of bile pigments in the Ames Salmonella test
    • A.C. Bulmer, K. Ried, J.S. Coombes, J.T. Blanchfield, I. Toth, K.H. Wagner, The anti-mutagenic and antioxidant effects of bile pigments in the Ames Salmonella test, Mutat. Res. 629 (2007) 122-132.
    • (2007) Mutat. Res. , vol.629 , pp. 122-132
    • Bulmer, A.C.1    Ried, K.2    Coombes, J.S.3    Blanchfield, J.T.4    Toth, I.5    Wagner, K.H.6
  • 7
    • 4043058702 scopus 로고    scopus 로고
    • Bilirubin inhibits iNOS expression and NO production in response to endotoxin in rats
    • W.W. Wang, D.L. Smith, S.D. Zucker, Bilirubin inhibits iNOS expression and NO production in response to endotoxin in rats, Hepatology 40 (2004) 424-433.
    • (2004) Hepatology , vol.40 , pp. 424-433
    • Wang, W.W.1    Smith, D.L.2    Zucker, S.D.3
  • 12
    • 4644351861 scopus 로고    scopus 로고
    • Serum bilirubin levels in the U.S. population: Gender effect and inverse correlation with colorectal cancer
    • S.D. Zucker, P.S. Horn, K.E. Sherman, Serum bilirubin levels in the U.S. population: gender effect and inverse correlation with colorectal cancer, Hepatology 40 (2004) 827-835.
    • (2004) Hepatology , vol.40 , pp. 827-835
    • Zucker, S.D.1    Horn, P.S.2    Sherman, K.E.3
  • 13
    • 78650751290 scopus 로고    scopus 로고
    • Clinical and experimental evidence for oxidative stress as an exacerbating factor of diabetes mellitus
    • R. Takayanagi, T. Inoguchi, K. Ohnaka, Clinical and experimental evidence for oxidative stress as an exacerbating factor of diabetes mellitus, J. Clin. Biochem. Nutr. 48 (2011) 72-77.
    • (2011) J. Clin. Biochem. Nutr. , vol.48 , pp. 72-77
    • Takayanagi, R.1    Inoguchi, T.2    Ohnaka, K.3
  • 15
    • 41149177025 scopus 로고    scopus 로고
    • Pharmacological and clinical aspects of heme oxygenase
    • N.G. Abraham, A. Kappas, Pharmacological and clinical aspects of heme oxygenase, Pharmacol. Rev. 60 (2008) 79-127.
    • (2008) Pharmacol. Rev. , vol.60 , pp. 79-127
    • Abraham, N.G.1    Kappas, A.2
  • 18
    • 36348957437 scopus 로고    scopus 로고
    • Statin treatment increases formation of carbon monoxide and bilirubin in mice: A novel mechanism of in vivo antioxidant protection
    • L. Muchova, R.J. Wong, M. Hsu, I. Morioka, L. Vitek, J. Zelenka, H. Schroder, D.K. Stevenson, Statin treatment increases formation of carbon monoxide and bilirubin in mice: a novel mechanism of in vivo antioxidant protection, Can. J. Physiol. Pharmacol. 85 (2007) 800-810.
    • (2007) Can. J. Physiol. Pharmacol. , vol.85 , pp. 800-810
    • Muchova, L.1    Wong, R.J.2    Hsu, M.3    Morioka, I.4    Vitek, L.5    Zelenka, J.6    Schroder, H.7    Stevenson, D.K.8
  • 19
    • 0015394313 scopus 로고
    • The ready isomerization of bilirubin IX- in aqueous solution
    • A.F. McDonagh, F. Assisi, The ready isomerization of bilirubin IX- in aqueous solution, Biochem. J. 129 (1972) 797-800.
    • (1972) Biochem. J. , vol.129 , pp. 797-800
    • McDonagh, A.F.1    Assisi, F.2
  • 20
    • 0023837193 scopus 로고
    • Heme oxygenase activity as measured by carbon monoxide production
    • H.J. Vreman, D.K. Stevenson, Heme oxygenase activity as measured by carbon monoxide production, Anal. Biochem. 168 (1988) 31-38.
    • (1988) Anal. Biochem. , vol.168 , pp. 31-38
    • Vreman, H.J.1    Stevenson, D.K.2
  • 21
    • 0032468407 scopus 로고    scopus 로고
    • Simultaneous production of carbon monoxide and thiobarbituric acid reactive substances in rat tissue preparations by an iron-ascorbate system
    • H.J. Vreman, R.J. Wong, C.A. Sanesi, P.A. Dennery, D.K. Stevenson, Simultaneous production of carbon monoxide and thiobarbituric acid reactive substances in rat tissue preparations by an iron-ascorbate system, Can. J. Physiol. Pharmacol. 76 (1998) 1057-1065.
    • (1998) Can. J. Physiol. Pharmacol. , vol.76 , pp. 1057-1065
    • Vreman, H.J.1    Wong, R.J.2    Sanesi, C.A.3    Dennery, P.A.4    Stevenson, D.K.5
  • 22
    • 0023927014 scopus 로고
    • Kinetic properties and regulation of biliverdin reductase
    • J.E. Bell, M.D. Maines, Kinetic properties and regulation of biliverdin reductase, Arch. Biochem. Biophys. 263 (1988) 1-9.
    • (1988) Arch. Biochem. Biophys. , vol.263 , pp. 1-9
    • Bell, J.E.1    Maines, M.D.2
  • 23
    • 0036425961 scopus 로고    scopus 로고
    • Critical role of mitochondrial reactive oxygen species formation in visible laser irradiation-induced apoptosis in rat brain astrocytes (RBA-1)
    • M.J. Jou, S.B. Jou, H.M. Chen, C.H. Lin, T.I. Peng, Critical role of mitochondrial reactive oxygen species formation in visible laser irradiation-induced apoptosis in rat brain astrocytes (RBA-1), J. Biomed. Sci. 9 (2002) 507-516.
    • (2002) J. Biomed. Sci. , vol.9 , pp. 507-516
    • Jou, M.J.1    Jou, S.B.2    Chen, H.M.3    Lin, C.H.4    Peng, T.I.5
  • 25
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • H. Ohkawa, N. Ohishi, K. Yagi, Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction, Anal. Biochem. 95 (1979) 351-358.
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 26
    • 33751253746 scopus 로고    scopus 로고
    • Factors affecting the binding of bilirubin to serum albumins: Validation and application of the peroxidase method
    • L. Roca, S. Calligaris, R.P. Wennberg, C.E. Ahlfors, S.G. Malik, J.D. Ostrow, C. Tiribelli, Factors affecting the binding of bilirubin to serum albumins: validation and application of the peroxidase method, Pediatr. Res. 60 (2006) 724-728.
    • (2006) Pediatr. Res. , vol.60 , pp. 724-728
    • Roca, L.1    Calligaris, S.2    Wennberg, R.P.3    Ahlfors, C.E.4    Malik, S.G.5    Ostrow, J.D.6    Tiribelli, C.7
  • 27
    • 77958510339 scopus 로고    scopus 로고
    • Acute promyelocytic leukaemia: Novel insights into the mechanisms of cure
    • H. de The, Z. Chen, Acute promyelocytic leukaemia: novel insights into the mechanisms of cure, Nat. Rev. Cancer 10 (2010) 775-783.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 775-783
    • De The, H.1    Chen, Z.2
  • 28
    • 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
    • S.M. Keyse, R.M. Tyrrell, 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. U. S. A 86 (1989) 99-103.
    • (1989) Proc. Natl. Acad. Sci. U. S. A , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 29
    • 0023654957 scopus 로고
    • Reduction of the C2 and C4 vinyl groups of Sn-protoporphyrin to form Sn-mesoporphyrin markedly enhances the ability of the metalloporphyrin to inhibit in vivo heme catabolism
    • G.S. Drummond, R.A. Galbraith, M.K. Sardana, A. Kappas, Reduction of the C2 and C4 vinyl groups of Sn-protoporphyrin to form Sn-mesoporphyrin markedly enhances the ability of the metalloporphyrin to inhibit in vivo heme catabolism, Arch. Biochem. Biophys. 255 (1987) 64-74.
    • (1987) Arch. Biochem. Biophys. , vol.255 , pp. 64-74
    • Drummond, G.S.1    Galbraith, R.A.2    Sardana, M.K.3    Kappas, A.4
  • 30
    • 0032496159 scopus 로고    scopus 로고
    • Intracellular signaling by reactive oxygen species during hypoxia in cardiomyocytes
    • J. Duranteau, N.S. Chandel, A. Kulisz, Z. Shao, P.T. Schumacker, Intracellular signaling by reactive oxygen species during hypoxia in cardiomyocytes, J. Biol. Chem. 273 (1998) 11619-11624.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11619-11624
    • Duranteau, J.1    Chandel, N.S.2    Kulisz, A.3    Shao, Z.4    Schumacker, P.T.5
  • 31
    • 0031993031 scopus 로고    scopus 로고
    • Transcriptional activation of the HO-1 gene by lipopolysaccharide is mediated by 5′ distal enhancers: Role of reactive oxygen intermediates and AP-1
    • S.L. Camhi, J. Alam, G.W. Wiegand, B.Y. Chin, A.M. Choi, Transcriptional activation of the HO-1 gene by lipopolysaccharide is mediated by 5′ distal enhancers: role of reactive oxygen intermediates and AP-1, Am. J. Respir. Cell. Mol. Biol. 18 (1998) 226-234.
    • (1998) Am. J. Respir. Cell. Mol. Biol. , vol.18 , pp. 226-234
    • Camhi, S.L.1    Alam, J.2    Wiegand, G.W.3    Chin, B.Y.4    Choi, A.M.5
  • 33
    • 0033407605 scopus 로고    scopus 로고
    • Uptake of [(3)H]bilirubin in freshly isolated rat hepatocytes: Role of free bilirubin concentration
    • M.G. Mediavilla, L. Pascolo, J.V. Rodriguez, E.E. Guibert, J.D. Ostrow, C. Tiribelli, Uptake of [(3)H]bilirubin in freshly isolated rat hepatocytes: role of free bilirubin concentration, FEBS Lett. 463 (1999) 143-145.
    • (1999) FEBS Lett. , vol.463 , pp. 143-145
    • Mediavilla, M.G.1    Pascolo, L.2    Rodriguez, J.V.3    Guibert, E.E.4    Ostrow, J.D.5    Tiribelli, C.6
  • 34
    • 0032897558 scopus 로고    scopus 로고
    • Antioxidant and cytotoxic effects of bilirubin on neonatal erythrocytes
    • L.C. Mireles, M.A. Lum, P.A. Dennery, Antioxidant and cytotoxic effects of bilirubin on neonatal erythrocytes, Pediatr. Res. 45 (1999) 355-362.
    • (1999) Pediatr. Res. , vol.45 , pp. 355-362
    • Mireles, L.C.1    Lum, M.A.2    Dennery, P.A.3
  • 35
    • 0029129079 scopus 로고
    • Hyperbilirubinemia results in reduced oxidative injury in neonatal Gunn rats exposed to hyperoxia
    • P.A. Dennery, A.F. McDonagh, D.R. Spitz, P.A. Rodgers, D.K. Stevenson, Hyperbilirubinemia results in reduced oxidative injury in neonatal Gunn rats exposed to hyperoxia, Free Radic. Biol. Med. 19 (1995) 395-404.
    • (1995) Free Radic. Biol. Med. , vol.19 , pp. 395-404
    • Dennery, P.A.1    McDonagh, A.F.2    Spitz, D.R.3    Rodgers, P.A.4    Stevenson, D.K.5
  • 36
    • 33344476414 scopus 로고    scopus 로고
    • Expression of UDP-glucuronosyltransferase isoform mRNAs during inflammation and infection in mouse liver and kidney
    • T.A. Richardson, M. Sherman, D. Kalman, E.T. Morgan, Expression of UDP-glucuronosyltransferase isoform mRNAs during inflammation and infection in mouse liver and kidney, Drug Metab. Dispos. 34 (2006) 351-353.
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 351-353
    • Richardson, T.A.1    Sherman, M.2    Kalman, D.3    Morgan, E.T.4
  • 37
    • 0032944048 scopus 로고    scopus 로고
    • Regulation of the multidrug resistance protein 2 in the rat liver by lipopolysaccharide and dexamethasone
    • R. Kubitz, M. Wettstein, U. Warskulat, D. Häussinger, Regulation of the multidrug resistance protein 2 in the rat liver by lipopolysaccharide and dexamethasone, Gastroenterology 116 (1999) 401-410.
    • (1999) Gastroenterology , vol.116 , pp. 401-410
    • Kubitz, R.1    Wettstein, M.2    Warskulat, U.3    Häussinger, D.4
  • 38
    • 60249090785 scopus 로고    scopus 로고
    • Protective effect of hemin against cadmium-induced testicular damage in rats
    • A.A. Fouad, H.A. Qureshi, A.I. Al-Sultan, M.T. Yacoubi, A.A. Ali, Protective effect of hemin against cadmium-induced testicular damage in rats, Toxicology 257 (2009) 153-160.
    • (2009) Toxicology , vol.257 , pp. 153-160
    • Fouad, A.A.1    Qureshi, H.A.2    Al-Sultan, A.I.3    Yacoubi, M.T.4    Ali, A.A.5
  • 40
    • 66649132533 scopus 로고    scopus 로고
    • Up-regulating the hemeoxygenase system enhances insulin sensitivity and improves glucose metabolism in insulin-resistant diabetes in Goto-Kakizaki rats
    • J.F. Ndisang, A. Jadhav, Up-regulating the hemeoxygenase system enhances insulin sensitivity and improves glucose metabolism in insulin-resistant diabetes in Goto-Kakizaki rats, Endocrinology 150 (2009) 2627-2636.
    • (2009) Endocrinology , vol.150 , pp. 2627-2636
    • Ndisang, J.F.1    Jadhav, A.2
  • 41
    • 34249857235 scopus 로고    scopus 로고
    • Non-heme induction of heme oxygenase-1 does not alter cellular iron metabolism
    • A.D. Sheftel, S.F. Kim, P. Ponka, Non-heme induction of heme oxygenase-1 does not alter cellular iron metabolism, J. Biol. Chem. 282 (2007) 10480-10486.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10480-10486
    • Sheftel, A.D.1    Kim, S.F.2    Ponka, P.3
  • 42
    • 33845640469 scopus 로고    scopus 로고
    • HO-1 is located in liver mitochondria and modulates mitochondrial heme content and metabolism
    • D.P. Converso, C. Taille, M.C. Carreras, A. Jaitovich, J.J. Poderoso, J. Boczkowski, HO-1 is located in liver mitochondria and modulates mitochondrial heme content and metabolism, FASEB J. 20 (2006) 1236-1238.
    • (2006) FASEB J. , vol.20 , pp. 1236-1238
    • Converso, D.P.1    Taille, C.2    Carreras, M.C.3    Jaitovich, A.4    Poderoso, J.J.5    Boczkowski, J.6
  • 44
    • 77949908145 scopus 로고    scopus 로고
    • Hormesis is central to toxicology, pharmacology and risk assessment
    • E.J. Calabrese, Hormesis is central to toxicology, pharmacology and risk assessment, Hum. Exp. Toxicol. 29 (2010) 249-261.
    • (2010) Hum. Exp. Toxicol. , vol.29 , pp. 249-261
    • Calabrese, E.J.1


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