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Volumn 90, Issue 5, 2011, Pages 997-1015

Immunomodulatory and immunotoxic effects of bilirubin: Molecular mechanisms

Author keywords

Bax; CD95; Oxidative stress; P38MAPK; Unconjugated bilirubin

Indexed keywords

BILIRUBIN; CALCIUM ION; CASPASE 8; CASPASE INHIBITOR; CD19 ANTIBODY; CYTOKINE; FAS ANTIGEN; GLUTATHIONE SYNTHASE; LIPOPOLYSACCHARIDE; MITOGEN ACTIVATED PROTEIN KINASE P38; MITOGENIC AGENT; PROTEIN BAX;

EID: 80055083634     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1189/jlb.0211070     Document Type: Article
Times cited : (48)

References (75)
  • 1
    • 4844219758 scopus 로고    scopus 로고
    • Bilirubin: An endogenous product of heme degradation with both cytotoxic and cytoprotective properties
    • Kapitulnik, J. (2004) Bilirubin: an endogenous product of heme degradation with both cytotoxic and cytoprotective properties. Mol. Pharmacol. 66, 773-779.
    • (2004) Mol. Pharmacol , vol.66 , pp. 773-779
    • Kapitulnik, J.1
  • 3
    • 0035075564 scopus 로고    scopus 로고
    • New concepts in bilirubin neurotoxicity and the need for studies at clinically relevant bilirubin concentrations
    • Ostrow, J. D., Tiribelli, C. (2001) New concepts in bilirubin neurotoxicity and the need for studies at clinically relevant bilirubin concentrations. J. Hepatol. 34, 467-470.
    • (2001) J. Hepatol , vol.34 , pp. 467-470
    • Ostrow, J.D.1    Tiribelli, C.2
  • 4
    • 0036234687 scopus 로고    scopus 로고
    • Mechanisms of bilirubin neurotoxicity
    • Ostrow, J. D., Pascolo, L., Tiribelli, C. (2002) Mechanisms of bilirubin neurotoxicity. Hepatology 35, 1277-1280.
    • (2002) Hepatology , vol.35 , pp. 1277-1280
    • Ostrow, J.D.1    Pascolo, L.2    Tiribelli, C.3
  • 6
    • 0036238782 scopus 로고    scopus 로고
    • Bilirubin induces apoptosis via the mitochondrial pathway in developing rat brain neurons
    • Rodrigues, C. M., Sola, S., Brites, D. (2002) Bilirubin induces apoptosis via the mitochondrial pathway in developing rat brain neurons. Hepatology 35, 1186-1195.
    • (2002) Hepatology , vol.35 , pp. 1186-1195
    • Rodrigues, C.M.1    Sola, S.2    Brites, D.3
  • 7
    • 58249089412 scopus 로고    scopus 로고
    • The cytotoxic effect of unconjugated bilirubin in human neuroblastoma SH-SY5Y cells is modulated by the expression level of MRP1 but not MDR1
    • Corich, L., Aranda, A., Carrassa, L., Bellarosa, C., Ostrow, J. D., Tiribelli, C. (2009) The cytotoxic effect of unconjugated bilirubin in human neuroblastoma SH-SY5Y cells is modulated by the expression level of MRP1 but not MDR1. Biochem. J. 417, 305-312.
    • (2009) Biochem. J , vol.417 , pp. 305-312
    • Corich, L.1    Aranda, A.2    Carrassa, L.3    Bellarosa, C.4    Ostrow, J.D.5    Tiribelli, C.6
  • 10
    • 0036202904 scopus 로고    scopus 로고
    • Rat cultured neuronal and glial cells respond differently to toxicity of unconjugated bilirubin
    • Silva, R. F. M., Rodrigues, C. M. P., Brites, D. (2002) Rat cultured neuronal and glial cells respond differently to toxicity of unconjugated bilirubin. Pediatr. Res. 51, 535-541.
    • (2002) Pediatr. Res , vol.51 , pp. 535-541
    • Silva, R.F.M.1    Rodrigues, C.M.P.2    Brites, D.3
  • 11
    • 0036073635 scopus 로고    scopus 로고
    • Apoptosis in murine hepatoma hepa 1c1c7 wild-type, C12, and C4 cells mediated by bilirubin
    • Seubert, J. M., Darmon, A. J., El-Kadi, A. O., D'Souza, S. J., Bend, J. R. (2002) Apoptosis in murine hepatoma hepa 1c1c7 wild-type, C12, and C4 cells mediated by bilirubin. Mol. Pharmacol. 62, 257-264.
    • (2002) Mol. Pharmacol , vol.62 , pp. 257-264
    • Seubert, J.M.1    Darmon, A.J.2    El-Kadi, A.O.3    D'Souza, S.J.4    Bend, J.R.5
  • 12
    • 0030607714 scopus 로고    scopus 로고
    • Cytotoxicity of bilirubin for human fibroblasts and rat astrocytes in culture. Effect of the ratio of bilirubin to serum albumin
    • Chuniaud, L., Dessante, M., Chantoux, F., Blondeau, J. P., Francon, J., Trivin, F. (1996) Cytotoxicity of bilirubin for human fibroblasts and rat astrocytes in culture. Effect of the ratio of bilirubin to serum albumin. Clin. Chim. Acta 256, 103-114.
    • (1996) Clin. Chim. Acta , vol.256 , pp. 103-114
    • Chuniaud, L.1    Dessante, M.2    Chantoux, F.3    Blondeau, J.P.4    Francon, J.5    Trivin, F.6
  • 13
    • 33749989103 scopus 로고    scopus 로고
    • Bilirubin toxicity to human erythrocytes: A review
    • Alexandra Brito, M., Silva, R. F., Brites, D. (2006) Bilirubin toxicity to human erythrocytes: a review. Clin. Chim. Acta 374, 46-56.
    • (2006) Clin. Chim. Acta , vol.374 , pp. 46-56
    • Alexandra Brito, M.1    Silva, R.F.2    Brites, D.3
  • 14
    • 4644344388 scopus 로고    scopus 로고
    • Unconjugated bilirubin induces apoptosis in colon cancer cells by triggering mitochondrial depolarization
    • Keshavan, P., Schwemberger, S. J., Smith, D. L., Babcock, G. F., Zucker, S. D. (2004) Unconjugated bilirubin induces apoptosis in colon cancer cells by triggering mitochondrial depolarization. Int. J. Cancer 112, 433-445.
    • (2004) Int. J. Cancer , vol.112 , pp. 433-445
    • Keshavan, P.1    Schwemberger, S.J.2    Smith, D.L.3    Babcock, G.F.4    Zucker, S.D.5
  • 15
    • 0037192399 scopus 로고    scopus 로고
    • Bilirubin produces apoptosis in cultured bovine brain endothelial cells
    • Akin, E., Clower, B., Tibbs, R., Tang, J., Zhang, J. (2002) Bilirubin produces apoptosis in cultured bovine brain endothelial cells. Brain Res. 931, 168-175.
    • (2002) Brain Res , vol.931 , pp. 168-175
    • Akin, E.1    Clower, B.2    Tibbs, R.3    Tang, J.4    Zhang, J.5
  • 16
    • 0036191788 scopus 로고    scopus 로고
    • Bilirubin directly disrupts membrane lipid polarity and fluidity, protein order, and redox status in rat mitochondria
    • Rodrigues, C. M., Sola, S., Brito, M. A., Brites, D., Moura, J. J. (2002) Bilirubin directly disrupts membrane lipid polarity and fluidity, protein order, and redox status in rat mitochondria. J. Hepatol. 36, 335-341.
    • (2002) J. Hepatol , vol.36 , pp. 335-341
    • Rodrigues, C.M.1    Sola, S.2    Brito, M.A.3    Brites, D.4    Moura, J.J.5
  • 17
    • 0344234422 scopus 로고    scopus 로고
    • p38 MAP kinase mediates bilirubin-induced neuronal death of cultured rat cerebellar granule neurons
    • Lin, S., Yan, C., Wei, X., Paul, S. M., Du, Y. (2003) p38 MAP kinase mediates bilirubin-induced neuronal death of cultured rat cerebellar granule neurons. Neurosci. Lett. 353, 209-212.
    • (2003) Neurosci. Lett , vol.353 , pp. 209-212
    • Lin, S.1    Yan, C.2    Wei, X.3    Paul, S.M.4    Du, Y.5
  • 18
    • 0033669937 scopus 로고    scopus 로고
    • Bilirubin induces apoptosis via activation of NMDA receptors in developing rat brain neurons
    • Grojean, S., Koziel, V., Vert, P., Daval, J. L. (2000) Bilirubin induces apoptosis via activation of NMDA receptors in developing rat brain neurons. Exp. Neurol. 166, 334-341.
    • (2000) Exp. Neurol , vol.166 , pp. 334-341
    • Grojean, S.1    Koziel, V.2    Vert, P.3    Daval, J.L.4
  • 19
    • 0031846693 scopus 로고    scopus 로고
    • Modification of the MTT method for the study of bilirubin cytotoxicity
    • Ngai, K. C., Yeung, C. Y., Karlberg, J. (1998) Modification of the MTT method for the study of bilirubin cytotoxicity. Acta Paediatr. Jpn. 40, 313-317.
    • (1998) Acta Paediatr. Jpn , vol.40 , pp. 313-317
    • Ngai, K.C.1    Yeung, C.Y.2    Karlberg, J.3
  • 20
    • 4043058702 scopus 로고    scopus 로고
    • Bilirubin inhibits iNOS expression and NO production in response to endotoxin in rats
    • Wang, W. W., Smith, D. L., Zucker, S. D. (2004) Bilirubin inhibits iNOS expression and NO production in response to endotoxin in rats. Hepatology 40, 424-433.
    • (2004) Hepatology , vol.40 , pp. 424-433
    • Wang, W.W.1    Smith, D.L.2    Zucker, S.D.3
  • 21
    • 49649097976 scopus 로고    scopus 로고
    • Bilirubin possesses powerful immunomodulatory activity and suppresses experimental autoimmune encephalomyelitis
    • Liu, Y., Li, P., Lu, J., Xiong, W., Oger, J., Tetzlaff, W., Cynader, M. (2008) Bilirubin possesses powerful immunomodulatory activity and suppresses experimental autoimmune encephalomyelitis. J. Immunol. 181, 1887-1897.
    • (2008) J. Immunol , vol.181 , pp. 1887-1897
    • Liu, Y.1    Li, P.2    Lu, J.3    Xiong, W.4    Oger, J.5    Tetzlaff, W.6    Cynader, M.7
  • 23
    • 33645577621 scopus 로고    scopus 로고
    • Products of heme oxygenase and their potential therapeutic applications
    • Kirkby, K. A., Adin, C. A. (2006) Products of heme oxygenase and their potential therapeutic applications. Am. J. Physiol. Renal Physiol. 290, F563-F571.
    • (2006) Am. J. Physiol. Renal Physiol , vol.290
    • Kirkby, K.A.1    Adin, C.A.2
  • 26
    • 0030036986 scopus 로고    scopus 로고
    • Intracellular accumulation of unconjugated bilirubin inhibits phytohemagglutin-induced proliferation and interleukin-2 production of human lymphocytes
    • Haga, Y., Tempero, M. A., Kay, D., Zetterman, R. K. (1996) Intracellular accumulation of unconjugated bilirubin inhibits phytohemagglutin-induced proliferation and interleukin-2 production of human lymphocytes. Dig. Dis. Sci. 41, 1468-1474.
    • (1996) Dig. Dis. Sci , vol.41 , pp. 1468-1474
    • Haga, Y.1    Tempero, M.A.2    Kay, D.3    Zetterman, R.K.4
  • 27
    • 0030573972 scopus 로고    scopus 로고
    • Unconjugated bilirubin inhibits in vitro cytotoxic T lymphocyte activity of human lymphocyte
    • Haga, Y., Tempero, M. A., Zetterman, R. K. (1996) Unconjugated bilirubin inhibits in vitro cytotoxic T lymphocyte activity of human lymphocyte. Biochim. Biophys. Acta 1317, 65-70.
    • (1996) Biochim. Biophys. Acta , vol.1317 , pp. 65-70
    • Haga, Y.1    Tempero, M.A.2    Zetterman, R.K.3
  • 28
    • 0023792123 scopus 로고
    • The potential immunosuppressive effects of bilirubin
    • Miler, I., Síma, P., Vetvicka, V. (1988) The potential immunosuppressive effects of bilirubin. Allerg. Immunol. (Leipz.) 34, 177-184.
    • (1988) Allerg. Immunol. (Leipz.) , vol.34 , pp. 177-184
    • Miler, I.1    Síma, P.2    Vetvicka, V.3
  • 29
    • 0019295232 scopus 로고
    • The suppressive effects of continuous infusion of bilirubin on immumne response in mice
    • Síma, P., Mala, J., Miler, I., Hodr, R., Truxova, E. (1980) The suppressive effects of continuous infusion of bilirubin on immumne response in mice. Folia Microbiol. (Praha) 25, 483-490.
    • (1980) Folia Microbiol. (Praha) , vol.25 , pp. 483-490
    • Síma, P.1    Mala, J.2    Miler, I.3    Hodr, R.4    Truxova, E.5
  • 30
  • 31
    • 33750354325 scopus 로고    scopus 로고
    • Impaired T-lymphocyte proliferation function in biliary atresia patients with chronic cholestatic jaundice after a Kasai operation
    • Wu, J. F., Chiang, B. L., Chen, H. L., Lai, H. S., Chang, M. H., Ni, Y. H. (2006) Impaired T-lymphocyte proliferation function in biliary atresia patients with chronic cholestatic jaundice after a Kasai operation. Pediatr. Res. 60, 602-606.
    • (2006) Pediatr. Res , vol.60 , pp. 602-606
    • Wu, J.F.1    Chiang, B.L.2    Chen, H.L.3    Lai, H.S.4    Chang, M.H.5    Ni, Y.H.6
  • 32
    • 40749141616 scopus 로고    scopus 로고
    • Hyperbilirubinemia: A risk factor for infection in the surgical intensive care unit
    • Field, E., Horst, H. M., Rubinfeld, I. S., Copeland, C. F., Waheed, U., Jordan, J. (2008) Hyperbilirubinemia: a risk factor for infection in the surgical intensive care unit. Am. J. Surg. 195, 304-306.
    • (2008) Am. J. Surg , vol.195 , pp. 304-306
    • Field, E.1    Horst, H.M.2    Rubinfeld, I.S.3    Copeland, C.F.4    Waheed, U.5    Jordan, J.6
  • 33
    • 67650088580 scopus 로고    scopus 로고
    • Unbound (free) bilirubin: Improving the paradigm for evaluating neonatal jaundice
    • Ahlfors, C. E., Wennberg, R. P., Ostrow, J. D., Tiribelli, C. (2009) Unbound (free) bilirubin: improving the paradigm for evaluating neonatal jaundice. Clin. Chem. 55, 1288-1299.
    • (2009) Clin. Chem , vol.55 , pp. 1288-1299
    • Ahlfors, C.E.1    Wennberg, R.P.2    Ostrow, J.D.3    Tiribelli, C.4
  • 34
    • 34447136697 scopus 로고    scopus 로고
    • Bilirubin toxicity to human erythrocytes: A more sanguine view
    • McDonagh, A. F. (2007) Bilirubin toxicity to human erythrocytes: a more sanguine view. Pediatrics 120, 175-178.
    • (2007) Pediatrics , vol.120 , pp. 175-178
    • McDonagh, A.F.1
  • 35
    • 0035986194 scopus 로고    scopus 로고
    • Bilirubin induces loss of membrane lipids and exposure of phosphatidylserine in human erythrocytes
    • Brito, M. A., Silva, R. F. M., Brites, D. (2002) Bilirubin induces loss of membrane lipids and exposure of phosphatidylserine in human erythrocytes. Cell Biol. Toxicol. 18, 181-192.
    • (2002) Cell Biol. Toxicol , vol.18 , pp. 181-192
    • Brito, M.A.1    Silva, R.F.M.2    Brites, D.3
  • 37
    • 77954549811 scopus 로고    scopus 로고
    • Effect of bilirubin on cytochrome c oxidase activity of mitochondria from mouse brain and liver
    • Malik, S. G., Irwanto, K. A., Ostrow, J. D., Tiribelli, C. (2010) Effect of bilirubin on cytochrome c oxidase activity of mitochondria from mouse brain and liver. BMC Res. Notes 3, 162.
    • (2010) BMC Res. Notes , vol.3 , pp. 162
    • Malik, S.G.1    Irwanto, K.A.2    Ostrow, J.D.3    Tiribelli, C.4
  • 38
    • 0029131346 scopus 로고
    • Mechanisms of bilirubin toxicity
    • Amato, M. (1995) Mechanisms of bilirubin toxicity. Eur. J. Pediatr. 154 (Suppl. 4), S54-S59.
    • (1995) Eur. J. Pediatr , vol.154 , Issue.SUPPL. 4
    • Amato, M.1
  • 39
    • 0032897558 scopus 로고    scopus 로고
    • Antioxidant and cytotoxic effects of bilirubin on neonatal erythrocytes
    • Mireles, L. C., Lum, M. A., Dennery, P. A. (1999) Antioxidant and cytotoxic effects of bilirubin on neonatal erythrocytes. Pediatr. Res. 45, 355-362.
    • (1999) Pediatr. Res , vol.45 , pp. 355-362
    • Mireles, L.C.1    Lum, M.A.2    Dennery, P.A.3
  • 41
    • 0038647817 scopus 로고    scopus 로고
    • Reassessment of the unbound concentrations of unconjugated bilirubin in relation to neurotoxicity in vitro
    • Ostrow, J. D., Pascolo, L., Tiribelli, C. (2003) Reassessment of the unbound concentrations of unconjugated bilirubin in relation to neurotoxicity in vitro. Pediatr. Res. 54, 98-104.
    • (2003) Pediatr. Res , vol.54 , pp. 98-104
    • Ostrow, J.D.1    Pascolo, L.2    Tiribelli, C.3
  • 42
    • 0344868501 scopus 로고    scopus 로고
    • Bilirubin inhibits bile acid induced apoptosis in rat hepatocytes
    • Granato, A., Gores, G., Vilei, M. T., Tolando, R., Ferraresso, C., Muraca, M. (2003) Bilirubin inhibits bile acid induced apoptosis in rat hepatocytes. Gut 52, 1774-1778.
    • (2003) Gut , vol.52 , pp. 1774-1778
    • Granato, A.1    Gores, G.2    Vilei, M.T.3    Tolando, R.4    Ferraresso, C.5    Muraca, M.6
  • 43
    • 0015394313 scopus 로고
    • The ready isomerization of bilirubin IX-α in aqueous solution
    • McDonagh, A. F., Assisi, F. (1972) The ready isomerization of bilirubin IX-α in aqueous solution. Biochem. J. 129, 797-800.
    • (1972) Biochem. J , vol.129 , pp. 797-800
    • McDonagh, A.F.1    Assisi, F.2
  • 44
    • 59649115414 scopus 로고    scopus 로고
    • L-Arginine reverses radiation-induced immune dysfunction: The need for optimum treatment window
    • Shukla, J., Chatterjee, S., Thakur, V. S., Premachandran, S., Checker, R., Poduval, T. B. (2009) L-Arginine reverses radiation-induced immune dysfunction: the need for optimum treatment window. Radiat. Res. 171, 180-187.
    • (2009) Radiat. Res , vol.171 , pp. 180-187
    • Shukla, J.1    Chatterjee, S.2    Thakur, V.S.3    Premachandran, S.4    Checker, R.5    Poduval, T.B.6
  • 45
    • 79957963355 scopus 로고    scopus 로고
    • Pro-oxidants ameliorate radiation-induced apoptosis through activation of the calcium-ERK1/2-Nrf2 pathway
    • Khan, N. M., Sandur, S. K., Checker, R., Sharma, D., Poduval, T. B., Sainis, K. B. (2011) Pro-oxidants ameliorate radiation-induced apoptosis through activation of the calcium-ERK1/2-Nrf2 pathway. Free Radic. Biol. Med. 51, 115-128.
    • (2011) Free Radic. Biol. Med , vol.51 , pp. 115-128
    • Khan, N.M.1    Sandur, S.K.2    Checker, R.3    Sharma, D.4    Poduval, T.B.5    Sainis, K.B.6
  • 46
    • 78549280111 scopus 로고    scopus 로고
    • Differential activation of NF-κB and nitric oxide in lymphocytes regulates in vitro and in vivo radiosensitivity
    • Sharma, D., Sandur, S. K., Rashmi, R., Maurya, D. K., Suryavanshi, S., Checker, R., Sainis, K. B. (2010) Differential activation of NF-κB and nitric oxide in lymphocytes regulates in vitro and in vivo radiosensitivity. Mutat. Res. 703, 149-157.
    • (2010) Mutat. Res , vol.703 , pp. 149-157
    • Sharma, D.1    Sandur, S.K.2    Rashmi, R.3    Maurya, D.K.4    Suryavanshi, S.5    Checker, R.6    Sainis, K.B.7
  • 48
    • 77954910039 scopus 로고    scopus 로고
    • Plumbagin inhibits proliferative and inflammatory responses of T cells independent of ROS generation but by modulating intracellular thiols
    • Checker, R., Sharma, D., Sandur, S. K., Subrahmanyam, G., Krishnan, S., Poduval, T. B., Sainis, K. B. (2010) Plumbagin inhibits proliferative and inflammatory responses of T cells independent of ROS generation but by modulating intracellular thiols. J. Cell. Biochem. 110, 1082-1093.
    • (2010) J. Cell. Biochem , vol.110 , pp. 1082-1093
    • Checker, R.1    Sharma, D.2    Sandur, S.K.3    Subrahmanyam, G.4    Krishnan, S.5    Poduval, T.B.6    Sainis, K.B.7
  • 49
    • 34548762437 scopus 로고    scopus 로고
    • Glutathione depletion activates mitogen-activated protein kinase (MAPK) pathways that display organ-specific responses and brain protection in mice
    • Limón-Pacheco, J. H., Hernández, N. A., Fanjul-Moles, M. L., Gonsebatt, M. E. (2007) Glutathione depletion activates mitogen-activated protein kinase (MAPK) pathways that display organ-specific responses and brain protection in mice. Free Radic. Biol. Med. 43, 1335-1347.
    • (2007) Free Radic. Biol. Med , vol.43 , pp. 1335-1347
    • Limón-Pacheco, J.H.1    Hernández, N.A.2    Fanjul-Moles, M.L.3    Gonsebatt, M.E.4
  • 50
    • 0033520376 scopus 로고    scopus 로고
    • p38 Mitogen-activated protein kinase is involved in Fas ligand expression
    • Hsu, S. C., Gavrilin, M. A., Tsai, M. H., Hani, J., Lai, M. Z. (1999) p38 Mitogen-activated protein kinase is involved in Fas ligand expression. J. Biol. Chem. 274, 25769-25776.
    • (1999) J. Biol. Chem , vol.274 , pp. 25769-25776
    • Hsu, S.C.1    Gavrilin, M.A.2    Tsai, M.H.3    Hani, J.4    Lai, M.Z.5
  • 51
    • 10044219516 scopus 로고    scopus 로고
    • Activation of p38 MAPK is required for Bax translocation to mitochondria, cytochrome c release and apoptosis induced by UVB irradiation in human keratinocytes
    • Van Laethem, A., Kelst, S. V., Lippens, S., Declercq, W., Vandenabeele, P., Janssens, S. (2004) Activation of p38 MAPK is required for Bax translocation to mitochondria, cytochrome c release and apoptosis induced by UVB irradiation in human keratinocytes. FASEB J. 18, 1946-1948.
    • (2004) FASEB J , vol.18 , pp. 1946-1948
    • van Laethem, A.1    Kelst, S.V.2    Lippens, S.3    Declercq, W.4    Vandenabeele, P.5    Janssens, S.6
  • 52
    • 0029154990 scopus 로고
    • Uptake and distribution of N-acetylcysteine in mice: Tissue-specific effects on glutathione concentrations
    • McLellan, L. I., Lewis, A. D., Hall, D. J., Ansell, J. D., Wolf, C. R. (1995) Uptake and distribution of N-acetylcysteine in mice: tissue-specific effects on glutathione concentrations. Carcinogenesis 16, 2099-2106.
    • (1995) Carcinogenesis , vol.16 , pp. 2099-2106
    • McLellan, L.I.1    Lewis, A.D.2    Hall, D.J.3    Ansell, J.D.4    Wolf, C.R.5
  • 54
    • 45849105912 scopus 로고    scopus 로고
    • Cadmium specifically induces MKP-1 expression via the glutathione depletion-mediated p38 MAPK activation in C6 glioma cells
    • Kim, S. M., Jong, G. P., Won, K. B., Min, H. S., Hyung, L., Yooc, S. K., Kyung, H. J., Seong, I. S., Byeong, C. J. (2008) Cadmium specifically induces MKP-1 expression via the glutathione depletion-mediated p38 MAPK activation in C6 glioma cells. Neurosci. Lett. 440, 289-293.
    • (2008) Neurosci. Lett , vol.440 , pp. 289-293
    • Kim, S.M.1    Jong, G.P.2    Won, K.B.3    Min, H.S.4    Hyung, L.5    Yooc, S.K.6    Kyung, H.J.7    Seong, I.S.8    Byeong, C.J.9
  • 55
    • 4944257937 scopus 로고    scopus 로고
    • Glutathione depletion in CYP2E1-expressing liver cells induces toxicity due to the activation of p38 mitogen-activated protein kinase and reduction of nuclear factor-κB DNA binding activity
    • Wu, D., Arthur, C. (2004) Glutathione depletion in CYP2E1-expressing liver cells induces toxicity due to the activation of p38 mitogen-activated protein kinase and reduction of nuclear factor-κB DNA binding activity. Mol. Pharmacol. 66, 749-760.
    • (2004) Mol. Pharmacol , vol.66 , pp. 749-760
    • Wu, D.1    Arthur, C.2
  • 57
    • 0042031556 scopus 로고    scopus 로고
    • Bilirubin rinse: A simple protectant against the rat liver graft injury mimicking heme oxygenase-1 preconditioning
    • Kato, Y., Shimazu, M., Kondo, M., Uchida, K., Kumamoto, Y., Wakabayashi, G. (2003) Bilirubin rinse: a simple protectant against the rat liver graft injury mimicking heme oxygenase-1 preconditioning. Hepatology 38, 364-373.
    • (2003) Hepatology , vol.38 , pp. 364-373
    • Kato, Y.1    Shimazu, M.2    Kondo, M.3    Uchida, K.4    Kumamoto, Y.5    Wakabayashi, G.6
  • 59
    • 0015071632 scopus 로고
    • The enzymatic degradation of hemoglobin to bile pigments by macrophages
    • Pimstone, N. R., Tenhunen, R., Seitz, P. T., Marver, H. S., Schmid, R. (1971) The enzymatic degradation of hemoglobin to bile pigments by macrophages. J. Exp. Med. 133, 1264-1281.
    • (1971) J. Exp. Med , vol.133 , pp. 1264-1281
    • Pimstone, N.R.1    Tenhunen, R.2    Seitz, P.T.3    Marver, H.S.4    Schmid, R.5
  • 60
    • 34547879316 scopus 로고    scopus 로고
    • Serum albumin leads to false-positive results in the XTT and the MTT assay
    • Funk, D., Schrenk, H. H., Frei, E. (2007) Serum albumin leads to false-positive results in the XTT and the MTT assay. Biotechniques 43, 178-186.
    • (2007) Biotechniques , vol.43 , pp. 178-186
    • Funk, D.1    Schrenk, H.H.2    Frei, E.3
  • 61
    • 0035072101 scopus 로고    scopus 로고
    • Bilirubin-induced apoptosis in cultured rat neural cells is aggravated by chenodeoxycholic acid but prevented by ursodeoxycholic acid
    • Silva, R. F., Rodrigues, C. M., Brites, D. (2001) Bilirubin-induced apoptosis in cultured rat neural cells is aggravated by chenodeoxycholic acid but prevented by ursodeoxycholic acid. J. Hepatol. 34, 402-408.
    • (2001) J. Hepatol , vol.34 , pp. 402-408
    • Silva, R.F.1    Rodrigues, C.M.2    Brites, D.3
  • 62
    • 77950801520 scopus 로고    scopus 로고
    • Global changes in gene regulation demonstrate that unconjugated bilirubin is able to upregulate and activate select components of the endoplasmic reticulum stress response pathway
    • Oakes, G. H., Bend, J. R. (2010) Global changes in gene regulation demonstrate that unconjugated bilirubin is able to upregulate and activate select components of the endoplasmic reticulum stress response pathway. J. Biochem. Mol. Toxicol. 24, 73-88.
    • (2010) J. Biochem. Mol. Toxicol , vol.24 , pp. 73-88
    • Oakes, G.H.1    Bend, J.R.2
  • 63
    • 0037081744 scopus 로고    scopus 로고
    • The involvement of l-γ-glutamyl-l-cysteinyl-glycine (glutahthione/GSH) in the mechanism of redox signaling mediating MAPKp38-dependent regulation of cytokine production
    • Haddad, J. J. (2002) The involvement of l-γ-glutamyl-l-cysteinyl-glycine (glutahthione/GSH) in the mechanism of redox signaling mediating MAPKp38-dependent regulation of cytokine production. Biochem. Pharmacol. 63, 305-320.
    • (2002) Biochem. Pharmacol , vol.63 , pp. 305-320
    • Haddad, J.J.1
  • 64
    • 0030789179 scopus 로고    scopus 로고
    • The level of intracellular glutathione is a key regulator for the induction of stressactivated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents
    • Wilhelm, D., Bender, K., Knebel, A., Angel, P. (1997) The level of intracellular glutathione is a key regulator for the induction of stressactivated signal transduction pathways including Jun N-terminal protein kinases and p38 kinase by alkylating agents. Mol. Cell. Biol. 17, 4792-4800.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 4792-4800
    • Wilhelm, D.1    Bender, K.2    Knebel, A.3    Angel, P.4
  • 65
    • 70349172938 scopus 로고    scopus 로고
    • Apoptosis and glutathione: Beyond an antioxidant
    • Franco, R., Cidlowski, J. A. (2009) Apoptosis and glutathione: beyond an antioxidant. Cell Death Differ. 16, 1303-1314.
    • (2009) Cell Death Differ , vol.16 , pp. 1303-1314
    • Franco, R.1    Cidlowski, J.A.2
  • 66
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker, R., Yamamoto, Y., McDonagh, A. F., Glazer, A. N., 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
  • 67
    • 34447309034 scopus 로고    scopus 로고
    • Bilirubin as an antioxidant in micelles and lipid bilayers: Its contribution to the total antioxidant capacity of human blood plasma
    • MacLean, P. D., Drake, E. C., Ross, L., Barclay, C. (2007) Bilirubin as an antioxidant in micelles and lipid bilayers: its contribution to the total antioxidant capacity of human blood plasma. Free Radic. Biol. Med. 43, 600-609.
    • (2007) Free Radic. Biol. Med , vol.43 , pp. 600-609
    • McLean, P.D.1    Drake, E.C.2    Ross, L.3    Barclay, C.4
  • 68
    • 70449399294 scopus 로고    scopus 로고
    • Redox state, oxidative stress, and molecular mechanisms of protective and toxic effects of bilirubin on cells
    • Tell, G., Gustincich, S. (2009) Redox state, oxidative stress, and molecular mechanisms of protective and toxic effects of bilirubin on cells. Curr. Pharm. Des. 15, 2908-2914.
    • (2009) Curr. Pharm. Des , vol.15 , pp. 2908-2914
    • Tell, G.1    Gustincich, S.2
  • 70
  • 71
    • 35649013187 scopus 로고    scopus 로고
    • Glutathione depletion is necessary for apoptosis in lymphoid cells independent of reactive oxygen species formation
    • Franco, R., Mihalis, I. P., John, A. C. (2007) Glutathione depletion is necessary for apoptosis in lymphoid cells independent of reactive oxygen species formation. J. Biol. Chem. 282, 30452-30465.
    • (2007) J. Biol. Chem , vol.282 , pp. 30452-30465
    • Franco, R.1    Mihalis, I.P.2    John, A.C.3
  • 72
    • 45149124114 scopus 로고    scopus 로고
    • Apoptosis in arsenic trioxide-treated Calu-6 lung cells is correlated with the depletion of GSH levels rather than the changes of ROS levels
    • Han, Y. H., Kim, S. H., Kim, S. Z., Park, W. H. (2008) Apoptosis in arsenic trioxide-treated Calu-6 lung cells is correlated with the depletion of GSH levels rather than the changes of ROS levels. J. Cell. Biochem. 104, 862-878.
    • (2008) J. Cell. Biochem , vol.104 , pp. 862-878
    • Han, Y.H.1    Kim, S.H.2    Kim, S.Z.3    Park, W.H.4
  • 73
    • 0028939139 scopus 로고
    • Programmed cell death and Bcl-2 protection in very low oxygen
    • Jacobson, M. D., Raff, M. C. (1995) Programmed cell death and Bcl-2 protection in very low oxygen. Nature 374, 814-816.
    • (1995) Nature , vol.374 , pp. 814-816
    • Jacobson, M.D.1    Raff, M.C.2
  • 74
    • 40449133369 scopus 로고    scopus 로고
    • Apoptosis in pyrogallol-treated Calu-6 cells is correlated with the changes of intracellular GSH levels rather than ROS levels
    • Han, Y. H., Kim, S. Z., Kim, S. H., Park, W. H. (2008) Apoptosis in pyrogallol-treated Calu-6 cells is correlated with the changes of intracellular GSH levels rather than ROS levels. Lung Cancer 59, 301-314.
    • (2008) Lung Cancer , vol.59 , pp. 301-314
    • Han, Y.H.1    Kim, S.Z.2    Kim, S.H.3    Park, W.H.4
  • 75
    • 2542577882 scopus 로고    scopus 로고
    • Bilirubin benefits: Cellular protection by a biliverdin reductase antioxidant cycle
    • Sedlak, T. W., Snyder, S. H. (2004) Bilirubin benefits: cellular protection by a biliverdin reductase antioxidant cycle. Pediatrics 113, 1776-1782.
    • (2004) Pediatrics , vol.113 , pp. 1776-1782
    • Sedlak, T.W.1    Snyder, S.H.2


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