메뉴 건너뛰기




Volumn 39, Issue 4, 2005, Pages 558-564

Catalytically inactive heme oxygenase-2 mutant is cytoprotective

Author keywords

Bilirubin; Carbon monoxide; Hemin; Hydrogen peroxide; Iron

Indexed keywords

HEME; HEME OXYGENASE 2; HEMIN; HYDROGEN PEROXIDE; MUTANT PROTEIN; OXIDIZING AGENT; PROTEIN;

EID: 22544454485     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2005.04.009     Document Type: Article
Times cited : (30)

References (31)
  • 1
    • 0024241523 scopus 로고
    • Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation
    • J.M. Gutteridge, and A. Smith Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation Biochem. J. 256 3 1988 861 865
    • (1988) Biochem. J. , vol.256 , Issue.3 , pp. 861-865
    • Gutteridge, J.M.1    Smith, A.2
  • 2
    • 0021322523 scopus 로고
    • Hemin-mediated oxidative degradation of proteins
    • R.L. Aft, and G.C. Mueller Hemin-mediated oxidative degradation of proteins J. Biol. Chem. 259 1 1984 301 305
    • (1984) J. Biol. Chem. , vol.259 , Issue.1 , pp. 301-305
    • Aft, R.L.1    Mueller, G.C.2
  • 3
    • 0021100151 scopus 로고
    • Hemin-mediated DNA strand scission
    • R.L. Aft, and G.C. Mueller Hemin-mediated DNA strand scission J. Biol. Chem. 258 19 1983 12069 12072
    • (1983) J. Biol. Chem. , vol.258 , Issue.19 , pp. 12069-12072
    • Aft, R.L.1    Mueller, G.C.2
  • 4
    • 0022668643 scopus 로고
    • On the mechanism of the chemical and enzymic oxygenations of alpha-oxyprotohemin IX to Fe.biliverdin IX alpha
    • S. Sano, T. Sano, I. Morishima, Y. Shiro, and Y. Maeda On the mechanism of the chemical and enzymic oxygenations of alpha-oxyprotohemin IX to Fe.biliverdin IX alpha Proc. Natl. Acad. Sci. USA 83 3 1986 531 535
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , Issue.3 , pp. 531-535
    • Sano, S.1    Sano, T.2    Morishima, I.3    Shiro, Y.4    Maeda, Y.5
  • 8
    • 0022632224 scopus 로고
    • Characterization of two constitutive forms of rat liver microsomal heme oxygenase. only one molecular species of the enzyme is inducible
    • M.D. Maines, G.M. Trakshel, and R.K. Kutty Characterization of two constitutive forms of rat liver microsomal heme oxygenase. Only one molecular species of the enzyme is inducible J. Biol. Chem. 261 1 1986 411 419
    • (1986) J. Biol. Chem. , vol.261 , Issue.1 , pp. 411-419
    • Maines, M.D.1    Trakshel, G.M.2    Kutty, R.K.3
  • 9
    • 0037096194 scopus 로고    scopus 로고
    • Decreased activity of the antioxidant heme oxygenase enzyme: Implications in ischemia and in Alzheimer's disease
    • S. Doré Decreased activity of the antioxidant heme oxygenase enzyme: implications in ischemia and in Alzheimer's disease Free Radic. Biol. Med. 32 12 2002 1276 1282
    • (2002) Free Radic. Biol. Med. , vol.32 , Issue.12 , pp. 1276-1282
    • Doré, S.1
  • 14
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • T. Mosmann Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays J. Immunol. Methods 65 1-2 1983 55 63
    • (1983) J. Immunol. Methods , vol.65 , Issue.1-2 , pp. 55-63
    • Mosmann, T.1
  • 15
    • 10344219952 scopus 로고    scopus 로고
    • Distinct protective mechanisms of HO-1 and HO-2 against hydroperoxide-induced cytotoxicity
    • Y.S. Kim, H. Zhuang, R.C. Koehler, and S. Doré Distinct protective mechanisms of HO-1 and HO-2 against hydroperoxide-induced cytotoxicity Free Radic. Biol. Med. 38 1 2005 85 92
    • (2005) Free Radic. Biol. Med. , vol.38 , Issue.1 , pp. 85-92
    • Kim, Y.S.1    Zhuang, H.2    Koehler, R.C.3    Doré, S.4
  • 16
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • M.D. Maines The heme oxygenase system: a regulator of second messenger gases Annu. Rev. Pharmacol. Toxicol. 37 1997 517 554
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 17
    • 4544220638 scopus 로고    scopus 로고
    • Why heme needs to be degraded to iron, biliverdin IXalpha, and carbon monoxide?
    • S. Sassa Why heme needs to be degraded to iron, biliverdin IXalpha, and carbon monoxide? Antioxid. Redox. Signal. 6 5 2004 819 824
    • (2004) Antioxid. Redox. Signal. , vol.6 , Issue.5 , pp. 819-824
    • Sassa, S.1
  • 19
    • 0026310705 scopus 로고
    • The cytoprotective effects of bilirubin and biliverdin on rat hepatocytes and human erythrocytes and the impact of albumin
    • T.W. Wu, D. Carey, J. Wu, and H. Sugiyama The cytoprotective effects of bilirubin and biliverdin on rat hepatocytes and human erythrocytes and the impact of albumin Biochem. Cell Biol. 69 12 1991 828 834
    • (1991) Biochem. Cell Biol. , vol.69 , Issue.12 , pp. 828-834
    • Wu, T.W.1    Carey, D.2    Wu, J.3    Sugiyama, H.4
  • 20
    • 0032738907 scopus 로고    scopus 로고
    • Hemoglobin and iron-evoked oxidative stress in the brain: Protection by bile pigments, manganese and S-nitrosoglutathione
    • P. Van Bergen, P. Rauhala, C.M. Spooner, and C.C. Chiueh Hemoglobin and iron-evoked oxidative stress in the brain: protection by bile pigments, manganese and S-nitrosoglutathione Free Radic. Res. 31 6 1999 631 640
    • (1999) Free Radic. Res. , vol.31 , Issue.6 , pp. 631-640
    • Van Bergen, P.1    Rauhala, P.2    Spooner, C.M.3    Chiueh, C.C.4
  • 21
    • 0020314348 scopus 로고
    • Identification of the product of heme degradation catalyzed by the heme oxygenase system as biliverdin IX alpha by reversed-phase high- performance liquid chromatography
    • M. Noguchi, T. Yoshida, and G. Kikuchi Identification of the product of heme degradation catalyzed by the heme oxygenase system as biliverdin IX alpha by reversed-phase high- performance liquid chromatography J. Biochem. (Tokyo) 91 5 1982 1479 1483
    • (1982) J. Biochem. (Tokyo) , vol.91 , Issue.5 , pp. 1479-1483
    • Noguchi, M.1    Yoshida, T.2    Kikuchi, G.3
  • 22
    • 0037173578 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells
    • R.R. Crichton, S. Wilmet, R. Legssyer, and R.J. Ward Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells J. Inorg. Biochem. 91 1 2002 9 18
    • (2002) J. Inorg. Biochem. , vol.91 , Issue.1 , pp. 9-18
    • Crichton, R.R.1    Wilmet, S.2    Legssyer, R.3    Ward, R.J.4
  • 23
    • 0027255106 scopus 로고
    • Oxidative stress resulting from ultraviolet a irradiation of human skin fibroblasts leads to a heme oxygenase-dependent increase in ferritin
    • G.F. Vile, and R.M. Tyrrell Oxidative stress resulting from ultraviolet A irradiation of human skin fibroblasts leads to a heme oxygenase-dependent increase in ferritin J. Biol. Chem. 268 20 1993 14678 14681
    • (1993) J. Biol. Chem. , vol.268 , Issue.20 , pp. 14678-14681
    • Vile, G.F.1    Tyrrell, R.M.2
  • 24
    • 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, and 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 12 1998 1057 1065
    • (1998) Can. J. Physiol. Pharmacol. , vol.76 , Issue.12 , pp. 1057-1065
    • Vreman, H.J.1    Wong, R.J.2    Sanesi, C.A.3    Dennery, P.A.4    Stevenson, D.K.5
  • 25
    • 0020353758 scopus 로고
    • The step of carbon monoxide liberation in the sequence of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system
    • T. Yoshida, M. Noguchi, and G. Kikuchi The step of carbon monoxide liberation in the sequence of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system J. Biol. Chem. 257 16 1982 9345 9348
    • (1982) J. Biol. Chem. , vol.257 , Issue.16 , pp. 9345-9348
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3
  • 27
    • 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
    • S. Brouard, P.O. Berberat, E. Tobiasch, M.P. Seldon, F.H. Bach, and M.P. Soares 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 20 2002 17950 17961
    • (2002) J. Biol. Chem. , vol.277 , Issue.20 , 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
  • 29
    • 0344012607 scopus 로고    scopus 로고
    • Evidence for heme oxygenase-1 association with caveolin-1 and -2 in mouse mesangial cells
    • N.H. Jung, H.P. Kim, B.R. Kim, S.H. Cha, G.A. Kim, H. Ha, Y.E. Na, and Y.N. Cha Evidence for heme oxygenase-1 association with caveolin-1 and -2 in mouse mesangial cells IUBMB Life 55 9 2003 525 532
    • (2003) IUBMB Life , vol.55 , Issue.9 , pp. 525-532
    • Jung, N.H.1    Kim, H.P.2    Kim, B.R.3    Cha, S.H.4    Kim, G.A.5    Ha, H.6    Na, Y.E.7    Cha, Y.N.8
  • 30
    • 3042737456 scopus 로고    scopus 로고
    • Caveolae compartmentalization of heme oxygenase-1 in endothelial cells
    • H.P. Kim, X. Wang, F. Galbiati, S.W. Ryter, and A.M. Choi Caveolae compartmentalization of heme oxygenase-1 in endothelial cells FASEB J. 18 10 2004 1080 1089
    • (2004) FASEB J. , vol.18 , Issue.10 , pp. 1080-1089
    • Kim, H.P.1    Wang, X.2    Galbiati, F.3    Ryter, S.W.4    Choi, A.M.5
  • 31
    • 0347065363 scopus 로고    scopus 로고
    • Interaction between heme oxygenase-1 and -2 proteins
    • Y.H. Weng, G. Yang, S. Weiss, and P.A. Dennery Interaction between heme oxygenase-1 and -2 proteins J. Biol. Chem. 278 51 2003 50999 51005
    • (2003) J. Biol. Chem. , vol.278 , Issue.51 , pp. 50999-51005
    • Weng, Y.H.1    Yang, G.2    Weiss, S.3    Dennery, P.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.