메뉴 건너뛰기




Volumn 38, Issue 1, 2005, Pages 85-92

Distinct protective mechanisms of HO-1 and HO-2 against hydroperoxide-induced cytotoxicity

Author keywords

Cytochrome P 450 reductase; Endoplasmic reticulum; Free radicals; Heme oxygenase; Microsome; Prostaglandins; Subcellular localization

Indexed keywords

HEME OXYGENASE 1; HEME OXYGENASE 2; HEMIN; HYDROGEN PEROXIDE; ISOENZYME; PROSTAGLANDIN DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; TERT BUTYL HYDROPEROXIDE;

EID: 10344219952     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.09.031     Document Type: Article
Times cited : (58)

References (41)
  • 1
    • 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 2002 1276 1282
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1276-1282
    • Doré, S.1
  • 2
    • 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
  • 3
    • 0242525192 scopus 로고    scopus 로고
    • The heme oxygenase dilemma in cellular homeostasis: New insights for the feedback regulation of heme catabolism
    • S. Shibahara The heme oxygenase dilemma in cellular homeostasis: new insights for the feedback regulation of heme catabolism J. Tohoku, Exp. Med. 200 2003 167 186
    • (2003) J. Tohoku, Exp. Med. , vol.200 , pp. 167-186
    • Shibahara, S.1
  • 6
    • 0023029882 scopus 로고
    • Cadmium-mediated inhibition of testicular heme oxygenase activity: The role of NADPH-cytochrome c (P-450) reductase
    • G.M. Trakshel, R.K. Kutty, and M.D. Maines Cadmium-mediated inhibition of testicular heme oxygenase activity: the role of NADPH-cytochrome c (P-450) reductase Arch. Biochem. Biophys. 251 1986 175 187
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 175-187
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 7
    • 0034638487 scopus 로고    scopus 로고
    • Alteration of expression levels of neuronal nitric oxide synthase and haem oxygenase-2 messenger RNA in the hippocampi and cortices of young adult and aged cognitively unimpaired and impaired Long-Evans rats
    • S. Doré, A. Law, S. Blackshaw, S. Gauthier, and R. Quirion Alteration of expression levels of neuronal nitric oxide synthase and haem oxygenase-2 messenger RNA in the hippocampi and cortices of young adult and aged cognitively unimpaired and impaired Long-Evans rats Neuroscience 100 2000 769 775
    • (2000) Neuroscience , vol.100 , pp. 769-775
    • Doré, S.1    Law, A.2    Blackshaw, S.3    Gauthier, S.4    Quirion, R.5
  • 8
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • W.K. McCoubrey Jr., T.J. Huang, and M.D. Maines Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3 Eur. J. Biochem. 247 1997 725 732
    • (1997) Eur. J. Biochem. , vol.247 , pp. 725-732
    • McCoubrey Jr., W.K.1    Huang, T.J.2    Maines, M.D.3
  • 9
    • 0037713341 scopus 로고    scopus 로고
    • Potential mechanism by which resveratrol, a red wine constituent, protects neurons
    • H. Zhuang, Y.S. Kim, R.C. Koehler, and S. Doré Potential mechanism by which resveratrol, a red wine constituent, protects neurons Ann. N. Y. Acad. Sci. 993 2003 276 286 (discussion 287-288)
    • (2003) Ann. N. Y. Acad. Sci. , vol.993 , pp. 276-286
    • Zhuang, H.1    Kim, Y.S.2    Koehler, R.C.3    Doré, S.4
  • 11
    • 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, and 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
  • 12
    • 0028300334 scopus 로고
    • Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts
    • G.F. Vile, S. Basu-Modak, C. Waltner, and R.M. Tyrrell Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts Proc. Natl. Acad. Sci. U. S. A. 91 1994 2607 2610
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 2607-2610
    • Vile, G.F.1    Basu-Modak, S.2    Waltner, C.3    Tyrrell, R.M.4
  • 13
    • 0028941025 scopus 로고
    • Acquired resistance to acute oxidative stress. Possible role of heme oxygenase and ferritin
    • B.A. Vogt, J. Alam, A.J. Croatt, G.M. Vercellotti, and K.A. Nath Acquired resistance to acute oxidative stress. Possible role of heme oxygenase and ferritin Lab. Invest. 72 1995 474 483
    • (1995) Lab. Invest. , vol.72 , pp. 474-483
    • Vogt, B.A.1    Alam, J.2    Croatt, A.J.3    Vercellotti, G.M.4    Nath, K.A.5
  • 14
    • 0028879538 scopus 로고
    • Relationship of lead-induced proteins to stress response proteins in astroglial cells
    • L.A. Opanashuk, and J.N. Finkelstein Relationship of lead-induced proteins to stress response proteins in astroglial cells J. Neurosci. Res. 42 1995 623 632
    • (1995) J. Neurosci. Res. , vol.42 , pp. 623-632
    • Opanashuk, L.A.1    Finkelstein, J.N.2
  • 17
    • 0015501157 scopus 로고
    • Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system
    • B.A. Schacter, E.B. Nelson, H.S. Marver, and B.S. Masters Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system J. Biol. Chem. 247 1972 3601 3607
    • (1972) J. Biol. Chem. , vol.247 , pp. 3601-3607
    • Schacter, B.A.1    Nelson, E.B.2    Marver, H.S.3    Masters, B.S.4
  • 18
    • 0019332526 scopus 로고
    • Oxygenated form of heme•heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex
    • T. Yoshida, M. Noguchi, and G. Kikuchi Oxygenated form of heme•heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex J. Biol. Chem. 255 1980 4418 4420
    • (1980) J. Biol. Chem. , vol.255 , pp. 4418-4420
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3
  • 19
    • 0020479233 scopus 로고
    • The occurrence of molecular interactions among NADPH-cytochrome c reductase, heme oxygenase, and biliverdin reductase in heme degradation
    • T. Yoshinaga, S. Sassa, and A. Kappas The occurrence of molecular interactions among NADPH-cytochrome c reductase, heme oxygenase, and biliverdin reductase in heme degradation J. Biol. Chem. 257 1982 7786 7793
    • (1982) J. Biol. Chem. , vol.257 , pp. 7786-7793
    • Yoshinaga, T.1    Sassa, S.2    Kappas, A.3
  • 20
    • 0027440198 scopus 로고
    • Rat liver heme oxygenase: High level expression of a truncated soluble form and nature of the meso-hydroxylating species
    • A. Wilks, and P.R. Ortiz de Montellano Rat liver heme oxygenase: high level expression of a truncated soluble form and nature of the meso-hydroxylating species J. Biol. Chem. 268 1993 22357 22362
    • (1993) J. Biol. Chem. , vol.268 , pp. 22357-22362
    • Wilks, A.1    Ortiz De Montellano, P.R.2
  • 21
    • 0026496121 scopus 로고
    • Effect of oxidant stress on calcium signaling in vascular endothelial cells
    • S.J. Elliott, J.G. Meszaros, and W.P. Schilling Effect of oxidant stress on calcium signaling in vascular endothelial cells Free Radic. Biol. Med. 1992 635 650
    • (1992) Free Radic. Biol. Med. , pp. 635-650
    • Elliott, S.J.1    Meszaros, J.G.2    Schilling, W.P.3
  • 26
    • 0024496298 scopus 로고
    • Detection of peroxyl and alkoxyl radicals produced by reaction of hydroperoxides with rat liver microsomal fractions
    • M.J. Davies Detection of peroxyl and alkoxyl radicals produced by reaction of hydroperoxides with rat liver microsomal fractions Biochem. J. 257 1989 603 606
    • (1989) Biochem. J. , vol.257 , pp. 603-606
    • Davies, M.J.1
  • 27
    • 0034098993 scopus 로고    scopus 로고
    • Subcellular localization of presenilins: Association with a unique membrane pool in cultured cells
    • S.H. Kim, J.J. Lah, G. Thinakaran, A. Levey, and S.S. Sisodia Subcellular localization of presenilins: association with a unique membrane pool in cultured cells Neurobiol. Dis. 7 2000 99 117
    • (2000) Neurobiol. Dis. , vol.7 , pp. 99-117
    • Kim, S.H.1    Lah, J.J.2    Thinakaran, G.3    Levey, A.4    Sisodia, S.S.5
  • 28
    • 0038051202 scopus 로고    scopus 로고
    • Prostaglandins of J series control heme oxygenase expression: Potential significance in modulating neuroinflammation
    • H. Zhuang, Y.S. Kim, K. Namiranian, and S. Doré Prostaglandins of J series control heme oxygenase expression: potential significance in modulating neuroinflammation Ann. N. Y. Acad. Sci. 993 2003 208 216
    • (2003) Ann. N. Y. Acad. Sci. , vol.993 , pp. 208-216
    • Zhuang, H.1    Kim, Y.S.2    Namiranian, K.3    Doré, S.4
  • 29
    • 0023854047 scopus 로고
    • Evidence suggesting that the two forms of heme oxygenase are products of different genes
    • I. Cruse, and M.D. Maines Evidence suggesting that the two forms of heme oxygenase are products of different genes J. Biol. Chem. 263 1988 3348 3353
    • (1988) J. Biol. Chem. , vol.263 , pp. 3348-3353
    • Cruse, I.1    Maines, M.D.2
  • 34
    • 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 2003 525 532
    • (2003) IUBMB Life , vol.55 , 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
  • 35
    • 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 2003 50999 51005
    • (2003) J. Biol. Chem. , vol.278 , pp. 50999-51005
    • Weng, Y.H.1    Yang, G.2    Weiss, S.3    Dennery, P.A.4
  • 37
    • 0027176344 scopus 로고
    • Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain
    • J.F. Ewing, C.M. Weber, and M.D. Maines Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain J. Neurochem. 61 1993 1015 1023
    • (1993) J. Neurochem. , vol.61 , pp. 1015-1023
    • Ewing, J.F.1    Weber, C.M.2    Maines, M.D.3
  • 38
    • 0038051345 scopus 로고    scopus 로고
    • Mitochondria, oxidative damage, and inflammation in Parkinson's disease
    • M.F. Beal Mitochondria, oxidative damage, and inflammation in Parkinson's disease Ann. N. Y. Acad. Sci. 991 2003 120 131
    • (2003) Ann. N. Y. Acad. Sci. , vol.991 , pp. 120-131
    • Beal, M.F.1
  • 39
    • 0023853836 scopus 로고
    • Cytochrome P-450-dependent oxidase activity and hydroxyl radical production in micellar and membranous types of reconstituted systems
    • Y. Terelius, and M. Ingelman-Sundberg Cytochrome P-450-dependent oxidase activity and hydroxyl radical production in micellar and membranous types of reconstituted systems Biochem. Pharmacol. 37 1988 1383 1389
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 1383-1389
    • Terelius, Y.1    Ingelman-Sundberg, M.2
  • 41
    • 0029900542 scopus 로고    scopus 로고
    • ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide
    • D.P. Barr, M.R. Gunther, L.J. Deterding, K.B. Tomer, and R.P. Mason ESR spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide J. Biol. Chem. 271 1996 15498 15503
    • (1996) J. Biol. Chem. , vol.271 , pp. 15498-15503
    • Barr, D.P.1    Gunther, M.R.2    Deterding, L.J.3    Tomer, K.B.4    Mason, R.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.