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Volumn 181, Issue 1, 2009, Pages 52-60

Involvement of an aldo-keto reductase (AKR1C3) in redox cycling of 9,10-phenanthrenequinone leading to apoptosis in human endothelial cells

Author keywords

9,10 Phenanthrenequinone; Aldo keto reductase 1C3; Apoptosis; Endothelial cells; Oxidative stress; Redox cycling

Indexed keywords

ALDO KETO REDUCTASE 1C3; CASPASE; FLUFENAMIC ACID; GLUTATHIONE; INDOMETACIN; MESSENGER RNA; OXIDOREDUCTASE; PHENANTHRENEQUINONE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 67650663252     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2009.05.005     Document Type: Article
Times cited : (40)

References (52)
  • 1
    • 0005312032 scopus 로고    scopus 로고
    • Biological effects of diesel exhaust particles (DEP). III. Pathogenesis of asthma like symptoms in mice
    • Sagai M., Furuyama A., and Ichinose T. Biological effects of diesel exhaust particles (DEP). III. Pathogenesis of asthma like symptoms in mice. Free Radic. Biol. Med. 21 (1996) 199-209
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 199-209
    • Sagai, M.1    Furuyama, A.2    Ichinose, T.3
  • 2
    • 0036558481 scopus 로고    scopus 로고
    • Allergic susceptibility associated with diesel exhaust particle exposure: clear as mud
    • Polosa R., Salvi S., and Di Maria G.U. Allergic susceptibility associated with diesel exhaust particle exposure: clear as mud. Arch. Environ. Health 57 (2002) 188-193
    • (2002) Arch. Environ. Health , vol.57 , pp. 188-193
    • Polosa, R.1    Salvi, S.2    Di Maria, G.U.3
  • 3
    • 0033571350 scopus 로고    scopus 로고
    • Chemicals in diesel exhaust particles generate reactive oxygen radicals and induce apoptosis in macrophages
    • Hiura T.S., Kaszubowski M.P., Li N., and Nel A.E. Chemicals in diesel exhaust particles generate reactive oxygen radicals and induce apoptosis in macrophages. J. Immunol. 163 (1999) 5582-5591
    • (1999) J. Immunol. , vol.163 , pp. 5582-5591
    • Hiura, T.S.1    Kaszubowski, M.P.2    Li, N.3    Nel, A.E.4
  • 5
    • 11344291782 scopus 로고    scopus 로고
    • 9,10-Phenanthraquinone in diesel exhaust particles downregulates Cu,Zn-SOD and HO-1 in human pulmonary epithelial cells: intracellular iron scavenger 1,10-phenanthroline affords protection against apoptosis
    • Sugimoto R., Kumagai Y., Nakai Y., and Ishii T. 9,10-Phenanthraquinone in diesel exhaust particles downregulates Cu,Zn-SOD and HO-1 in human pulmonary epithelial cells: intracellular iron scavenger 1,10-phenanthroline affords protection against apoptosis. Free Radic. Biol. Med. 38 (2005) 388-395
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 388-395
    • Sugimoto, R.1    Kumagai, Y.2    Nakai, Y.3    Ishii, T.4
  • 6
    • 29044434447 scopus 로고    scopus 로고
    • Sequence dependence of charge transport through DNA domains
    • Shao F., Augustyn K., and Barton J.K. Sequence dependence of charge transport through DNA domains. J. Am. Chem. Soc. 127 (2005) 17445-17452
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17445-17452
    • Shao, F.1    Augustyn, K.2    Barton, J.K.3
  • 8
    • 0031034402 scopus 로고    scopus 로고
    • Generation of reactive oxygen species during interaction of diesel exhaust particle components with NADPH-cytochrome P450 reductase and involvement of the bioactivation in the DNA damage
    • Kumagai Y., Arimoto T., Shinyashiki M., Shimojo N., Nakai Y., Yoshikawa T., and Sagai M. Generation of reactive oxygen species during interaction of diesel exhaust particle components with NADPH-cytochrome P450 reductase and involvement of the bioactivation in the DNA damage. Free Radic. Biol. Med. 22 (1997) 479-487
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 479-487
    • Kumagai, Y.1    Arimoto, T.2    Shinyashiki, M.3    Shimojo, N.4    Nakai, Y.5    Yoshikawa, T.6    Sagai, M.7
  • 9
    • 0026331348 scopus 로고
    • Polycyclic aromatic hydrocarbon quinone-mediated oxidation reduction cycling catalyzed by a human placental NADPH-linked carbonyl reductase
    • Jarabak J. Polycyclic aromatic hydrocarbon quinone-mediated oxidation reduction cycling catalyzed by a human placental NADPH-linked carbonyl reductase. Arch. Biochem. Biophys. 291 (1991) 334-338
    • (1991) Arch. Biochem. Biophys. , vol.291 , pp. 334-338
    • Jarabak, J.1
  • 10
    • 23944455857 scopus 로고    scopus 로고
    • Involvement of carbonyl reductase in superoxide formation through redox cycling of adrenochrome and 9,10-phenanthrenequinone in pig heart
    • Oginuma M., Shimada H., and Imamura Y. Involvement of carbonyl reductase in superoxide formation through redox cycling of adrenochrome and 9,10-phenanthrenequinone in pig heart. Chem. Biol. Interact. 155 (2005) 148-154
    • (2005) Chem. Biol. Interact. , vol.155 , pp. 148-154
    • Oginuma, M.1    Shimada, H.2    Imamura, Y.3
  • 11
    • 39949085604 scopus 로고    scopus 로고
    • l-Xylulose reductase is involved in 9,10-phenanthrenequinone-induced apoptosis in human T lymphoma cells
    • Matsunaga T., Kamiya T., Sumi D., Kumagai Y., Kalyanaraman B., and Hara A. l-Xylulose reductase is involved in 9,10-phenanthrenequinone-induced apoptosis in human T lymphoma cells. Free Radic. Biol. Med. 44 (2008) 1191-1202
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1191-1202
    • Matsunaga, T.1    Kamiya, T.2    Sumi, D.3    Kumagai, Y.4    Kalyanaraman, B.5    Hara, A.6
  • 12
    • 33645963469 scopus 로고    scopus 로고
    • Multiplicity of mammalian reductases for xenobiotic carbonyl compounds
    • Matsunaga T., Shintani S., and Hara A. Multiplicity of mammalian reductases for xenobiotic carbonyl compounds. Drug Metab. Pharmacokinet. 21 (2006) 1-18
    • (2006) Drug Metab. Pharmacokinet. , vol.21 , pp. 1-18
    • Matsunaga, T.1    Shintani, S.2    Hara, A.3
  • 14
    • 37349047898 scopus 로고    scopus 로고
    • An indomethacin analogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor of aldo-keto reductase 1C3 (type 2 3alpha-HSD, type 5 17beta-HSD, and prostaglandin F synthase), a potential target for the treatment of hormone dependent and hormone independent malignancies
    • Byrns M.C., Steckelbroeck S., and Penning T.M. An indomethacin analogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor of aldo-keto reductase 1C3 (type 2 3alpha-HSD, type 5 17beta-HSD, and prostaglandin F synthase), a potential target for the treatment of hormone dependent and hormone independent malignancies. Biochem. Pharmacol. 75 (2008) 484-493
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 484-493
    • Byrns, M.C.1    Steckelbroeck, S.2    Penning, T.M.3
  • 15
    • 33846945701 scopus 로고    scopus 로고
    • Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology
    • Oppermann U. Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology. Annu. Rev. Pharmacol. Toxicol. 47 (2007) 293-322
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 293-322
    • Oppermann, U.1
  • 16
    • 0034287545 scopus 로고    scopus 로고
    • Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
    • Penning T.M., Burczynski M.E., Jez J.M., Hung C.-F., Lin H.-K., Ma H., Moode M., Palackal N., and Patnam K. Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones. Biochem. J. 351 (2000) 67-77
    • (2000) Biochem. J. , vol.351 , pp. 67-77
    • Penning, T.M.1    Burczynski, M.E.2    Jez, J.M.3    Hung, C.-F.4    Lin, H.-K.5    Ma, H.6    Moode, M.7    Palackal, N.8    Patnam, K.9
  • 17
    • 1342346696 scopus 로고    scopus 로고
    • Aldo-keto reductases and formation of polycyclic aromatic hydrocarbon o-quinones
    • Penning T.M. Aldo-keto reductases and formation of polycyclic aromatic hydrocarbon o-quinones. Methods Enzymol. 378 (2004) 31-67
    • (2004) Methods Enzymol. , vol.378 , pp. 31-67
    • Penning, T.M.1
  • 18
    • 47549097394 scopus 로고    scopus 로고
    • Comparisons of (+/-)-benzo[a]pyrene-trans-7,8-dihydrodiol activation by human cytochrome P450 and aldo-keto reductase enzymes: effect of redox state and expression levels
    • Quinn A.M., and Penning T.M. Comparisons of (+/-)-benzo[a]pyrene-trans-7,8-dihydrodiol activation by human cytochrome P450 and aldo-keto reductase enzymes: effect of redox state and expression levels. Chem. Res. Toxicol. 21 (2008) 1086-1094
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 1086-1094
    • Quinn, A.M.1    Penning, T.M.2
  • 19
    • 34547093431 scopus 로고    scopus 로고
    • An approach to evaluate two-electron reduction of 9,10-phenanthraquinone and redox activity of the hydroquinone associated with oxidative stress
    • Taguchi K., Fujii S., Yamano S., Cho A.K., Kamisuki S., Nakai Y., Sugawara F., Froines J.R., and Kumagai Y. An approach to evaluate two-electron reduction of 9,10-phenanthraquinone and redox activity of the hydroquinone associated with oxidative stress. Free Radic. Biol. Med. 43 (2007) 789-799
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 789-799
    • Taguchi, K.1    Fujii, S.2    Yamano, S.3    Cho, A.K.4    Kamisuki, S.5    Nakai, Y.6    Sugawara, F.7    Froines, J.R.8    Kumagai, Y.9
  • 21
    • 0035283005 scopus 로고    scopus 로고
    • The cytotoxic effects of diesel exhaust particles on human pulmonary artery endothelial cells in vitro: role of active oxygen species
    • Bai Y., Suzuki A.K., and Sagai M. The cytotoxic effects of diesel exhaust particles on human pulmonary artery endothelial cells in vitro: role of active oxygen species. Free Radic. Biol. Med. 30 (2001) 555-562
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 555-562
    • Bai, Y.1    Suzuki, A.K.2    Sagai, M.3
  • 22
    • 0032400498 scopus 로고    scopus 로고
    • Roles of the C-terminal domains of human dihydrodiol dehydrogenase isoforms in the binding of substrates and modulators: probing with chimaeric enzymes
    • Matsuura K., Hara A., Deyashiki Y., Iwasa H., Kume T., Ishikura S., Shiraishi H., and Katagiri Y. Roles of the C-terminal domains of human dihydrodiol dehydrogenase isoforms in the binding of substrates and modulators: probing with chimaeric enzymes. Biochem. J. 336 (1998) 429-436
    • (1998) Biochem. J. , vol.336 , pp. 429-436
    • Matsuura, K.1    Hara, A.2    Deyashiki, Y.3    Iwasa, H.4    Kume, T.5    Ishikura, S.6    Shiraishi, H.7    Katagiri, Y.8
  • 23
    • 0032168199 scopus 로고    scopus 로고
    • Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA
    • Shiraishi H., Ishikura S., Matsuura K., Deyashiki Y., Ninomiya M., Sakai S., and Hara A. Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA. Biochem. J. 334 (1998) 399-405
    • (1998) Biochem. J. , vol.334 , pp. 399-405
    • Shiraishi, H.1    Ishikura, S.2    Matsuura, K.3    Deyashiki, Y.4    Ninomiya, M.5    Sakai, S.6    Hara, A.7
  • 24
    • 0031759084 scopus 로고    scopus 로고
    • Identification of a principal mRNA species for human 3alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity
    • Matsuura K., Shiraishi H., Hara A., Sato K., Deyashiki Y., Ninomiya M., and Sakai S. Identification of a principal mRNA species for human 3alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity. J. Biochem. (Tokyo) 124 (1998) 940-946
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 940-946
    • Matsuura, K.1    Shiraishi, H.2    Hara, A.3    Sato, K.4    Deyashiki, Y.5    Ninomiya, M.6    Sakai, S.7
  • 25
    • 0029095106 scopus 로고
    • Expression and kinetic properties of a recombinant 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzyme of human liver
    • Deyashiki Y., Tamada Y., Miyabe Y., Nakanishi M., Matsuura K., and Hara A. Expression and kinetic properties of a recombinant 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzyme of human liver. J. Biochem. (Tokyo) 118 (1995) 285-290
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 285-290
    • Deyashiki, Y.1    Tamada, Y.2    Miyabe, Y.3    Nakanishi, M.4    Matsuura, K.5    Hara, A.6
  • 26
    • 0042125492 scopus 로고    scopus 로고
    • Tetrahydrobiopterin is synthesized from 6-pyruvoyl-tetrahydropterin by the human aldo-keto reductase AKR1 family members
    • Iino T., Tabata M., Takikawa S., Sawada H., Shintaku H., Ishikura S., and Hara A. Tetrahydrobiopterin is synthesized from 6-pyruvoyl-tetrahydropterin by the human aldo-keto reductase AKR1 family members. Arch. Biochem. Biophys. 416 (2003) 180-187
    • (2003) Arch. Biochem. Biophys. , vol.416 , pp. 180-187
    • Iino, T.1    Tabata, M.2    Takikawa, S.3    Sawada, H.4    Shintaku, H.5    Ishikura, S.6    Hara, A.7
  • 27
    • 0023125219 scopus 로고
    • Steroid receptor-mediated cytotoxicity of an antiestrogen and an antiprogestin in breast cancer cells
    • Bardon S., Vignon F., Montcourrier P., and Rochefort H. Steroid receptor-mediated cytotoxicity of an antiestrogen and an antiprogestin in breast cancer cells. Cancer Res. 47 (1987) 1441-1448
    • (1987) Cancer Res. , vol.47 , pp. 1441-1448
    • Bardon, S.1    Vignon, F.2    Montcourrier, P.3    Rochefort, H.4
  • 28
    • 0034721770 scopus 로고    scopus 로고
    • Doxorubicin-induced apoptosis in endothelial cells and cardiomyocytes is ameliorated by nitrone spin traps and ebselen. Role of reactive oxygen and nitrogen species
    • Kotamraju S., Konorev E.A., Joseph J., and Kalyanaraman B. Doxorubicin-induced apoptosis in endothelial cells and cardiomyocytes is ameliorated by nitrone spin traps and ebselen. Role of reactive oxygen and nitrogen species. J. Biol. Chem. 275 (2000) 33585-33592
    • (2000) J. Biol. Chem. , vol.275 , pp. 33585-33592
    • Kotamraju, S.1    Konorev, E.A.2    Joseph, J.3    Kalyanaraman, B.4
  • 29
    • 3142543756 scopus 로고    scopus 로고
    • Ceramide-induced intracellular oxidant formation, iron signaling, and apoptosis in endothelial cells: protective role of endogenous nitric oxide
    • Matsunaga T., Kotamraju S., Kalivendi S.V., Dhanasekaran A., Joseph J., and Kalyanaraman B. Ceramide-induced intracellular oxidant formation, iron signaling, and apoptosis in endothelial cells: protective role of endogenous nitric oxide. J. Biol. Chem. 279 (2004) 28614-28624
    • (2004) J. Biol. Chem. , vol.279 , pp. 28614-28624
    • Matsunaga, T.1    Kotamraju, S.2    Kalivendi, S.V.3    Dhanasekaran, A.4    Joseph, J.5    Kalyanaraman, B.6
  • 30
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord J.M., and Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244 (1969) 6049-6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 31
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues
    • Tietze F. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27 (1969) 502-522
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 32
    • 0033282790 scopus 로고    scopus 로고
    • Expression of mRNAs for dihydrodiol dehydrogenase isoforms in human tissues
    • Shiraishi H., Matsuura K., Kume T., and Hara A. Expression of mRNAs for dihydrodiol dehydrogenase isoforms in human tissues. Adv. Exp. Med. Biol. 463 (1999) 539-544
    • (1999) Adv. Exp. Med. Biol. , vol.463 , pp. 539-544
    • Shiraishi, H.1    Matsuura, K.2    Kume, T.3    Hara, A.4
  • 35
    • 50149114676 scopus 로고    scopus 로고
    • Characterization of human DHRS4: an inducible short-chain dehydrogenase/reductase enzyme with 3beta-hydroxysteroid dehydrogenase activity
    • Matsunaga T., Endo S., Maeda S., Ishikura S., Tajima K., Tanaka N., Nakamura K.T., Imamura Y., and Hara A. Characterization of human DHRS4: an inducible short-chain dehydrogenase/reductase enzyme with 3beta-hydroxysteroid dehydrogenase activity. Arch. Biochem. Biophys. 477 (2008) 339-347
    • (2008) Arch. Biochem. Biophys. , vol.477 , pp. 339-347
    • Matsunaga, T.1    Endo, S.2    Maeda, S.3    Ishikura, S.4    Tajima, K.5    Tanaka, N.6    Nakamura, K.T.7    Imamura, Y.8    Hara, A.9
  • 36
    • 0037428060 scopus 로고    scopus 로고
    • Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells: role of transferrin receptor-dependent iron uptake in apoptosis
    • Tampo Y., Kotamraju S., Chitambar C.R., Kalivendi S.V., Keszler A., Joseph J., and Kalyanaraman B. Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells: role of transferrin receptor-dependent iron uptake in apoptosis. Circ. Res. 92 (2003) 56-63
    • (2003) Circ. Res. , vol.92 , pp. 56-63
    • Tampo, Y.1    Kotamraju, S.2    Chitambar, C.R.3    Kalivendi, S.V.4    Keszler, A.5    Joseph, J.6    Kalyanaraman, B.7
  • 37
    • 0035173178 scopus 로고    scopus 로고
    • Characterization of a major form of human isatin reductase and the reduced metabolite
    • Usami N., Kitahara K., Ishikura S., Nagano M., Sakai S., and Hara A. Characterization of a major form of human isatin reductase and the reduced metabolite. Eur. J. Biochem. 268 (2001) 5755-5763
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5755-5763
    • Usami, N.1    Kitahara, K.2    Ishikura, S.3    Nagano, M.4    Sakai, S.5    Hara, A.6
  • 38
    • 6344283093 scopus 로고    scopus 로고
    • Quinones and aromatic chemical compounds in particulate matter induce mitochondrial dysfunction: implications for ultrafine particle toxicity
    • Xia T., Korge P., Weiss J.N., Li N., Venkatesen M.I., Sioutas C., and Nel A. Quinones and aromatic chemical compounds in particulate matter induce mitochondrial dysfunction: implications for ultrafine particle toxicity. Environ. Health Perspect. 112 (2004) 1347-1358
    • (2004) Environ. Health Perspect. , vol.112 , pp. 1347-1358
    • Xia, T.1    Korge, P.2    Weiss, J.N.3    Li, N.4    Venkatesen, M.I.5    Sioutas, C.6    Nel, A.7
  • 39
    • 0032570577 scopus 로고    scopus 로고
    • Cytochrome c in the apoptotic and antioxidant cascades
    • Skulachev V.P. Cytochrome c in the apoptotic and antioxidant cascades. FEBS Lett. 423 (1998) 275-280
    • (1998) FEBS Lett. , vol.423 , pp. 275-280
    • Skulachev, V.P.1
  • 40
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., and Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91 (1997) 479-489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 41
    • 22544466964 scopus 로고    scopus 로고
    • Doxorubicin activates nuclear factor of activated T-lymphocytes and Fas ligand transcription: role of mitochondrial reactive oxygen species and calcium
    • Kalivendi S.V., Konorev E.A., Cunningham S., Vanamala S.K., Kaji E.H., Joseph J., and Kalyanaraman B. Doxorubicin activates nuclear factor of activated T-lymphocytes and Fas ligand transcription: role of mitochondrial reactive oxygen species and calcium. Biochem. J. 389 (2005) 527-539
    • (2005) Biochem. J. , vol.389 , pp. 527-539
    • Kalivendi, S.V.1    Konorev, E.A.2    Cunningham, S.3    Vanamala, S.K.4    Kaji, E.H.5    Joseph, J.6    Kalyanaraman, B.7
  • 42
    • 4444315545 scopus 로고    scopus 로고
    • Supplementation of endothelial cells with mitochondria-targeted antioxidants inhibit peroxide-induced mitochondrial iron uptake, oxidative damage, and apoptosis
    • Dhanasekaran A., Kotamraju S., Kalivendi S.V., Matsunaga T., Shang T., Keszler A., Joseph J., and Kalyanaraman B. Supplementation of endothelial cells with mitochondria-targeted antioxidants inhibit peroxide-induced mitochondrial iron uptake, oxidative damage, and apoptosis. J. Biol. Chem. 279 (2004) 37575-37587
    • (2004) J. Biol. Chem. , vol.279 , pp. 37575-37587
    • Dhanasekaran, A.1    Kotamraju, S.2    Kalivendi, S.V.3    Matsunaga, T.4    Shang, T.5    Keszler, A.6    Joseph, J.7    Kalyanaraman, B.8
  • 43
    • 33846887645 scopus 로고    scopus 로고
    • Disparity in the induction of glutathione depletion, ROS formation, poly(ADP-ribose) polymerase-1 activation, and apoptosis by quinonoid derivatives of naphthalene in human cultured cells
    • Lin C.H., Huang C.C., Wang T.W., Wang Y.J., and Lin P.H. Disparity in the induction of glutathione depletion, ROS formation, poly(ADP-ribose) polymerase-1 activation, and apoptosis by quinonoid derivatives of naphthalene in human cultured cells. Chem. Biol. Interact. 165 (2007) 200-210
    • (2007) Chem. Biol. Interact. , vol.165 , pp. 200-210
    • Lin, C.H.1    Huang, C.C.2    Wang, T.W.3    Wang, Y.J.4    Lin, P.H.5
  • 44
    • 44349169635 scopus 로고    scopus 로고
    • Evidence for the aldo-keto reductase pathway of polycyclic aromatic trans-dihydrodiol activation in human lung A549 cells
    • Park J.H., Mangal D., Tacka K.A., Quinn A.M., Harvey R.G., Blair I.A., and Penning T.M. Evidence for the aldo-keto reductase pathway of polycyclic aromatic trans-dihydrodiol activation in human lung A549 cells. Proc. Natl. Acad. Sci. U.S.A. 105 (2008) 6846-6851
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6846-6851
    • Park, J.H.1    Mangal, D.2    Tacka, K.A.3    Quinn, A.M.4    Harvey, R.G.5    Blair, I.A.6    Penning, T.M.7
  • 46
    • 0027207716 scopus 로고
    • Studies on three reductases which have polycyclic aromatic hydrocarbon quinines as substrates
    • Jarabak J., and Harvey R.G. Studies on three reductases which have polycyclic aromatic hydrocarbon quinines as substrates. Arch. Biochem. Biophys. 303 (1993) 394-401
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 394-401
    • Jarabak, J.1    Harvey, R.G.2
  • 47
    • 0026497715 scopus 로고
    • Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells
    • Fernando M.R., Nanri H., Yoshitake S., Nagata-Kuno K., and Minakami S. Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells. Eur. J. Biochem. 209 (1992) 917-922
    • (1992) Eur. J. Biochem. , vol.209 , pp. 917-922
    • Fernando, M.R.1    Nanri, H.2    Yoshitake, S.3    Nagata-Kuno, K.4    Minakami, S.5
  • 48
    • 1642535437 scopus 로고    scopus 로고
    • Interactions of quinones with thioredoxin reductase: a challenge to the antioxidant role of the mammalian selenoprotein
    • Cenas N., Nivinskas H., Anusevicius Z., Sarlauskas J., Lederer F., and Arnér E.S. Interactions of quinones with thioredoxin reductase: a challenge to the antioxidant role of the mammalian selenoprotein. J. Biol. Chem. 279 (2004) 2583-2592
    • (2004) J. Biol. Chem. , vol.279 , pp. 2583-2592
    • Cenas, N.1    Nivinskas, H.2    Anusevicius, Z.3    Sarlauskas, J.4    Lederer, F.5    Arnér, E.S.6
  • 49
    • 11144221439 scopus 로고    scopus 로고
    • Widespread sulfenic acid formation in tissues in response to hydrogen peroxide
    • Saurin A.T., Neubert H., Brennan J.P., and Eaton P. Widespread sulfenic acid formation in tissues in response to hydrogen peroxide. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 17982-17987
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 17982-17987
    • Saurin, A.T.1    Neubert, H.2    Brennan, J.P.3    Eaton, P.4
  • 51
    • 44649119229 scopus 로고    scopus 로고
    • 4-Hydroxynonenal contributes to macrophage foam cell formation through increased expression of class A scavenger receptor at the level of translation
    • Yun M.R., Im D.S., Lee S.J., Woo J.W., Hong K.W., Bae S.S., and Kim C.D. 4-Hydroxynonenal contributes to macrophage foam cell formation through increased expression of class A scavenger receptor at the level of translation. Free Radic. Biol. Med. 45 (2008) 177-183
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 177-183
    • Yun, M.R.1    Im, D.S.2    Lee, S.J.3    Woo, J.W.4    Hong, K.W.5    Bae, S.S.6    Kim, C.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.