메뉴 건너뛰기




Volumn 32, Issue 1-4, 2008, Pages 59-70

NADPH-dependent coenzyme Q reductase is the main enzyme responsible for the reduction of non-mitochondrial CoQ in cells

Author keywords

Antioxidant; Coenzyme Q; NADPH CoQ reductase; Rat liver; Ubiquinol; Zinc

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE; GLUTATHIONE REDUCTASE; OXIDOREDUCTASE; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SMALL INTERFERING RNA; THIOREDOXIN REDUCTASE; ZINC;

EID: 58149385537     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520320108     Document Type: Conference Paper
Times cited : (16)

References (40)
  • 1
    • 0026636509 scopus 로고
    • Distribution and redox state of ubiquinones in rat and human tissues
    • F. Åberg, E.-L. Appelkvist, G. Dallner and L. Ernster, Distribution and redox state of ubiquinones in rat and human tissues, Arch Biochem Biophys 295 (1992), 230-234.
    • (1992) Arch Biochem Biophys , vol.295 , pp. 230-234
    • Åberg, F.1    Appelkvist, E.-L.2    Dallner, G.3    Ernster, L.4
  • 2
    • 0035839019 scopus 로고    scopus 로고
    • Coenzyme Q blocks biochemical but not receptor-mediated apoptosis by increasing mitochondrial antioxidant protection
    • R. Alleva, M. Tomasetti, L. Andera, N. Gellert, B. Borghi, C. Weber, M.P. Murphy and J. Neuzil, Coenzyme Q blocks biochemical but not receptor-mediated apoptosis by increasing mitochondrial antioxidant protection, FEBS Lett 503 (2001), 46-50.
    • (2001) FEBS Lett , vol.503 , pp. 46-50
    • Alleva, R.1    Tomasetti, M.2    Andera, L.3    Gellert, N.4    Borghi, B.5    Weber, C.6    Murphy, M.P.7    Neuzil, J.8
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal Biochem 72 (1976), 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 77957000392 scopus 로고
    • DT-diaphorase
    • R.W. Estabrook and M.E. Pullman, eds, Academic Press, New York
    • L. Ernster, DT-diaphorase, in: Methods in Enzymology 10, R.W. Estabrook and M.E. Pullman, eds, Academic Press, New York, 1967, pp. 309-317.
    • (1967) Methods in Enzymology , vol.10 , pp. 309-317
    • Ernster, L.1
  • 6
    • 0025809391 scopus 로고
    • Inhibition of lipid peroxidation by ubiquinol in submitochondrial particles in the absence of vitamin E
    • P. Forsmark, F. Åberg, B. Norling, K. Nordenbrand, G. Dallner and L. Ernster, Inhibition of lipid peroxidation by ubiquinol in submitochondrial particles in the absence of vitamin E, FEBS Lett 285 (1991), 39-43.
    • (1991) FEBS Lett , vol.285 , pp. 39-43
    • Forsmark, P.1    Åberg, F.2    Norling, B.3    Nordenbrand, K.4    Dallner, G.5    Ernster, L.6
  • 7
    • 0025327523 scopus 로고
    • Ubiquinol-10 is an effective lipid-soluble antioxidant at physiological concentrations
    • B. Frei, M.C. Kim and B.N. Ames, Ubiquinol-10 is an effective lipid-soluble antioxidant at physiological concentrations, Proc Natl Acad Sci USA 87 (1990), 4879-4883.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4879-4883
    • Frei, B.1    Kim, M.C.2    Ames, B.N.3
  • 10
    • 0016697619 scopus 로고
    • Studies on the reaction mechanism of DT diaphorase. Action of dead-end inhibitors and effects of phospholipids
    • P.M. Hollander and L. Ernster, Studies on the reaction mechanism of DT diaphorase. Action of dead-end inhibitors and effects of phospholipids, Arch Biochem Biophys 169 (1975), 560-567.
    • (1975) Arch Biochem Biophys , vol.169 , pp. 560-567
    • Hollander, P.M.1    Ernster, L.2
  • 11
    • 0025005727 scopus 로고
    • Recycling and antioxidant activity of tocopherol homologs of differing hydrocarbon chain lengths in liver microsomes
    • V.E. Kagan, E.A. Serbinova and L. Packer, Recycling and antioxidant activity of tocopherol homologs of differing hydrocarbon chain lengths in liver microsomes, Arch Biochem Biophys 282 (1990), 221-225.
    • (1990) Arch Biochem Biophys , vol.282 , pp. 221-225
    • Kagan, V.E.1    Serbinova, E.A.2    Packer, L.3
  • 13
    • 46649094055 scopus 로고
    • Ubiquinone binding proteins in liver soluble fraction
    • K. Folkers, G.P. Littarru and T. Yamagami, eds, Elsevier Science Publishers, Amsterdam
    • T. Kishi, K. Fukui, Y. Fukunaga, T. Takahashi, T. Okamoto and T. Yamagami, Ubiquinone binding proteins in liver soluble fraction, in: Biomedical and Clinical Aspects of Coenzyme Q, K. Folkers, G.P. Littarru and T. Yamagami, eds, Elsevier Science Publishers, Amsterdam, 1991, pp. 107-114.
    • (1991) Biomedical and Clinical Aspects of Coenzyme Q , pp. 107-114
    • Kishi, T.1    Fukui, K.2    Fukunaga, Y.3    Takahashi, T.4    Okamoto, T.5    Yamagami, T.6
  • 14
    • 0036554585 scopus 로고    scopus 로고
    • Effect of dicumarol, a NAD(P)H: Quinone acceptor oxidoreductase 1 (DT-diaphorase) inhibitor on ubiquinone redox cycling in cultured rat hepatocytes
    • T. Kishi, T. Takahashi, S. Mizobuchi, K. Mori and T. Okamoto, Effect of dicumarol, a NAD(P)H: quinone acceptor oxidoreductase 1 (DT-diaphorase) inhibitor on ubiquinone redox cycling in cultured rat hepatocytes, Free Radic Res 36 (2002), 413-419.
    • (2002) Free Radic Res , vol.36 , pp. 413-419
    • Kishi, T.1    Takahashi, T.2    Mizobuchi, S.3    Mori, K.4    Okamoto, T.5
  • 15
    • 0014636042 scopus 로고
    • Equilibrium relations between pyridine nucleotides and adenine nucleotides and their roles in the regulation of metabolic processes
    • G. Weber, ed, Pergamon Press, Oxford
    • H.A. Krebs and R.L. Veech, Equilibrium relations between pyridine nucleotides and adenine nucleotides and their roles in the regulation of metabolic processes, in: Advances in Enzyme Regulation 7, G. Weber, ed., Pergamon Press, Oxford, 1968, pp. 397-413.
    • (1968) Advances in Enzyme Regulation , vol.7 , pp. 397-413
    • Krebs, H.A.1    Veech, R.L.2
  • 16
    • 0029859863 scopus 로고    scopus 로고
    • DT-Diaphorase maintains the reduced state of ubiquinones in lipid vesicles thereby promoting their antioxidant function
    • L. Landi, D. Fiorentini, M.C. Galli, J. Segura-Aguilar and R.E. Beyer, DT-Diaphorase maintains the reduced state of ubiquinones in lipid vesicles thereby promoting their antioxidant function, Free Radic Biol Med 22 (1997), 329-335.
    • (1997) Free Radic Biol Med , vol.22 , pp. 329-335
    • Landi, L.1    Fiorentini, D.2    Galli, M.C.3    Segura-Aguilar, J.4    Beyer, R.E.5
  • 18
    • 0028925916 scopus 로고
    • Capsaicin inhibits preferentially the NADH oxidase and growth of transformed cells in culture
    • D.J. Morré, P.J. Chueh and D.M. Morré, Capsaicin inhibits preferentially the NADH oxidase and growth of transformed cells in culture, Proc Natl Acad Sci USA 92 (1995), 1831-1835.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1831-1835
    • Morré, D.J.1    Chueh, P.J.2    Morré, D.M.3
  • 19
    • 0025358550 scopus 로고
    • Stopped-flow kinetic study of the regeneration reaction of tocopheroxyl radical by reduced ubiquinone-10 in solution
    • K. Mukai, S. Kikuchi and S. Urano, Stopped-flow kinetic study of the regeneration reaction of tocopheroxyl radical by reduced ubiquinone-10 in solution, Biochim Biophys Acta 1035 (1990), 77-82.
    • (1990) Biochim Biophys Acta , vol.1035 , pp. 77-82
    • Mukai, K.1    Kikuchi, S.2    Urano, S.3
  • 21
    • 34147146403 scopus 로고    scopus 로고
    • Enrichment of coenzyme Q10 in plasma and blood cells: Defense against oxidative damage
    • P. Niklowitz, A. Sonnenschein, B. Janetzky, W. Andler and T. Menke, Enrichment of coenzyme Q10 in plasma and blood cells: defense against oxidative damage, Int J Biol Sci 3 (2007), 257-262.
    • (2007) Int J Biol Sci , vol.3 , pp. 257-262
    • Niklowitz, P.1    Sonnenschein, A.2    Janetzky, B.3    Andler, W.4    Menke, T.5
  • 23
    • 0023715570 scopus 로고
    • Determination of reduced and total ubiquinones in biological materials by liquid chromatography with electrochemical detection
    • T. Okamoto, Y. Fukunaga, Y. Ida and T. Kishi, Determination of reduced and total ubiquinones in biological materials by liquid chromatography with electrochemical detection, J Chromatogr 430 (1988), 11-19.
    • (1988) J Chromatogr , vol.430 , pp. 11-19
    • Okamoto, T.1    Fukunaga, Y.2    Ida, Y.3    Kishi, T.4
  • 26
    • 0024207283 scopus 로고
    • Purification and crystallization of rat liver NAD(P)H:(quinone-acceptor) oxidoreductase by cibacron blue affinity chromatography: Identification of a new and potent inhibitor
    • H.J. Prochaska, Purification and crystallization of rat liver NAD(P)H:(quinone-acceptor) oxidoreductase by cibacron blue affinity chromatography: identification of a new and potent inhibitor, Arch Biochem Biophys 267 (1988), 529-538.
    • (1988) Arch Biochem Biophys , vol.267 , pp. 529-538
    • Prochaska, H.J.1
  • 28
    • 0038389439 scopus 로고    scopus 로고
    • 3-nitropropionic acid inhibition of succinate dehydrogenase (complex II) activity in cultured Chinese hamster ovary cells: Antagonism by L-carnitine
    • discussion 345-349
    • A.C. Scallet, R.L. Haley, D.M. Scallet, H.M. Duhart and Z.K. Binienda, 3-nitropropionic acid inhibition of succinate dehydrogenase (complex II) activity in cultured Chinese hamster ovary cells: antagonism by L-carnitine, Ann NY Acad Sci 993 (2003), 305-312; discussion 345-349.
    • (2003) Ann NY Acad Sci , vol.993 , pp. 305-312
    • Scallet, A.C.1    Haley, R.L.2    Scallet, D.M.3    Duhart, H.M.4    Binienda, Z.K.5
  • 29
    • 0025979077 scopus 로고
    • Ubiquinol-10 protects human low density lipoprotein more efficiently against lipid peroxidation than does alpha-tocopherol
    • R. Stocker, V.W. Bowry and B. Frei, Ubiquinol-10 protects human low density lipoprotein more efficiently against lipid peroxidation than does alpha-tocopherol, Proc Natl Acad Sci USA 88 (1991), 1646-1650.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1646-1650
    • Stocker, R.1    Bowry, V.W.2    Frei, B.3
  • 30
    • 0027447549 scopus 로고
    • Comparative antioxidant activity of tocotrienols and other natural lipid-soluble antioxidants in a homogeneous system, and in rat and human lipoproteins
    • C. Suarna, R.L. Hood, R.T. Dean and R. Stocker, Comparative antioxidant activity of tocotrienols and other natural lipid-soluble antioxidants in a homogeneous system, and in rat and human lipoproteins, Biochim Biophys Acta 1166 (1993), 163-170.
    • (1993) Biochim Biophys Acta , vol.1166 , pp. 163-170
    • Suarna, C.1    Hood, R.L.2    Dean, R.T.3    Stocker, R.4
  • 33
    • 0029774736 scopus 로고    scopus 로고
    • protective effect against carbon tetrachloride-induced hepatotoxicity in the rat
    • Cellular antioxidant defense by a ubiquinol-regenerating system coupled with cytosolic NADPH-dependent ubiquinone reductase
    • T. Takahashi, N. Sugimoto, K. Takahata, T. Okamoto and T. Kishi, Cellular antioxidant defense by a ubiquinol-regenerating system coupled with cytosolic NADPH-dependent ubiquinone reductase: protective effect against carbon tetrachloride-induced hepatotoxicity in the rat, Biol Pharm Bull 19 (1996), 1005-1012.
    • (1996) Biol Pharm Bull , vol.19 , pp. 1005-1012
    • Takahashi, T.1    Sugimoto, N.2    Takahata, K.3    Okamoto, T.4    Kishi, T.5
  • 34
    • 0030027791 scopus 로고    scopus 로고
    • effect of various factors on ubiquinone-reducing activity and discrimination from other quinone reductases
    • Characterization of NADPH-dependent ubiquinone reductase activity in rat liver cytosol
    • T. Takahashi, T. Okamoto and T. Kishi, Characterization of NADPH-dependent ubiquinone reductase activity in rat liver cytosol: effect of various factors on ubiquinone-reducing activity and discrimination from other quinone reductases, J Biochem 119 (1996), 256-263.
    • (1996) J Biochem , vol.119 , pp. 256-263
    • Takahashi, T.1    Okamoto, T.2    Kishi, T.3
  • 35
    • 0027203251 scopus 로고
    • Distribution of ubiquinone and ubiquinol homologues in rat tissues and subcellular fractions
    • T. Takahashi, T. Okamoto, K. Mori, H. Sayo and T. Kishi, Distribution of ubiquinone and ubiquinol homologues in rat tissues and subcellular fractions, Lipids 28 (1993), 803-809.
    • (1993) Lipids , vol.28 , pp. 803-809
    • Takahashi, T.1    Okamoto, T.2    Mori, K.3    Sayo, H.4    Kishi, T.5
  • 36
    • 0029111988 scopus 로고
    • Reduction of ubiquinone in membrane lipids by rat liver cytosol and its involvement in the cellular defence system against lipid peroxidation
    • T. Takahashi, T. Yamaguchi, M. Shitashige, T. Okamoto and T. Kishi, Reduction of ubiquinone in membrane lipids by rat liver cytosol and its involvement in the cellular defence system against lipid peroxidation, Biochem J 309 (1995), 883-890.
    • (1995) Biochem J , vol.309 , pp. 883-890
    • Takahashi, T.1    Yamaguchi, T.2    Shitashige, M.3    Okamoto, T.4    Kishi, T.5
  • 37
    • 0035087829 scopus 로고    scopus 로고
    • Reduction of ubiquinone by lipoamide dehydrogenase. An antioxidant regenerating pathway
    • L. Xia, M. Björnstedt, T. Nordman, L.C. Eriksson and J.M. Olsson, Reduction of ubiquinone by lipoamide dehydrogenase. An antioxidant regenerating pathway, Eur J Biochem 268 (2001), 1486-1490.
    • (2001) Eur J Biochem , vol.268 , pp. 1486-1490
    • Xia, L.1    Björnstedt, M.2    Nordman, T.3    Eriksson, L.C.4    Olsson, J.M.5
  • 39
    • 0025611704 scopus 로고
    • Antioxidant activity of ubiquinol in solution and phosphatidylcholine liposome
    • Y. Yamamoto, E. Komuro and E. Niki, Antioxidant activity of ubiquinol in solution and phosphatidylcholine liposome, J Nutr Sci Vitaminol (Tokyo) 36 (1990), 505-511.
    • (1990) J Nutr Sci Vitaminol (Tokyo) , vol.36 , pp. 505-511
    • Yamamoto, Y.1    Komuro, E.2    Niki, E.3
  • 40
    • 33748907052 scopus 로고    scopus 로고
    • Evaluation of the dietary effects of coenzyme Q in vivo by the oxidative stress marker, hydroxyoctadecadienoic acid and its stereoisomer ratio
    • Y. Yoshida, M. Hayakawa, Y. Habuchi and E Niki, Evaluation of the dietary effects of coenzyme Q in vivo by the oxidative stress marker, hydroxyoctadecadienoic acid and its stereoisomer ratio, Biochim Biophys Acta 1760 (2006), 1558-1568.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 1558-1568
    • Yoshida, Y.1    Hayakawa, M.2    Habuchi, Y.3    Niki, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.