메뉴 건너뛰기




Volumn 110, Issue 1-3, 1996, Pages 85-93

Ortho-phenanthroline modulates enzymes of cellular energy metabolism

Author keywords

ATPase; Glycolysis; Ortho phenanthroline; Reactive oxygen species; Respiratory chain

Indexed keywords

1,10 PHENANTHROLINE; ADENOSINE TRIPHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; LACTATE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE;

EID: 0030011696     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0300-483X(96)03331-8     Document Type: Article
Times cited : (13)

References (32)
  • 1
    • 0025016281 scopus 로고
    • Reactive oxygen molecule-mediated injury in endothelial and renal tubular epithelial cells in vitro
    • Andreoli, S.P., McAteer, J.A. and Mallett, C. (1990) Reactive oxygen molecule-mediated injury in endothelial and renal tubular epithelial cells in vitro. Kidney Int. 38, 785-794.
    • (1990) Kidney Int. , vol.38 , pp. 785-794
    • Andreoli, S.P.1    McAteer, J.A.2    Mallett, C.3
  • 2
    • 0028540244 scopus 로고
    • Lethal interaction between hydrogen peroxide and o-phenanthroline in Escherichia coli
    • Asad, N.R., Asad, L.M.B.O., Almeida, C.E.B. and Leitao, A.C. (1994) Lethal interaction between hydrogen peroxide and o-phenanthroline in Escherichia coli. Brazilian J. Med. Biol. Res. 27, 2551 -2555.
    • (1994) Brazilian J. Med. Biol. Res. , vol.27 , pp. 2551-2555
    • Asad, N.R.1    Asad, L.M.B.O.2    Almeida, C.E.B.3    Leitao, A.C.4
  • 3
    • 0026582192 scopus 로고
    • Effect of lipophilic chelators on oxy-radical-induced DNA strand breaks in human granulocytes: Paradoxical effect of 1,10-phenanthroline
    • Birnboim, H.C. (1992) Effect of lipophilic chelators on oxy-radical-induced DNA strand breaks in human granulocytes: paradoxical effect of 1,10-phenanthroline. Arch. Biochem. Biophys. 294, 17-21.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 17-21
    • Birnboim, H.C.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0019802669 scopus 로고
    • Uncoupler-reversible inhibition of mitochondrial ATPase by metal chelates of bathophenanthroline
    • Carlsson, C. and Ernster, L. (1981) Uncoupler-reversible inhibition of mitochondrial ATPase by metal chelates of bathophenanthroline. Biochim. Biophys. Acta 638, 345-357.
    • (1981) Biochim. Biophys. Acta , vol.638 , pp. 345-357
    • Carlsson, C.1    Ernster, L.2
  • 6
    • 0021360269 scopus 로고
    • In vivo formation of single-strand breaks in DNA by hydrogen peroxide is mediated by the Haber-Weiss-reaction
    • De Mello Filho, A.C. and Meneghini, R. (1984) In vivo formation of single-strand breaks in DNA by hydrogen peroxide is mediated by the Haber-Weiss-reaction. Biochim. Biophys. Acta 781, 56-63.
    • (1984) Biochim. Biophys. Acta , vol.781 , pp. 56-63
    • De Mello Filho, A.C.1    Meneghini, R.2
  • 7
    • 0022244540 scopus 로고
    • Protection of mammalian cells by o-phenanthroline from lethal and DNA-damaging effects produced by reactive oxygen species
    • De Mello Filho, A.C. and Meneghini, R. (1985) Protection of mammalian cells by o-phenanthroline from lethal and DNA-damaging effects produced by reactive oxygen species. Biochim. Biophys. Acta 847, 82-89.
    • (1985) Biochim. Biophys. Acta , vol.847 , pp. 82-89
    • De Mello Filho, A.C.1    Meneghini, R.2
  • 8
    • 0025170605 scopus 로고
    • Modification of bases in DNA by copper ion-1,10-phenanthroline complexes
    • Dizdaroglu, M., Aruoma, O.I. and Halliwell, B. (1990) Modification of bases in DNA by copper ion-1,10-phenanthroline complexes. Biochemistry 29, 8447-8451.
    • (1990) Biochemistry , vol.29 , pp. 8447-8451
    • Dizdaroglu, M.1    Aruoma, O.I.2    Halliwell, B.3
  • 9
    • 0028222395 scopus 로고
    • Identification, purification and partial charcterization of a carboxypeptidase from the matrix of rat liver mitochondria: A novel metalloenzyme
    • Figueiredo, E. and Duque-Magalhaes, M.C. (1994) Identification, purification and partial charcterization of a carboxypeptidase from the matrix of rat liver mitochondria: a novel metalloenzyme. Biochem. J. 15, 15-19.
    • (1994) Biochem. J. , vol.15 , pp. 15-19
    • Figueiredo, E.1    Duque-Magalhaes, M.C.2
  • 10
    • 0000824291 scopus 로고
    • Influence of ethanol on the liver metabolism of fed and starved rats
    • Forsander, O.A., Raiha, N., Salaspuro, M. and Maenpaa, P. (1965) Influence of ethanol on the liver metabolism of fed and starved rats. Biochem. J. 94, 259-265.
    • (1965) Biochem. J. , vol.94 , pp. 259-265
    • Forsander, O.A.1    Raiha, N.2    Salaspuro, M.3    Maenpaa, P.4
  • 12
    • 0344202524 scopus 로고
    • Preparation and assay of phosphorylating submitochondrial particles: Particles from rat liver prepared by drastic sonication
    • R.W. Estabrook and M.E. Pullman (Eds), Academic Press, New York
    • Gregg, C.T. (1967) Preparation and assay of phosphorylating submitochondrial particles: particles from rat liver prepared by drastic sonication. In: R.W. Estabrook and M.E. Pullman (Eds), Methods in Enzymology: Oxidation and Phosphorylation, Academic Press, New York, pp. 181-185.
    • (1967) Methods in Enzymology: Oxidation and Phosphorylation , pp. 181-185
    • Gregg, C.T.1
  • 13
    • 0022394280 scopus 로고
    • The importance of free radicals and catalytic metal ions in human diseases
    • Halliwell, B. and Gutteridge, M.C. (1985) The importance of free radicals and catalytic metal ions in human diseases. Mol. Asp. Med. 8, 89-193.
    • (1985) Mol. Asp. Med. , vol.8 , pp. 89-193
    • Halliwell, B.1    Gutteridge, M.C.2
  • 14
    • 0017188188 scopus 로고
    • Inhibition of mitochondrial electron transport by hydrophilic metal chelators
    • Harmon, H.J. and Crane, F.L. (1976) Inhibition of mitochondrial electron transport by hydrophilic metal chelators. Biochim. Biophys. Acta 440, 45-58.
    • (1976) Biochim. Biophys. Acta , vol.440 , pp. 45-58
    • Harmon, H.J.1    Crane, F.L.2
  • 15
    • 0027479009 scopus 로고
    • Role of iron and superoxide in mediating hydrogen peroxide injury to cultured rat gastric cells
    • Hiraishi, H., Terano, A., Razandi, M., Sugimoto, T., Harada, T. and Ivey, K.J. (1993) Role of iron and superoxide in mediating hydrogen peroxide injury to cultured rat gastric cells. Gastroenterology 104, 780-788.
    • (1993) Gastroenterology , vol.104 , pp. 780-788
    • Hiraishi, H.1    Terano, A.2    Razandi, M.3    Sugimoto, T.4    Harada, T.5    Ivey, K.J.6
  • 16
    • 0028225357 scopus 로고
    • Reactive oxygen metabolite-induced toxicity to cultured bovine endothelial cells: Status of cellular iron in mediating injury
    • Hiraishi, H., Terano, A., Razandi, M., Pedram, A., Sugimoto, T., Harada, T. and Ivey, K.I. (1994) Reactive oxygen metabolite-induced toxicity to cultured bovine endothelial cells: status of cellular iron in mediating injury. J. Cell. Physiol. 160, 132-140.
    • (1994) J. Cell. Physiol. , vol.160 , pp. 132-140
    • Hiraishi, H.1    Terano, A.2    Razandi, M.3    Pedram, A.4    Sugimoto, T.5    Harada, T.6    Ivey, K.I.7
  • 17
    • 0024970703 scopus 로고
    • Characteristics of purified protoporphyrinogen oxidase from barley
    • Jacobs, N.J., Borotz, S.E. and Jacobs, J.M. (1989) Characteristics of purified protoporphyrinogen oxidase from barley. Biochem. Biophys. Res. Commun. 161, 790-796.
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 790-796
    • Jacobs, N.J.1    Borotz, S.E.2    Jacobs, J.M.3
  • 18
    • 0003083966 scopus 로고
    • Isolation of liver or kidney mitochondria
    • R.W. Estabrook and M.E. Pullman (Eds), Academic Press, New York
    • Johnson, D. and Lardy, H. (1967) Isolation of liver or kidney mitochondria. In: R.W. Estabrook and M.E. Pullman (Eds), Methods in Enzymology: Oxidation and Phosphorylation, Academic Press, New York, pp. 110-112.
    • (1967) Methods in Enzymology: Oxidation and Phosphorylation , pp. 110-112
    • Johnson, D.1    Lardy, H.2
  • 19
    • 0009507697 scopus 로고
    • On the prosthetic group of succinic dehydrogenase
    • Kearney, E.B. and Singer, T.P. (1955) On the prosthetic group of succinic dehydrogenase. Biochim. Biophys. Acta 17, 596-597.
    • (1955) Biochim. Biophys. Acta , vol.17 , pp. 596-597
    • Kearney, E.B.1    Singer, T.P.2
  • 20
    • 0025147397 scopus 로고
    • The general mitochondrial matrix processing protease from rat liver: Structural characterization of the catalytic subunit
    • Kleiber, J., Kalousek, F., Swaroop, M. and Rosenberg, L.E (1990) The general mitochondrial matrix processing protease from rat liver: structural characterization of the catalytic subunit. Proc. Natl. Acad. Sci. U.S.A. 87, 7978-7982.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 7978-7982
    • Kleiber, J.1    Kalousek, F.2    Swaroop, M.3    Rosenberg, L.E.4
  • 21
    • 0017105620 scopus 로고
    • Expiratory measurement of maximal aminopyrine demethylation in vivo: Effect of phenobarbital, partial hepatectomy, portacaval shunt and bile duct ligation in the rat
    • Lauterburg, B.H. and Bircher, J. (1976) Expiratory measurement of maximal aminopyrine demethylation in vivo: effect of phenobarbital, partial hepatectomy, portacaval shunt and bile duct ligation in the rat. J. Pharmacol. Exp. Therapeutics 196, 501-509.
    • (1976) J. Pharmacol. Exp. Therapeutics , vol.196 , pp. 501-509
    • Lauterburg, B.H.1    Bircher, J.2
  • 22
    • 0008380952 scopus 로고
    • The role of iron in beef-heart succinic dehydrogenase
    • Massey, V. (1958) The role of iron in beef-heart succinic dehydrogenase. Biochim. Biophys. Acta 30, 500-509.
    • (1958) Biochim. Biophys. Acta , vol.30 , pp. 500-509
    • Massey, V.1
  • 23
    • 0019883347 scopus 로고
    • Topology and some properties of the renal brush border membrane-bound peptidase(s) participating in the metabolism of s-carbamidomethyl glutathione
    • Okajima, K., Inoue, M. and Morino, Y. (1981) Topology and some properties of the renal brush border membrane-bound peptidase(s) participating in the metabolism of s-carbamidomethyl glutathione. Biochim. Biophys. Acta 675, 379-385.
    • (1981) Biochim. Biophys. Acta , vol.675 , pp. 379-385
    • Okajima, K.1    Inoue, M.2    Morino, Y.3
  • 25
    • 0015207654 scopus 로고
    • Quinne interaction with the respiratory chain-linked NADH dehydrogenase of beef heart mitochondria II. Duroquinone reductase activity
    • Ruzicka, F.J. and Crane, F.L. (1971) Quinne interaction with the respiratory chain-linked NADH dehydrogenase of beef heart mitochondria II. Duroquinone reductase activity. Biochim. Biophys. Acta 226, 221-233.
    • (1971) Biochim. Biophys. Acta , vol.226 , pp. 221-233
    • Ruzicka, F.J.1    Crane, F.L.2
  • 26
    • 0028796632 scopus 로고
    • Mechanism for a new antitumor vanadium complex: Hydroxyl radical-dependent DNA cleavage by 1,10-phenanthroline-vanadyl complex in the presence of hydrogen peroxide
    • Sakurai, H., Tamura, H. and Okatani, K. (1995) Mechanism for a new antitumor vanadium complex: hydroxyl radical-dependent DNA cleavage by 1,10-phenanthroline-vanadyl complex in the presence of hydrogen peroxide. Biochem. Biophys. Res. Commun. 206, 133-137.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 133-137
    • Sakurai, H.1    Tamura, H.2    Okatani, K.3
  • 27
    • 0025981555 scopus 로고
    • Oxidation of tris to one-carbon compounds in a radical-producing model system, in microsomes, in hepatocytes and in rats
    • Schäcker, M., Foth, H., Schlüter, J. and Kahl, R. (1991) Oxidation of tris to one-carbon compounds in a radical-producing model system, in microsomes, in hepatocytes and in rats. Free Rad. Res. Comms. 11, 339-347.
    • (1991) Free Rad. Res. Comms. , vol.11 , pp. 339-347
    • Schäcker, M.1    Foth, H.2    Schlüter, J.3    Kahl, R.4
  • 28
    • 0017101039 scopus 로고
    • Preparation of isolated rat liver cells
    • Seglen, O. (1976) Preparation of isolated rat liver cells. Methods Cell Biol. 13, 29-83.
    • (1976) Methods Cell Biol. , vol.13 , pp. 29-83
    • Seglen, O.1
  • 29
    • 0018638739 scopus 로고
    • Oxygen-dependent cleavage of DNA by the 1,10-phenanthroline cuprous complex
    • Sigman, D.S., Graham, D.R., D'Aurora, V. and Stern, A.M. (1979) Oxygen-dependent cleavage of DNA by the 1,10-phenanthroline cuprous complex. J. Biol. Chem. 254, 12269-12272.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12269-12272
    • Sigman, D.S.1    Graham, D.R.2    D'Aurora, V.3    Stern, A.M.4
  • 30
    • 0001270185 scopus 로고
    • Zinc in horse liver alcohol dehydrogenase
    • Vallee, B.L. and Hoch, F.L. (1957) Zinc in horse liver alcohol dehydrogenase. J. Biol. Chem. 225, 185-195.
    • (1957) J. Biol. Chem. , vol.225 , pp. 185-195
    • Vallee, B.L.1    Hoch, F.L.2
  • 31
    • 0028007280 scopus 로고
    • Characterization of oxidative injury to an intestinal cell line (HT-29) by hydrogen peroxide
    • Watson, A.J.M., Askew, J.N. and Sandle, G.I. (1994) Characterization of oxidative injury to an intestinal cell line (HT-29) by hydrogen peroxide. GUT 35, 1575-1581.
    • (1994) GUT , vol.35 , pp. 1575-1581
    • Watson, A.J.M.1    Askew, J.N.2    Sandle, G.I.3
  • 32
    • 0026763905 scopus 로고
    • Genetic polymorphism and activities of human lung alcohol and aldehyde dehydrogenase: Implications for ethanol metabolism and cytotoxicity
    • Yin, S.J., Liao, C.S., Chen, C.M., Fan, F.T. and Lee, S.C. (1992) Genetic polymorphism and activities of human lung alcohol and aldehyde dehydrogenase: implications for ethanol metabolism and cytotoxicity. Biochem. Genet. 30, 203-215.
    • (1992) Biochem. Genet. , vol.30 , pp. 203-215
    • Yin, S.J.1    Liao, C.S.2    Chen, C.M.3    Fan, F.T.4    Lee, S.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.