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Volumn 23, Issue 6, 2007, Pages 413-420

Vanadate-induced cell death is dissociated from H2O2 generation

Author keywords

Erythroleukemic cells; Hydrogen peroxide; Renal cells; Vanadate

Indexed keywords

HYDROGEN PEROXIDE; PEROXOVANADIUM; UNCLASSIFIED DRUG; VANADIC ACID; VANADIUM DERIVATIVE;

EID: 37749035195     PISSN: 07422091     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10565-007-9003-4     Document Type: Article
Times cited : (39)

References (53)
  • 1
    • 17044378602 scopus 로고    scopus 로고
    • Decavanadate effects in biological systems
    • Aureliano M, Gandara RM. Decavanadate effects in biological systems. J Inorg Biochem 2005;99:979-85.
    • (2005) J Inorg Biochem , vol.99 , pp. 979-985
    • Aureliano, M.1    Gandara, R.M.2
  • 2
    • 0037036051 scopus 로고    scopus 로고
    • Oxidative stress in toadfish (Halobactrachus didactylus) cardiac muscle. Acute exposure to vanadate oligomers
    • Aureliano M, Joaquim N, Sousa A, Martins H, Coucelo JM. Oxidative stress in toadfish (Halobactrachus didactylus) cardiac muscle. Acute exposure to vanadate oligomers. J Inorg Biochem 2002;90:159-65.
    • (2002) J Inorg Biochem , vol.90 , pp. 159-165
    • Aureliano, M.1    Joaquim, N.2    Sousa, A.3    Martins, H.4    Coucelo, J.M.5
  • 3
    • 28444444952 scopus 로고    scopus 로고
    • Interactions of vanadium(V)-citrate complexes with the sarcoplasmic reticulum calcium pump
    • Aureliano M, Tiago T, Gandara RM, et al. Interactions of vanadium(V)-citrate complexes with the sarcoplasmic reticulum calcium pump. J Inorg Biochem 2005;99:2355-61.
    • (2005) J Inorg Biochem , vol.99 , pp. 2355-2361
    • Aureliano, M.1    Tiago, T.2    Gandara, R.M.3
  • 5
    • 0030898994 scopus 로고    scopus 로고
    • Hydroxyl free radicals generated by vanadyl[IV] induce cell blebbing in mitotic human Chang liver cells
    • Bay BH, Sit KH, Paramanantham R, Chan YG. Hydroxyl free radicals generated by vanadyl[IV] induce cell blebbing in mitotic human Chang liver cells. BioMetals 1997;10:119-22.
    • (1997) BioMetals , vol.10 , pp. 119-122
    • Bay, B.H.1    Sit, K.H.2    Paramanantham, R.3    Chan, Y.G.4
  • 6
    • 0029614706 scopus 로고
    • Peroxovanadium compounds: Biological actions and mechanism of insulin-mimetics
    • Bevan AP, Drake PG, Yale JF, Shaver A, Posner BI. Peroxovanadium compounds: biological actions and mechanism of insulin-mimetics. Mol Cell Biochem 1995;153:49-58.
    • (1995) Mol Cell Biochem , vol.153 , pp. 49-58
    • Bevan, A.P.1    Drake, P.G.2    Yale, J.F.3    Shaver, A.4    Posner, B.I.5
  • 7
    • 0028221248 scopus 로고
    • Renal toxicity and arterial hypertension in rats chronically exposed to vanadate
    • Boscolo P, Carmignani M, Volpe AR, et al. Renal toxicity and arterial hypertension in rats chronically exposed to vanadate. Occup Environ Med 1994;51:500-3.
    • (1994) Occup Environ Med , vol.51 , pp. 500-503
    • Boscolo, P.1    Carmignani, M.2    Volpe, A.R.3
  • 8
    • 0021265447 scopus 로고
    • Effects of vanadate on intracellular reduction equivalents in mouse liver and the fate of vanadium in plasma, erythrocytes and liver
    • Bruech M, Quintanilla ME, Legrum W, Koch J, Netter KJ, Fuhrmann GF. Effects of vanadate on intracellular reduction equivalents in mouse liver and the fate of vanadium in plasma, erythrocytes and liver. Toxicology 1984;31:283-95.
    • (1984) Toxicology , vol.31 , pp. 283-295
    • Bruech, M.1    Quintanilla, M.E.2    Legrum, W.3    Koch, J.4    Netter, K.J.5    Fuhrmann, G.F.6
  • 9
    • 0027162331 scopus 로고
    • Acute hypertensive response to saline induced by vanadate, an insulinomimetic agent
    • Bursztyn M, Mekler J. Acute hypertensive response to saline induced by vanadate, an insulinomimetic agent. J Hypertens 1993;11:605-9.
    • (1993) J Hypertens , vol.11 , pp. 605-609
    • Bursztyn, M.1    Mekler, J.2
  • 10
    • 0018800378 scopus 로고
    • The fate of cytoplasmic vanadium
    • Cantley LC Jr, Aisen P. The fate of cytoplasmic vanadium. Biol Chem 1979;254:1781-4.
    • (1979) Biol Chem , vol.254 , pp. 1781-1784
    • Cantley Jr., L.C.1    Aisen, P.2
  • 14
    • 0035877142 scopus 로고    scopus 로고
    • Reduced glutathione protect cells from ouabain toxicity
    • Capella LS, Gefe MR, Silva EF, et al. Reduced glutathione protect cells from ouabain toxicity. Biochim Biophys Acta 2001;1526:293-300.
    • (2001) Biochim Biophys Acta , vol.1526 , pp. 293-300
    • Capella, L.S.1    Gefe, M.R.2    Silva, E.F.3
  • 15
    • 0036399445 scopus 로고    scopus 로고
    • Mechanisms of vanadate-induced cellular toxicity: Role of cellular glutathione and NADPH
    • Capella LS, Gefe MR, Silva EF, et al. Mechanisms of vanadate-induced cellular toxicity: role of cellular glutathione and NADPH. Arch Biochem Biophys 2002;406:65-72.
    • (2002) Arch Biochem Biophys , vol.406 , pp. 65-72
    • Capella, L.S.1    Gefe, M.R.2    Silva, E.F.3
  • 17
    • 0026675228 scopus 로고
    • Forward mutations and DNA-protein crosslinks induced by ammonium metavanadate in cultured mammalian cells
    • Cohen MD, Klein CB, Costa M. Forward mutations and DNA-protein crosslinks induced by ammonium metavanadate in cultured mammalian cells. Mutat Res 1992;269:141-8.
    • (1992) Mutat Res , vol.269 , pp. 141-148
    • Cohen, M.D.1    Klein, C.B.2    Costa, M.3
  • 18
    • 1542378716 scopus 로고    scopus 로고
    • The chemistry and biochemistry of vanadium and the biological activities exerted by vanadium compounds
    • Crans DC, Smee JJ, Gaidamauskas E, Yang L. The chemistry and biochemistry of vanadium and the biological activities exerted by vanadium compounds. Chem Rev 2004;104:849-902.
    • (2004) Chem Rev , vol.104 , pp. 849-902
    • Crans, D.C.1    Smee, J.J.2    Gaidamauskas, E.3    Yang, L.4
  • 19
    • 0032989168 scopus 로고    scopus 로고
    • Vanadate-induced activation of activator protein-1: Role of reactive oxygen species
    • Ding M, Li J-J, Leonard SS, Ye J-P, et al. Vanadate-induced activation of activator protein-1: role of reactive oxygen species. Carcinogenesis 1999;20:663-8.
    • (1999) Carcinogenesis , vol.20 , pp. 663-668
    • Ding, M.1    Li, J.-J.2    Leonard, S.S.3    Ye, J.-P.4
  • 20
    • 0028364232 scopus 로고
    • Vanadium activates or inhibits receptor and non-receptor tyrosine kinases in cell-free experiments, depending on its oxidation state. Possible role of endogenous vanadium in controlling cellular protein kinase activity
    • Elberg G, Li J, Schechter Y. Vanadium activates or inhibits receptor and non-receptor tyrosine kinases in cell-free experiments, depending on its oxidation state. Possible role of endogenous vanadium in controlling cellular protein kinase activity. J Biol Chem 1994;269:9521-7.
    • (1994) J Biol Chem , vol.269 , pp. 9521-9527
    • Elberg, G.1    Li, J.2    Shechter, Y.3
  • 21
    • 0036273321 scopus 로고    scopus 로고
    • Vanadium in cancer treatment
    • Evangelou AM. Vanadium in cancer treatment. Crit Rev Oncol Hematol 2002;42:249-65.
    • (2002) Crit Rev Oncol Hematol , vol.42 , pp. 249-265
    • Evangelou, A.M.1
  • 22
    • 0024416087 scopus 로고
    • Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase
    • Fantus IG, Kadota S, Deragon G, Foster B, Posner B. Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase. Biochemistry 1989;28:8864-71.
    • (1989) Biochemistry , vol.28 , pp. 8864-8871
    • Fantus, I.G.1    Kadota, S.2    Deragon, G.3    Foster, B.4    Posner, B.5
  • 23
    • 0036889665 scopus 로고    scopus 로고
    • Endogenous drug transporters in in vitro and in vivo models for the prediction of drug disposition in man
    • Goh LB, Spears KJ, Yao D, et al. Endogenous drug transporters in in vitro and in vivo models for the prediction of drug disposition in man. Biochem Pharmacol 2002;64: 1569-78.
    • (2002) Biochem Pharmacol , vol.64 , pp. 1569-1578
    • Goh, L.B.1    Spears, K.J.2    Yao, D.3
  • 24
    • 0025953405 scopus 로고
    • Use of vanadate as protein-phosphotyrosine phosphatase inhibitor
    • Gordon JA. Use of vanadate as protein-phosphotyrosine phosphatase inhibitor. Methods Enzymol 1991;201:477-82.
    • (1991) Methods Enzymol , vol.201 , pp. 477-482
    • Gordon, J.A.1
  • 26
    • 0034693044 scopus 로고    scopus 로고
    • Vanadate induces p53 transactivation through hydrogen peroxide and causes apoptosis
    • Huang C, Zhang Z, Ding M, et al. Vanadate induces p53 transactivation through hydrogen peroxide and causes apoptosis. J Biol Chem 2000;275:32516-22.
    • (2000) J Biol Chem , vol.275 , pp. 32516-32522
    • Huang, C.1    Zhang, Z.2    Ding, M.3
  • 27
    • 0031022433 scopus 로고    scopus 로고
    • Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate
    • Huyer G, Liu S, Kelly J, et al. Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. J Biol Chem 1997;272:843-51.
    • (1997) J Biol Chem , vol.272 , pp. 843-851
    • Huyer, G.1    Liu, S.2    Kelly, J.3
  • 29
    • 0017758369 scopus 로고
    • Isolation of a potent (Na-K)ATPase inhibitor from striated muscle
    • Josephson L, Cantley LC. Isolation of a potent (Na-K)ATPase inhibitor from striated muscle. Biochemistry 1977;16:4572-8.
    • (1977) Biochemistry , vol.16 , pp. 4572-4578
    • Josephson, L.1    Cantley, L.C.2
  • 31
    • 0028157138 scopus 로고
    • Mutagenicity, carcinogenicity and teratogenicity of vanadium compounds
    • Léonard A, Gerber GB. Mutagenicity, carcinogenicity and teratogenicity of vanadium compounds. Mutat Res 1994;317:81-8.
    • (1994) Mutat Res , vol.317 , pp. 81-88
    • Léonard, A.1    Gerber, G.B.2
  • 32
    • 0026716423 scopus 로고
    • Superoxide generated by glutathione reductase initiates a vanadate-dependent free radical chain oxidation of NADH
    • Liochev SI, Fridovich I. Superoxide generated by glutathione reductase initiates a vanadate-dependent free radical chain oxidation of NADH. Arch Biochem Biophys 1992;294:403-6.
    • (1992) Arch Biochem Biophys , vol.294 , pp. 403-406
    • Liochev, S.I.1    Fridovich, I.2
  • 33
    • 0028287275 scopus 로고
    • Interaction of tubulin and microtubule proteins with vanadate oligomers
    • Lobert S, Isern N, Hennington BS, Correia JJ. Interaction of tubulin and microtubule proteins with vanadate oligomers. Biochemistry 1994;33:6244-52.
    • (1994) Biochemistry , vol.33 , pp. 6244-6252
    • Lobert, S.1    Isern, N.2    Hennington, B.S.3    Correia, J.J.4
  • 34
    • 0031757319 scopus 로고    scopus 로고
    • From Vanadis to Atropos: Vanadium compounds as pharmacological tools in cell death signaling
    • Morinville A, Maysinger D, Shaver A. From Vanadis to Atropos: vanadium compounds as pharmacological tools in cell death signaling. TIPS 1998;19:452-60.
    • (1998) TIPS , vol.19 , pp. 452-460
    • Morinville, A.1    Maysinger, D.2    Shaver, A.3
  • 37
    • 33749567864 scopus 로고    scopus 로고
    • Decavanadate interactions with actin: Inhibition of G-actin polymerization and stabilization of decameric vanadate
    • Ramos S, Manuel M, Tiago T, et al. Decavanadate interactions with actin: inhibition of G-actin polymerization and stabilization of decameric vanadate. J Inorg Biochem 2006;100:1734-43.
    • (2006) J Inorg Biochem , vol.100 , pp. 1734-1743
    • Ramos, S.1    Manuel, M.2    Tiago, T.3
  • 38
    • 0039569078 scopus 로고    scopus 로고
    • Multidrug resistance in tumour cells: Characterization of the multidrug resistant cell line K562-Lucena 1
    • Rumjanek VM, Trindade GS, Wagner-Souza K, et al. Multidrug resistance in tumour cells: characterization of the multidrug resistant cell line K562-Lucena 1. An Acad Bras Cienc 2001;73:57-69.
    • (2001) An Acad Bras Cienc , vol.73 , pp. 57-69
    • Rumjanek, V.M.1    Trindade, G.S.2    Wagner-Souza, K.3
  • 39
    • 0019152613 scopus 로고
    • Insulin-like stimulation of glucose oxidation in rat adipocytes by vanadyl (IV) ions
    • Schechter Y, Karlish SJD. Insulin-like stimulation of glucose oxidation in rat adipocytes by vanadyl (IV) ions. Nature 1980;284:556-8.
    • (1980) Nature , vol.284 , pp. 556-558
    • Schechter, Y.1    Karlish, S.J.D.2
  • 40
    • 0037298297 scopus 로고    scopus 로고
    • Historic perspective and recent developments on the insulin-like actions of vanadium; Toward developing vanadium-based drugs for diabetes
    • Schechter Y, Goldwaser I, Mironchik M, Fridkin M, Gefel D. Historic perspective and recent developments on the insulin-like actions of vanadium; toward developing vanadium-based drugs for diabetes. Coord Chem Rev 2003;237:3-11.
    • (2003) Coord Chem Rev , vol.237 , pp. 3-11
    • Schechter, Y.1    Goldwaser, I.2    Mironchik, M.3    Fridkin, M.4    Gefel, D.5
  • 41
    • 27144539512 scopus 로고    scopus 로고
    • Are vanadium compounds drugable? Structures and effects of antidiabetic vanadium compounds: A critical review
    • Scior T, Guevara-García A, Bernard P, Do QT, Domeyer D, Laufer S. Are vanadium compounds drugable? Structures and effects of antidiabetic vanadium compounds: a critical review. Mini-Reviews Med Chem 2005;5:1-12.
    • (2005) Mini-Reviews Med Chem , vol.5 , pp. 1-12
    • Scior, T.1    Guevara-García, A.2    Bernard, P.3    Do, Q.T.4    Domeyer, D.5    Laufer, S.6
  • 42
    • 0027417482 scopus 로고
    • Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events
    • Secrist JP, Burns LA, Karnitz L, Koretzky GA, Abraham RT. Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events. J Biol Chem 1993;268:5886-93.
    • (1993) J Biol Chem , vol.268 , pp. 5886-5893
    • Secrist, J.P.1    Burns, L.A.2    Karnitz, L.3    Koretzky, G.A.4    Abraham, R.T.5
  • 43
    • 0025993608 scopus 로고
    • Flavoenzymes reduce vanadium(V) and molecular oxygen and generate hydroxyl radical
    • Shi X, Dalal NS. Flavoenzymes reduce vanadium(V) and molecular oxygen and generate hydroxyl radical. Arch Biochem Biophys 1991;289:355-61.
    • (1991) Arch Biochem Biophys , vol.289 , pp. 355-361
    • Shi, X.1    Dalal, N.S.2
  • 44
    • 0027141003 scopus 로고
    • Vanadate-mediated hydroxyl radical generation from superoxide radical in the presence of NADH: Haber-Weiss vs Fenton mechanism
    • Shi X, Dalal NS. Vanadate-mediated hydroxyl radical generation from superoxide radical in the presence of NADH: Haber-Weiss vs Fenton mechanism. Arch Biochem Biophys 1993;307:336-41.
    • (1993) Arch Biochem Biophys , vol.307 , pp. 336-341
    • Shi, X.1    Dalal, N.S.2
  • 45
    • 0027572351 scopus 로고
    • Vanadium as a modulator of cellular regulatory cascades and oncogene expression
    • Stern A, Yin X, Tsang SS, Davidson A, Moon J. Vanadium as a modulator of cellular regulatory cascades and oncogene expression. Biochem Cell Biol 1993;71:103-12.
    • (1993) Biochem Cell Biol , vol.71 , pp. 103-112
    • Stern, A.1    Yin, X.2    Tsang, S.S.3    Davidson, A.4    Moon, J.5
  • 46
    • 33750955253 scopus 로고    scopus 로고
    • Vanadium in diabetes: 100 years from phase 0 to phase I
    • Thompson KH, Orvig C. Vanadium in diabetes: 100 years from phase 0 to phase I. J Inorg Biochem 2006;100:1925-35.
    • (2006) J Inorg Biochem , vol.100 , pp. 1925-1935
    • Thompson, K.H.1    Orvig, C.2
  • 47
    • 2442444212 scopus 로고    scopus 로고
    • Decavanadate binding to a high affinity site near the myosin catalytic centre inhibits F-actin- stimulated myosin ATPase activity
    • Tiago T, Aureliano M, Gutierrez-Merino C. Decavanadate binding to a high affinity site near the myosin catalytic centre inhibits F-actin- stimulated myosin ATPase activity. Biochemistry 2004;43:5551-61.
    • (2004) Biochemistry , vol.43 , pp. 5551-5561
    • Tiago, T.1    Aureliano, M.2    Gutierrez-Merino, C.3
  • 48
    • 0036959483 scopus 로고    scopus 로고
    • Vanadate inhibition of protein tyrosine phosphatases mimics hydrogen peroxide in the activation of the ERK pathway in alveolar macrophages
    • Torres M, Forman HJ. Vanadate inhibition of protein tyrosine phosphatases mimics hydrogen peroxide in the activation of the ERK pathway in alveolar macrophages. Ann NY Acad Sci 2002;973:345-8.
    • (2002) Ann NY Acad Sci , vol.973 , pp. 345-348
    • Torres, M.1    Forman, H.J.2
  • 49
    • 0025905753 scopus 로고
    • Mechanism of vanadate-induced activation of tyrosine phosphorylation and of the respiratory burst in HL60 cells. Role of reduced oxygen metabolites
    • Trudel S, Pâquet MR, Grinstein S. Mechanism of vanadate-induced activation of tyrosine phosphorylation and of the respiratory burst in HL60 cells. Role of reduced oxygen metabolites. Biochem J 1991;276:611-9.
    • (1991) Biochem J , vol.276 , pp. 611-619
    • Trudel, S.1    Pâquet, M.R.2    Grinstein, S.3
  • 50
    • 0026529501 scopus 로고
    • The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions
    • Volberg T, Zick Y, Dror R, et al. The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions. EMBO J 1992;11:1733-42.
    • (1992) EMBO J , vol.11 , pp. 1733-1742
    • Volberg, T.1    Zick, Y.2    Dror, R.3
  • 51
    • 0033398624 scopus 로고    scopus 로고
    • Vanadate induces apoptosis in epidermal JB6 P+ cells via hydrogen peroxide-mediated reactions
    • Ye J, Ding M, Leonard SS, et al. Vanadate induces apoptosis in epidermal JB6 P+ cells via hydrogen peroxide-mediated reactions. Mol Cell Biochem 1999;202:9-17.
    • (1999) Mol Cell Biochem , vol.202 , pp. 9-17
    • Ye, J.1    Ding, M.2    Leonard, S.S.3
  • 52
    • 0026756732 scopus 로고
    • Vanadate-induced gene expression in mouse C127 cells: Roles of oxygen derived active species
    • Yin X, Davidson AJ, Tsang SS. Vanadate-induced gene expression in mouse C127 cells: roles of oxygen derived active species. Mol Cell Biochem 1992;115:85-96.
    • (1992) Mol Cell Biochem , vol.115 , pp. 85-96
    • Yin, X.1    Davidson, A.J.2    Tsang, S.S.3
  • 53
    • 0025197060 scopus 로고
    • 2 and vanadate concomitantly stimulates protein tyrosine phosphorylation and polyphosphoinositide breakdown in different cell lines
    • 2 and vanadate concomitantly stimulates protein tyrosine phosphorylation and polyphosphoinositide breakdown in different cell lines. Biochemistry 1990;29:10240-5.
    • (1990) Biochemistry , vol.29 , pp. 10240-10245
    • Zick, Y.1    Sager-Eisenberg, R.2


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