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Volumn 36, Issue 4, 2004, Pages 507-516

Depletion of deoxyribonucleoside triphosphate pools in tumor cells by nitric oxide

Author keywords

Deoxyribonucleotide; Free radicals; Leukemia; Macrophage; Nitric oxide; Ribonucleotide reductase

Indexed keywords

CYCLIC GMP; DEOXYADENOSINE TRIPHOSPHATE; DEOXYCYTIDINE TRIPHOSPHATE; DEOXYRIBONUCLEOSIDE TRIPHOSPHATE; DIPYRIDAMOLE; HYDROXYUREA; INDUCIBLE NITRIC OXIDE SYNTHASE; NITRIC OXIDE; PYRIMIDINE NUCLEOSIDE; SCAVENGER; THYMIDINE TRIPHOSPHATE;

EID: 1242328665     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2003.11.028     Document Type: Article
Times cited : (26)

References (46)
  • 1
    • 0037082119 scopus 로고    scopus 로고
    • Ribonucleotide reductases: The evolution of allosteric regulation
    • Reichard P. Ribonucleotide reductases: the evolution of allosteric regulation. Arch. Biochem. Biophys. 397:2002;149-155.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 149-155
    • Reichard, P.1
  • 2
    • 0023025598 scopus 로고
    • Changes of deoxyribonucleoside triphosphate pools induced by hydroxyurea and their relation to DNA synthesis
    • Bianchi V., Pontis E., Reichard P. Changes of deoxyribonucleoside triphosphate pools induced by hydroxyurea and their relation to DNA synthesis. J. Biol. Chem. 261:1986;16037-16042.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16037-16042
    • Bianchi, V.1    Pontis, E.2    Reichard, P.3
  • 3
    • 0026778383 scopus 로고
    • Mechanism of action of hydroxyurea
    • Yarbro J.W. Mechanism of action of hydroxyurea. Semin. Oncol. 19:1992;1-10.
    • (1992) Semin. Oncol. , vol.19 , pp. 1-10
    • Yarbro, J.W.1
  • 6
    • 0025938548 scopus 로고
    • Inhibition of tumor cell ribonucleotide reductase by macrophage-derived nitric oxide
    • Kwon N.S., Stuehr D.J., Nathan C.F. Inhibition of tumor cell ribonucleotide reductase by macrophage-derived nitric oxide. J. Exp. Med. 174:1991;761-767.
    • (1991) J. Exp. Med. , vol.174 , pp. 761-767
    • Kwon, N.S.1    Stuehr, D.J.2    Nathan, C.F.3
  • 7
    • 0026490231 scopus 로고
    • Early loss of the tyrosyl radical in ribonucleotide reductase of adenocarcinoma cells producing nitric oxide
    • Lepoivre M., Flaman J.-M., Henry Y. Early loss of the tyrosyl radical in ribonucleotide reductase of adenocarcinoma cells producing nitric oxide. J. Biol. Chem. 267:1992;22994-23000.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22994-23000
    • Lepoivre, M.1    Flaman, J.-M.2    Henry, Y.3
  • 8
    • 0029005691 scopus 로고
    • Inhibition of ribonucleotide reductase by nitric oxide derived from thionitrites: Reversible modifications of both subunits
    • Roy B., Lepoivre M., Henry Y., Fontecave M. Inhibition of ribonucleotide reductase by nitric oxide derived from thionitrites: reversible modifications of both subunits. Biochemistry. 34:1995;5411-5418.
    • (1995) Biochemistry , vol.34 , pp. 5411-5418
    • Roy, B.1    Lepoivre, M.2    Henry, Y.3    Fontecave, M.4
  • 9
    • 0032555652 scopus 로고    scopus 로고
    • Differential sensitivity of the tyrosyl radical of mouse ribonucleotide reductase to nitric oxide and peroxynitrite
    • Guittet O., Ducastel B., Salem J.S., Henry Y., Rubin H., Lemaire G., Lepoivre M. Differential sensitivity of the tyrosyl radical of mouse ribonucleotide reductase to nitric oxide and peroxynitrite. J. Biol. Chem. 273:1998;22136-22144.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22136-22144
    • Guittet, O.1    Ducastel, B.2    Salem, J.S.3    Henry, Y.4    Rubin, H.5    Lemaire, G.6    Lepoivre, M.7
  • 11
    • 0031406827 scopus 로고    scopus 로고
    • A mechanistic analysis of nitric oxide-induced cellular toxicity
    • Burney S., Tamir S., Gal A., Tannenbaum S.R. A mechanistic analysis of nitric oxide-induced cellular toxicity. Nitric Oxide. 1:1997;130-144.
    • (1997) Nitric Oxide , vol.1 , pp. 130-144
    • Burney, S.1    Tamir, S.2    Gal, A.3    Tannenbaum, S.R.4
  • 12
    • 0030861630 scopus 로고    scopus 로고
    • A novel, nerve growth factor-activated pathway involving nitric oxide, p53, and p21(WAF1) regulates neuronal differentiation of PC12 cells
    • Poluha W., Schonhoff C.M., Harrington K.S., Lachyankar M.B., Crosbie N.E., Bulseco D.A., Ross A.H. A novel, nerve growth factor-activated pathway involving nitric oxide, p53, and p21(WAF1) regulates neuronal differentiation of PC12 cells. J. Biol. Chem. 272:1997;24002-24007.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24002-24007
    • Poluha, W.1    Schonhoff, C.M.2    Harrington, K.S.3    Lachyankar, M.B.4    Crosbie, N.E.5    Bulseco, D.A.6    Ross, A.H.7
  • 13
    • 0035853035 scopus 로고    scopus 로고
    • Nitric oxide-induced cytostasis and cell cycle arrest of a human breast cancer cell line (MDA-MB-231): Potential role of cyclin D1
    • Pervin S., Singh R., Chaudhuri G. Nitric oxide-induced cytostasis and cell cycle arrest of a human breast cancer cell line (MDA-MB-231): potential role of cyclin D1. Proc. Natl. Acad. Sci. USA. 98:2001;3583-3588.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3583-3588
    • Pervin, S.1    Singh, R.2    Chaudhuri, G.3
  • 14
    • 0032740246 scopus 로고    scopus 로고
    • Role of nitric oxide in cancer biology
    • Moochhala S., Rajnakova A. Role of nitric oxide in cancer biology. Free Radical Res. 31:1999;671-679.
    • (1999) Free Radical Res. , vol.31 , pp. 671-679
    • Moochhala, S.1    Rajnakova, A.2
  • 15
    • 0031949941 scopus 로고    scopus 로고
    • Therapy of cancer metastasis by activation of the inducible nitric oxide synthase
    • Xie K.P., Fidler I.J. Therapy of cancer metastasis by activation of the inducible nitric oxide synthase. Cancer Metastasis Rev. 17:1998;55-75.
    • (1998) Cancer Metastasis Rev. , vol.17 , pp. 55-75
    • Xie, K.P.1    Fidler, I.J.2
  • 17
    • 0027980511 scopus 로고
    • Quenching of the tyrosyl free radical of ribonucleotide reductase by nitric oxide - Relationship to cytostasis induced in tumor cells by cytotoxic macrophages
    • Lepoivre M., Flaman J.M., Bobe P., Lemaire G., Henry Y. Quenching of the tyrosyl free radical of ribonucleotide reductase by nitric oxide - relationship to cytostasis induced in tumor cells by cytotoxic macrophages. J. Biol. Chem. 269:1994;21891-21897.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21891-21897
    • Lepoivre, M.1    Flaman, J.M.2    Bobe, P.3    Lemaire, G.4    Henry, Y.5
  • 18
    • 0033556220 scopus 로고    scopus 로고
    • Preferential inhibition of inducible nitric oxide synthase in intact cells by the 4-amino analogue of tetrahydrobiopterin
    • Schmidt K., WernerFelmayer G., Mayer B., Werner E.R. Preferential inhibition of inducible nitric oxide synthase in intact cells by the 4-amino analogue of tetrahydrobiopterin. Eur. J. Biochem. 259:1999;25-31.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 25-31
    • Schmidt, K.1    Wernerfelmayer, G.2    Mayer, B.3    Werner, E.R.4
  • 19
    • 0345552249 scopus 로고    scopus 로고
    • Simultaneous determination of pyrimidine or purine deoxyribonucleoside triphosphates using a polymerase assay
    • Roy B., Beuneu C., Roux P., Buc H., Lemaire G., Lepoivre M. Simultaneous determination of pyrimidine or purine deoxyribonucleoside triphosphates using a polymerase assay. Anal. Biochem. 269:1999;403-409.
    • (1999) Anal. Biochem. , vol.269 , pp. 403-409
    • Roy, B.1    Beuneu, C.2    Roux, P.3    Buc, H.4    Lemaire, G.5    Lepoivre, M.6
  • 20
    • 0031721513 scopus 로고    scopus 로고
    • Role of the M2 subunit of ribonucleotide reductase in regulation by hydroxyurea of the activity of the anti-HIV-1 agent 2′,3′- dideoxyinosine
    • Gao W.Y., Zhou B.S., Johns D.G., Mitsuya H., Yen Y. Role of the M2 subunit of ribonucleotide reductase in regulation by hydroxyurea of the activity of the anti-HIV-1 agent 2′,3′-dideoxyinosine. Biochem. Pharmacol. 56:1998;105-112.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 105-112
    • Gao, W.Y.1    Zhou, B.S.2    Johns, D.G.3    Mitsuya, H.4    Yen, Y.5
  • 21
    • 0029987410 scopus 로고    scopus 로고
    • DNTP pools imbalance as a signal to initiate apoptosis
    • Oliver F.J., Collins M.K.L., Lopez-Rivas A. dNTP pools imbalance as a signal to initiate apoptosis. Experientia. 52:1996;995-1000.
    • (1996) Experientia , vol.52 , pp. 995-1000
    • Oliver, F.J.1    Collins, M.K.L.2    Lopez-Rivas, A.3
  • 24
    • 0034620508 scopus 로고    scopus 로고
    • An apoptotic model for nitrosative stress
    • Eu J.P., Liu L.M., Zeng M., Stamler J.S. An apoptotic model for nitrosative stress. Biochemistry. 39:2000;1040-1047.
    • (2000) Biochemistry , vol.39 , pp. 1040-1047
    • Eu, J.P.1    Liu, L.M.2    Zeng, M.3    Stamler, J.S.4
  • 26
    • 0037138464 scopus 로고    scopus 로고
    • Effects of biological DNA precursor pool asymmetry upon accuracy of DNA replication in vitro
    • Martomo S.A., Mathews C.K. Effects of biological DNA precursor pool asymmetry upon accuracy of DNA replication in vitro. Mutat. Res. 499:2002;197-211.
    • (2002) Mutat. Res. , vol.499 , pp. 197-211
    • Martomo, S.A.1    Mathews, C.K.2
  • 27
    • 0014962872 scopus 로고
    • Ribonucleotide reductase and cell proliferation. I. Variations of ribonucleotide reductase activity with tumor growth rate in a series of rat hepatomas
    • Elford H.L., Freese M., Passamani E., Morris H.P. Ribonucleotide reductase and cell proliferation. I. Variations of ribonucleotide reductase activity with tumor growth rate in a series of rat hepatomas. J. Biol. Chem. 245:1970;5228-5233.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5228-5233
    • Elford, H.L.1    Freese, M.2    Passamani, E.3    Morris, H.P.4
  • 28
    • 0020955571 scopus 로고
    • Biochemical strategy of cancer cells and the design of chemotherapy
    • Weber G. Biochemical strategy of cancer cells and the design of chemotherapy. Cancer Res. 43:1983;3466-3492.
    • (1983) Cancer Res. , vol.43 , pp. 3466-3492
    • Weber, G.1
  • 29
    • 0028049835 scopus 로고
    • Identification of genes expressed in premalignant breast disease by microscopy-directed cloning
    • Jensen R.A., Page D.L., Holt J.T. Identification of genes expressed in premalignant breast disease by microscopy-directed cloning. Proc. Natl. Acad. Sci. USA. 91:1994;9257-9261.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9257-9261
    • Jensen, R.A.1    Page, D.L.2    Holt, J.T.3
  • 30
    • 0032522647 scopus 로고    scopus 로고
    • The mammalian ribonucleotide reductase R2 component cooperates with a variety of oncogenes in mechanisms of cellular transformation
    • Fan H.Z., Villegas C., Huang A., Wright J.A. The mammalian ribonucleotide reductase R2 component cooperates with a variety of oncogenes in mechanisms of cellular transformation. Cancer Res. 58:1998;1650-1653.
    • (1998) Cancer Res. , vol.58 , pp. 1650-1653
    • Fan, H.Z.1    Villegas, C.2    Huang, A.3    Wright, J.A.4
  • 34
    • 0032879957 scopus 로고    scopus 로고
    • Nitric oxide synthase in human breast cancer is associated with tumor grade, proliferation rate, and expression of progesterone receptors
    • Reveneau S., Arnould L., Jolimoy G., Hilpert S., Lejeune P., SaintGiorgio V., Belichard C., Jeannin J.F. Nitric oxide synthase in human breast cancer is associated with tumor grade, proliferation rate, and expression of progesterone receptors. Lab. Invest. 79:1999;1215-1225.
    • (1999) Lab. Invest. , vol.79 , pp. 1215-1225
    • Reveneau, S.1    Arnould, L.2    Jolimoy, G.3    Hilpert, S.4    Lejeune, P.5    Saintgiorgio, V.6    Belichard, C.7    Jeannin, J.F.8
  • 37
    • 0032721126 scopus 로고    scopus 로고
    • Differential expression of nitric oxide synthase in human stomach cancer
    • Koh E., Noh S.H., Lee Y.D., Lee H.Y., Han J.W., Lee H.W., Hong S. Differential expression of nitric oxide synthase in human stomach cancer. Cancer Lett. 146:1999;173-180.
    • (1999) Cancer Lett. , vol.146 , pp. 173-180
    • Koh, E.1    Noh, S.H.2    Lee, Y.D.3    Lee, H.Y.4    Han, J.W.5    Lee, H.W.6    Hong, S.7
  • 38
    • 0032929020 scopus 로고    scopus 로고
    • Expression of inducible nitric oxide synthase in tumors in relation with their regression induced by lipid a in rats
    • Onier N., Hilpert S., Reveneau S., Arnould L., SaintGiorgio V., Exbrayat J.M., Jeannin J.E. Expression of inducible nitric oxide synthase in tumors in relation with their regression induced by lipid A in rats. Int. J. Cancer. 81:1999;755-760.
    • (1999) Int. J. Cancer , vol.81 , pp. 755-760
    • Onier, N.1    Hilpert, S.2    Reveneau, S.3    Arnould, L.4    Saintgiorgio, V.5    Exbrayat, J.M.6    Jeannin, J.E.7
  • 40
    • 0032817856 scopus 로고    scopus 로고
    • Inhibition of ribonucleotide reductase by a new class of isoindole derivatives: Drug synergism with cytarabine (Ara-C) and induction of cellular apoptosis
    • Nandy P., Lien E.J., Avramis V.I. Inhibition of ribonucleotide reductase by a new class of isoindole derivatives: drug synergism with cytarabine (Ara-C) and induction of cellular apoptosis. Anticancer Res. 19:1999;1625-1633.
    • (1999) Anticancer Res. , vol.19 , pp. 1625-1633
    • Nandy, P.1    Lien, E.J.2    Avramis, V.I.3
  • 41
    • 0028876651 scopus 로고
    • Induction of apoptosis in chronic myelogenous leukemia lymphocytes by hydroxyurea and adriamycin
    • Anand S., Verma H., Kumar L., Singh N. Induction of apoptosis in chronic myelogenous leukemia lymphocytes by hydroxyurea and adriamycin. Cancer Lett. 88:1995;101-105.
    • (1995) Cancer Lett. , vol.88 , pp. 101-105
    • Anand, S.1    Verma, H.2    Kumar, L.3    Singh, N.4
  • 44
    • 0035798630 scopus 로고    scopus 로고
    • Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells
    • Guittet O., Hakansson P., Voevodskaya N., Fridd S., Graslund A., Arakawa H., Nakamura Y., Thelander L. Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells. J. Biol. Chem. 276:2001;40647-40651.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40647-40651
    • Guittet, O.1    Hakansson, P.2    Voevodskaya, N.3    Fridd, S.4    Graslund, A.5    Arakawa, H.6    Nakamura, Y.7    Thelander, L.8
  • 45
    • 0042166135 scopus 로고    scopus 로고
    • Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools
    • Kimura T., Takeda S., Sagiya Y., Gotoh M., Nakamura Y., Arakawa H. Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools. Nat. Genet. 34:2003;440-445.
    • (2003) Nat. Genet. , vol.34 , pp. 440-445
    • Kimura, T.1    Takeda, S.2    Sagiya, Y.3    Gotoh, M.4    Nakamura, Y.5    Arakawa, H.6
  • 46
    • 0032161269 scopus 로고    scopus 로고
    • A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools
    • Zhao X., Muller E.G., Rothstein R. A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools. Mol. Cell. 2:1998;329-340.
    • (1998) Mol. Cell , vol.2 , pp. 329-340
    • Zhao, X.1    Muller, E.G.2    Rothstein, R.3


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