메뉴 건너뛰기




Volumn 81, Issue 4, 2013, Pages 664-670

Expression and/or activity of the SVCT2 ascorbate transporter may be decreased in many aggressive cancers, suggesting potential utility for sodium bicarbonate and dehydroascorbic acid in cancer therapy

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; BICARBONATE; DEHYDROASCORBIC ACID; HYPOXIA INDUCIBLE FACTOR 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; SVCT2 ASCORBATE TRANSPORTER; UNCLASSIFIED DRUG;

EID: 84883787092     PISSN: 03069877     EISSN: 15322777     Source Type: Journal    
DOI: 10.1016/j.mehy.2013.07.023     Document Type: Article
Times cited : (19)

References (95)
  • 1
    • 0035432151 scopus 로고    scopus 로고
    • Hypoxia-inducible factor: Achilles' heel of antiangiogenic cancer therapy (review)
    • Blagosklonny M.V. Hypoxia-inducible factor: Achilles' heel of antiangiogenic cancer therapy (review). Int J Oncol 2001, 19(2):257-262.
    • (2001) Int J Oncol , vol.19 , Issue.2 , pp. 257-262
    • Blagosklonny, M.V.1
  • 2
    • 4444311880 scopus 로고    scopus 로고
    • Hypoxia inducible factor-1alpha as a cancer drug target
    • Powis G., Kirkpatrick L. Hypoxia inducible factor-1alpha as a cancer drug target. Mol Cancer Ther 2004, 3(5):647-654.
    • (2004) Mol Cancer Ther , vol.3 , Issue.5 , pp. 647-654
    • Powis, G.1    Kirkpatrick, L.2
  • 3
    • 18644366801 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha and the glycolytic phenotype in tumors
    • Robey I.F., Lien A.D., Welsh S.J., Baggett B.K., Gillies R.J. Hypoxia-inducible factor-1alpha and the glycolytic phenotype in tumors. Neoplasia 2005, 7(4):324-330.
    • (2005) Neoplasia , vol.7 , Issue.4 , pp. 324-330
    • Robey, I.F.1    Lien, A.D.2    Welsh, S.J.3    Baggett, B.K.4    Gillies, R.J.5
  • 4
    • 0037096732 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1-dependent regulation of the multidrug resistance (MDR1) gene
    • Comerford K.M., Wallace T.J., Karhausen J., Louis N.A., Montalto M.C., Colgan S.P. Hypoxia-inducible factor-1-dependent regulation of the multidrug resistance (MDR1) gene. Cancer Res 2002, 62(12):3387-3394.
    • (2002) Cancer Res , vol.62 , Issue.12 , pp. 3387-3394
    • Comerford, K.M.1    Wallace, T.J.2    Karhausen, J.3    Louis, N.A.4    Montalto, M.C.5    Colgan, S.P.6
  • 5
    • 33846870322 scopus 로고    scopus 로고
    • Role of hypoxia-inducible factor-1alpha as a cancer therapy target
    • Patiar S., Harris A.L. Role of hypoxia-inducible factor-1alpha as a cancer therapy target. Endocr Relat Cancer 2006, 13(Suppl. 1):S61-S75.
    • (2006) Endocr Relat Cancer , vol.13 , Issue.SUPPL. 1
    • Patiar, S.1    Harris, A.L.2
  • 6
    • 77950922592 scopus 로고    scopus 로고
    • Practical strategies for suppressing hypoxia-inducible factor activity in cancer therapy
    • McCarty M.F., Barroso-Aranda J., Contreras F. Practical strategies for suppressing hypoxia-inducible factor activity in cancer therapy. Med Hypotheses 2010, 74(5):789-797.
    • (2010) Med Hypotheses , vol.74 , Issue.5 , pp. 789-797
    • McCarty, M.F.1    Barroso-Aranda, J.2    Contreras, F.3
  • 7
    • 56149089262 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 and cancer pathogenesis
    • Semenza G.L. Hypoxia-inducible factor 1 and cancer pathogenesis. IUBMB Life 2008, 60(9):591-597.
    • (2008) IUBMB Life , vol.60 , Issue.9 , pp. 591-597
    • Semenza, G.L.1
  • 8
    • 0041885339 scopus 로고    scopus 로고
    • HIF prolyl and asparaginyl hydroxylases in the biological response to intracellular O(2) levels
    • Masson N., Ratcliffe P.J. HIF prolyl and asparaginyl hydroxylases in the biological response to intracellular O(2) levels. J Cell Sci 2003, 116(Pt. 15):3041-3049.
    • (2003) J Cell Sci , vol.116 , Issue.PART. 15 , pp. 3041-3049
    • Masson, N.1    Ratcliffe, P.J.2
  • 9
    • 0037337763 scopus 로고    scopus 로고
    • Oxygen-dependent regulation of hypoxia-inducible factors by prolyl and asparaginyl hydroxylation
    • Lando D., Gorman J.J., Whitelaw M.L., Peet D.J. Oxygen-dependent regulation of hypoxia-inducible factors by prolyl and asparaginyl hydroxylation. Eur J Biochem 2003, 270(5):781-790.
    • (2003) Eur J Biochem , vol.270 , Issue.5 , pp. 781-790
    • Lando, D.1    Gorman, J.J.2    Whitelaw, M.L.3    Peet, D.J.4
  • 10
    • 34547493149 scopus 로고    scopus 로고
    • Hydroxylation of hypoxia-inducible transcription factors and chemical compounds targeting the HIF-alpha hydroxylases
    • Bruegge K., Jelkmann W., Metzen E. Hydroxylation of hypoxia-inducible transcription factors and chemical compounds targeting the HIF-alpha hydroxylases. Curr Med Chem 2007, 14(17):1853-1862.
    • (2007) Curr Med Chem , vol.14 , Issue.17 , pp. 1853-1862
    • Bruegge, K.1    Jelkmann, W.2    Metzen, E.3
  • 11
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando D., Peet D.J., Gorman J.J., Whelan D.A., Whitelaw M.L., Bruick R.K. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev 2002, 16(12):1466-1471.
    • (2002) Genes Dev , vol.16 , Issue.12 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 12
    • 0019905709 scopus 로고
    • Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron. The role of ascorbate in peptidyl proline hydroxylation
    • de J.L., Albracht S.P., Kemp A. Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron. The role of ascorbate in peptidyl proline hydroxylation. Biochim Biophys Acta 1982, 704(2):326-332.
    • (1982) Biochim Biophys Acta , vol.704 , Issue.2 , pp. 326-332
    • de, J.L.1    Albracht, S.P.2    Kemp, A.3
  • 13
    • 59149091875 scopus 로고    scopus 로고
    • Metal ions-stimulated iron oxidation in hydroxylases facilitates stabilization of HIF-1 alpha protein
    • Kaczmarek M., Cachau R.E., Topol I.A., Kasprzak K.S., Ghio A., Salnikow K. Metal ions-stimulated iron oxidation in hydroxylases facilitates stabilization of HIF-1 alpha protein. Toxicol Sci 2009, 107(2):394-403.
    • (2009) Toxicol Sci , vol.107 , Issue.2 , pp. 394-403
    • Kaczmarek, M.1    Cachau, R.E.2    Topol, I.A.3    Kasprzak, K.S.4    Ghio, A.5    Salnikow, K.6
  • 14
    • 33645218975 scopus 로고    scopus 로고
    • Ascorbate depletion mediates up-regulation of hypoxia-associated proteins by cell density and nickel
    • Karaczyn A., Ivanov S., Reynolds M., Zhitkovich A., Kasprzak K.S., Salnikow K. Ascorbate depletion mediates up-regulation of hypoxia-associated proteins by cell density and nickel. J Cell Biochem 2006, 97(5):1025-1035.
    • (2006) J Cell Biochem , vol.97 , Issue.5 , pp. 1025-1035
    • Karaczyn, A.1    Ivanov, S.2    Reynolds, M.3    Zhitkovich, A.4    Kasprzak, K.S.5    Salnikow, K.6
  • 15
    • 33847051180 scopus 로고    scopus 로고
    • Modulation of hypoxia-inducible factor-1 alpha in cultured primary cells by intracellular ascorbate
    • Vissers M.C., Gunningham S.P., Morrison M.J., Dachs G.U., Currie M.J. Modulation of hypoxia-inducible factor-1 alpha in cultured primary cells by intracellular ascorbate. Free Radical Biol Med 2007, 42(6):765-772.
    • (2007) Free Radical Biol Med , vol.42 , Issue.6 , pp. 765-772
    • Vissers, M.C.1    Gunningham, S.P.2    Morrison, M.J.3    Dachs, G.U.4    Currie, M.J.5
  • 16
    • 38749106115 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha stabilization in nonhypoxic conditions: role of oxidation and intracellular ascorbate depletion
    • Page E.L., Chan D.A., Giaccia A.J., Levine M., Richard D.E. Hypoxia-inducible factor-1alpha stabilization in nonhypoxic conditions: role of oxidation and intracellular ascorbate depletion. Mol Biol Cell 2008, 19(1):86-94.
    • (2008) Mol Biol Cell , vol.19 , Issue.1 , pp. 86-94
    • Page, E.L.1    Chan, D.A.2    Giaccia, A.J.3    Levine, M.4    Richard, D.E.5
  • 17
    • 77950906905 scopus 로고    scopus 로고
    • Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents
    • Flashman E., Davies S.L., Yeoh K.K., Schofield C.J. Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents. Biochem J 2010, 427(1):135-142.
    • (2010) Biochem J , vol.427 , Issue.1 , pp. 135-142
    • Flashman, E.1    Davies, S.L.2    Yeoh, K.K.3    Schofield, C.J.4
  • 18
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells
    • Knowles H.J., Raval R.R., Harris A.L., Ratcliffe P.J. Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells. Cancer Res 2003, 63(8):1764-1768.
    • (2003) Cancer Res , vol.63 , Issue.8 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3    Ratcliffe, P.J.4
  • 19
    • 29644442625 scopus 로고    scopus 로고
    • Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1
    • Lu H., Dalgard C.L., Mohyeldin A., McFate T., Tait A.S., Verma A. Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1. J Biol Chem 2005, 280(51):41928-41939.
    • (2005) J Biol Chem , vol.280 , Issue.51 , pp. 41928-41939
    • Lu, H.1    Dalgard, C.L.2    Mohyeldin, A.3    McFate, T.4    Tait, A.S.5    Verma, A.6
  • 20
    • 33846630894 scopus 로고    scopus 로고
    • Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro
    • Pan Y., Mansfield K.D., Bertozzi C.C., et al. Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro. Mol Cell Biol 2007, 27(3):912-925.
    • (2007) Mol Cell Biol , vol.27 , Issue.3 , pp. 912-925
    • Pan, Y.1    Mansfield, K.D.2    Bertozzi, C.C.3
  • 21
    • 77951621559 scopus 로고    scopus 로고
    • Oxidative stress therapy for solid tumors - a proposal
    • McCarty M.F., Barroso-Aranda J., Contreras F. Oxidative stress therapy for solid tumors - a proposal. Med Hypotheses 2010, 74(6):1052-1054.
    • (2010) Med Hypotheses , vol.74 , Issue.6 , pp. 1052-1054
    • McCarty, M.F.1    Barroso-Aranda, J.2    Contreras, F.3
  • 22
    • 0038687134 scopus 로고    scopus 로고
    • Redox signaling of NF-kappaB by membrane NAD(P)H oxidases in normal and malignant cells
    • Brar S.S., Kennedy T.P., Quinn M., Hoidal J.R. Redox signaling of NF-kappaB by membrane NAD(P)H oxidases in normal and malignant cells. Protoplasma 2003, 221(1-2):117-127.
    • (2003) Protoplasma , vol.221 , Issue.1-2 , pp. 117-127
    • Brar, S.S.1    Kennedy, T.P.2    Quinn, M.3    Hoidal, J.R.4
  • 23
    • 0034682786 scopus 로고    scopus 로고
    • Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1alpha during hypoxia: a mechanism of O2 sensing
    • Chandel N.S., McClintock D.S., Feliciano C.E., et al. Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1alpha during hypoxia: a mechanism of O2 sensing. J Biol Chem 2000, 275(33):25130-25138.
    • (2000) J Biol Chem , vol.275 , Issue.33 , pp. 25130-25138
    • Chandel, N.S.1    McClintock, D.S.2    Feliciano, C.E.3
  • 24
  • 25
    • 33747596652 scopus 로고    scopus 로고
    • Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia
    • Guzy R.D., Schumacker P.T. Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia. Exp Physiol 2006, 91(5):807-819.
    • (2006) Exp Physiol , vol.91 , Issue.5 , pp. 807-819
    • Guzy, R.D.1    Schumacker, P.T.2
  • 26
    • 53049087909 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells
    • McFate T., Mohyeldin A., Lu H., et al. Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells. J Biol Chem 2008, 283(33):22700-22708.
    • (2008) J Biol Chem , vol.283 , Issue.33 , pp. 22700-22708
    • McFate, T.1    Mohyeldin, A.2    Lu, H.3
  • 27
    • 19944433653 scopus 로고    scopus 로고
    • Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase
    • Selak M.A., Armour S.M., MacKenzie E.D., et al. Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase. Cancer Cell 2005, 7(1):77-85.
    • (2005) Cancer Cell , vol.7 , Issue.1 , pp. 77-85
    • Selak, M.A.1    Armour, S.M.2    MacKenzie, E.D.3
  • 28
    • 35448961940 scopus 로고    scopus 로고
    • HIF-1 mediates the Warburg effect in clear cell renal carcinoma
    • Semenza G.L. HIF-1 mediates the Warburg effect in clear cell renal carcinoma. J Bioenerg Biomembr 2007, 39(3):231-234.
    • (2007) J Bioenerg Biomembr , vol.39 , Issue.3 , pp. 231-234
    • Semenza, G.L.1
  • 29
    • 4544342570 scopus 로고    scopus 로고
    • Nuclear factor-kappaB: the enemy within
    • Aggarwal B.B. Nuclear factor-kappaB: the enemy within. Cancer Cell 2004, 6(3):203-208.
    • (2004) Cancer Cell , vol.6 , Issue.3 , pp. 203-208
    • Aggarwal, B.B.1
  • 30
    • 33746647829 scopus 로고    scopus 로고
    • Preadministration of high-dose salicylates, suppressors of NF-kappaB activation, may increase the chemosensitivity of many cancers: an example of proapoptotic signal modulation therapy
    • McCarty M.F., Block K.I. Preadministration of high-dose salicylates, suppressors of NF-kappaB activation, may increase the chemosensitivity of many cancers: an example of proapoptotic signal modulation therapy. Integr Cancer Ther 2006, 5(3):252-268.
    • (2006) Integr Cancer Ther , vol.5 , Issue.3 , pp. 252-268
    • McCarty, M.F.1    Block, K.I.2
  • 31
    • 45349097483 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor-1alpha by NF-kappaB
    • van U.P., Kenneth N.S., Rocha S. Regulation of hypoxia-inducible factor-1alpha by NF-kappaB. Biochem J 2008, 412(3):477-484.
    • (2008) Biochem J , vol.412 , Issue.3 , pp. 477-484
    • van, U.P.1    Kenneth, N.S.2    Rocha, S.3
  • 32
    • 0037195261 scopus 로고    scopus 로고
    • Vitamin C suppresses TNF alpha-induced NF kappa B activation by inhibiting I kappa B alpha phosphorylation
    • Carcamo J.M., Pedraza A., Borquez-Ojeda O., Golde D.W. Vitamin C suppresses TNF alpha-induced NF kappa B activation by inhibiting I kappa B alpha phosphorylation. Biochemistry 2002, 41(43):12995-13002.
    • (2002) Biochemistry , vol.41 , Issue.43 , pp. 12995-13002
    • Carcamo, J.M.1    Pedraza, A.2    Borquez-Ojeda, O.3    Golde, D.W.4
  • 33
    • 0027076462 scopus 로고
    • Alpha-lipoic acid is a potent inhibitor of NF-kappa B activation in human T cells
    • Suzuki Y.J., Aggarwal B.B., Packer L. Alpha-lipoic acid is a potent inhibitor of NF-kappa B activation in human T cells. Biochem Biophys Res Commun 1992, 189(3):1709-1715.
    • (1992) Biochem Biophys Res Commun , vol.189 , Issue.3 , pp. 1709-1715
    • Suzuki, Y.J.1    Aggarwal, B.B.2    Packer, L.3
  • 34
    • 0035158577 scopus 로고    scopus 로고
    • Alpha-lipoic acid inhibits TNF-alpha-induced NF-kappaB activation and adhesion molecule expression in human aortic endothelial cells
    • Zhang W.J., Frei B. Alpha-lipoic acid inhibits TNF-alpha-induced NF-kappaB activation and adhesion molecule expression in human aortic endothelial cells. FASEB J 2001, 15(13):2423-2432.
    • (2001) FASEB J , vol.15 , Issue.13 , pp. 2423-2432
    • Zhang, W.J.1    Frei, B.2
  • 35
    • 0034110596 scopus 로고    scopus 로고
    • Thioredoxin inhibits tumor necrosis factor- or interleukin-1-induced NF-kappaB activation at a level upstream of NF-kappaB-inducing kinase
    • Takeuchi J., Hirota K., Itoh T., et al. Thioredoxin inhibits tumor necrosis factor- or interleukin-1-induced NF-kappaB activation at a level upstream of NF-kappaB-inducing kinase. Antioxid Redox Signal 2000, 2(1):83-92.
    • (2000) Antioxid Redox Signal , vol.2 , Issue.1 , pp. 83-92
    • Takeuchi, J.1    Hirota, K.2    Itoh, T.3
  • 36
    • 0034945361 scopus 로고    scopus 로고
    • Hydrogen peroxide activates NFkappaB and the interleukin-6 promoter through NFkappaB-inducing kinase
    • Zhang J., Johnston G., Stebler B., Keller E.T. Hydrogen peroxide activates NFkappaB and the interleukin-6 promoter through NFkappaB-inducing kinase. Antioxid Redox Signal 2001, 3(3):493-504.
    • (2001) Antioxid Redox Signal , vol.3 , Issue.3 , pp. 493-504
    • Zhang, J.1    Johnston, G.2    Stebler, B.3    Keller, E.T.4
  • 37
    • 3242695967 scopus 로고    scopus 로고
    • Vitamin C is a kinase inhibitor: dehydroascorbic acid inhibits IkappaBalpha kinase beta
    • Carcamo J.M., Pedraza A., Borquez-Ojeda O., Zhang B., Sanchez R., Golde D.W. Vitamin C is a kinase inhibitor: dehydroascorbic acid inhibits IkappaBalpha kinase beta. Mol Cell Biol 2004, 24(15):6645-6652.
    • (2004) Mol Cell Biol , vol.24 , Issue.15 , pp. 6645-6652
    • Carcamo, J.M.1    Pedraza, A.2    Borquez-Ojeda, O.3    Zhang, B.4    Sanchez, R.5    Golde, D.W.6
  • 38
    • 33845321931 scopus 로고    scopus 로고
    • Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving insight into hypoxia-induced NFkappaB activity
    • Cummins E.P., Berra E., Comerford K.M., et al. Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving insight into hypoxia-induced NFkappaB activity. Proc Natl Acad Sci USA 2006, 103(48):18154-18159.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.48 , pp. 18154-18159
    • Cummins, E.P.1    Berra, E.2    Comerford, K.M.3
  • 39
    • 84876515209 scopus 로고    scopus 로고
    • High concentrations of l-ascorbic acid specifically inhibit the growth of human leukemic cells via downregulation of HIF-1alpha transcription
    • Kawada H., Kaneko M., Sawanobori M., et al. High concentrations of l-ascorbic acid specifically inhibit the growth of human leukemic cells via downregulation of HIF-1alpha transcription. PLoS One 2013, 8(4):e62717.
    • (2013) PLoS One , vol.8 , Issue.4
    • Kawada, H.1    Kaneko, M.2    Sawanobori, M.3
  • 40
    • 0035010528 scopus 로고    scopus 로고
    • Vitamin C transport systems of mammalian cells
    • Liang W.J., Johnson D., Jarvis S.M. Vitamin C transport systems of mammalian cells. Mol Membr Biol 2001, 18(1):87-95.
    • (2001) Mol Membr Biol , vol.18 , Issue.1 , pp. 87-95
    • Liang, W.J.1    Johnson, D.2    Jarvis, S.M.3
  • 42
    • 77954620240 scopus 로고    scopus 로고
    • Cellular pathways for transport and efflux of ascorbate and dehydroascorbate
    • Corti A., Casini A.F., Pompella A. Cellular pathways for transport and efflux of ascorbate and dehydroascorbate. Arch Biochem Biophys 2010, 500(2):107-115.
    • (2010) Arch Biochem Biophys , vol.500 , Issue.2 , pp. 107-115
    • Corti, A.1    Casini, A.F.2    Pompella, A.3
  • 43
    • 78449246977 scopus 로고    scopus 로고
    • Histidine residues in the Na+-coupled ascorbic acid transporter-2 (SVCT2) are central regulators of SVCT2 function, modulating pH sensitivity, transporter kinetics, Na+ cooperativity, conformational stability, and subcellular localization
    • Ormazabal V., Zuniga F.A., Escobar E., et al. Histidine residues in the Na+-coupled ascorbic acid transporter-2 (SVCT2) are central regulators of SVCT2 function, modulating pH sensitivity, transporter kinetics, Na+ cooperativity, conformational stability, and subcellular localization. J Biol Chem 2010, 285(47):36471-36485.
    • (2010) J Biol Chem , vol.285 , Issue.47 , pp. 36471-36485
    • Ormazabal, V.1    Zuniga, F.A.2    Escobar, E.3
  • 44
    • 0018669229 scopus 로고
    • Failure of high-dose vitamin C (ascorbic acid) therapy to benefit patients with advanced cancer. A controlled trial
    • Creagan E.T., Moertel C.G., O'Fallon J.R., et al. Failure of high-dose vitamin C (ascorbic acid) therapy to benefit patients with advanced cancer. A controlled trial. N Engl J Med 1979, 301(13):687-690.
    • (1979) N Engl J Med , vol.301 , Issue.13 , pp. 687-690
    • Creagan, E.T.1    Moertel, C.G.2    O'Fallon, J.R.3
  • 45
    • 0021955675 scopus 로고
    • High-dose vitamin C versus placebo in the treatment of patients with advanced cancer who have had no prior chemotherapy. A randomized double-blind comparison
    • Moertel C.G., Fleming T.R., Creagan E.T., Rubin J., O'Connell M.J., Ames M.M. High-dose vitamin C versus placebo in the treatment of patients with advanced cancer who have had no prior chemotherapy. A randomized double-blind comparison. N Engl J Med 1985, 312(3):137-141.
    • (1985) N Engl J Med , vol.312 , Issue.3 , pp. 137-141
    • Moertel, C.G.1    Fleming, T.R.2    Creagan, E.T.3    Rubin, J.4    O'Connell, M.J.5    Ames, M.M.6
  • 46
    • 77955037416 scopus 로고    scopus 로고
    • Low ascorbate levels are associated with increased hypoxia-inducible factor-1 activity and an aggressive tumor phenotype in endometrial cancer
    • Kuiper C., Molenaar I.G., Dachs G.U., Currie M.J., Sykes P.H., Vissers M.C. Low ascorbate levels are associated with increased hypoxia-inducible factor-1 activity and an aggressive tumor phenotype in endometrial cancer. Cancer Res 2010, 70(14):5749-5758.
    • (2010) Cancer Res , vol.70 , Issue.14 , pp. 5749-5758
    • Kuiper, C.1    Molenaar, I.G.2    Dachs, G.U.3    Currie, M.J.4    Sykes, P.H.5    Vissers, M.C.6
  • 47
    • 70350719350 scopus 로고    scopus 로고
    • 6-Deoxy-6-[131I]iodo-l-ascorbic acid for the in vivo study of ascorbate: autoradiography, biodistribution in normal and hypolipidemic rats, and in tumor-bearing nude mice
    • Kim J., Yamamoto F., Gondo S., Yanase T., Mukai T., Maeda M. 6-Deoxy-6-[131I]iodo-l-ascorbic acid for the in vivo study of ascorbate: autoradiography, biodistribution in normal and hypolipidemic rats, and in tumor-bearing nude mice. Biol Pharm Bull 2009, 32(11):1906-1911.
    • (2009) Biol Pharm Bull , vol.32 , Issue.11 , pp. 1906-1911
    • Kim, J.1    Yamamoto, F.2    Gondo, S.3    Yanase, T.4    Mukai, T.5    Maeda, M.6
  • 48
    • 0024408986 scopus 로고
    • Blood flow, oxygen and nutrient supply, and metabolic microenvironment of human tumors: a review
    • Vaupel P., Kallinowski F., Okunieff P. Blood flow, oxygen and nutrient supply, and metabolic microenvironment of human tumors: a review. Cancer Res 1989, 49(23):6449-6465.
    • (1989) Cancer Res , vol.49 , Issue.23 , pp. 6449-6465
    • Vaupel, P.1    Kallinowski, F.2    Okunieff, P.3
  • 50
    • 65549170684 scopus 로고    scopus 로고
    • The potential role of systemic buffers in reducing intratumoral extracellular pH and acid-mediated invasion
    • Silva A.S., Yunes J.A., Gillies R.J., Gatenby R.A. The potential role of systemic buffers in reducing intratumoral extracellular pH and acid-mediated invasion. Cancer Res 2009, 69(6):2677-2684.
    • (2009) Cancer Res , vol.69 , Issue.6 , pp. 2677-2684
    • Silva, A.S.1    Yunes, J.A.2    Gillies, R.J.3    Gatenby, R.A.4
  • 51
    • 77957979206 scopus 로고    scopus 로고
    • Manipulating tumor acidification as a cancer treatment strategy
    • McCarty M.F., Whitaker J. Manipulating tumor acidification as a cancer treatment strategy. Altern Med Rev 2010, 15(3):264-272.
    • (2010) Altern Med Rev , vol.15 , Issue.3 , pp. 264-272
    • McCarty, M.F.1    Whitaker, J.2
  • 52
    • 0037192802 scopus 로고    scopus 로고
    • Acidic extracellular pH induces vascular endothelial growth factor (VEGF) in human glioblastoma cells via ERK1/2 MAPK signaling pathway: mechanism of low pH-induced VEGF
    • Xu L., Fukumura D., Jain R.K. Acidic extracellular pH induces vascular endothelial growth factor (VEGF) in human glioblastoma cells via ERK1/2 MAPK signaling pathway: mechanism of low pH-induced VEGF. J Biol Chem 2002, 277(13):11368-11374.
    • (2002) J Biol Chem , vol.277 , Issue.13 , pp. 11368-11374
    • Xu, L.1    Fukumura, D.2    Jain, R.K.3
  • 53
    • 0034662635 scopus 로고    scopus 로고
    • Acidic pH-induced elevation in interleukin 8 expression by human ovarian carcinoma cells
    • Xu L., Fidler I.J. Acidic pH-induced elevation in interleukin 8 expression by human ovarian carcinoma cells. Cancer Res 2000, 60(16):4610-4616.
    • (2000) Cancer Res , vol.60 , Issue.16 , pp. 4610-4616
    • Xu, L.1    Fidler, I.J.2
  • 54
    • 20144378365 scopus 로고    scopus 로고
    • Acidic extracellular pH induces matrix metalloproteinase-9 expression in mouse metastatic melanoma cells through the phospholipase d-mitogen-activated protein kinase signaling
    • Kato Y., Lambert C.A., Colige A.C., et al. Acidic extracellular pH induces matrix metalloproteinase-9 expression in mouse metastatic melanoma cells through the phospholipase d-mitogen-activated protein kinase signaling. J Biol Chem 2005, 280(12):10938-10944.
    • (2005) J Biol Chem , vol.280 , Issue.12 , pp. 10938-10944
    • Kato, Y.1    Lambert, C.A.2    Colige, A.C.3
  • 55
    • 33746149756 scopus 로고    scopus 로고
    • Acidic extracellular pH promotes experimental metastasis of human melanoma cells in athymic nude mice
    • Rofstad E.K., Mathiesen B., Kindem K., Galappathi K. Acidic extracellular pH promotes experimental metastasis of human melanoma cells in athymic nude mice. Cancer Res 2006, 66(13):6699-6707.
    • (2006) Cancer Res , vol.66 , Issue.13 , pp. 6699-6707
    • Rofstad, E.K.1    Mathiesen, B.2    Kindem, K.3    Galappathi, K.4
  • 57
    • 44449089860 scopus 로고    scopus 로고
    • Acid treatment of melanoma cells selects for invasive phenotypes
    • Moellering R.E., Black K.C., Krishnamurty C., et al. Acid treatment of melanoma cells selects for invasive phenotypes. Clin Exp Metastasis 2008, 25(4):411-425.
    • (2008) Clin Exp Metastasis , vol.25 , Issue.4 , pp. 411-425
    • Moellering, R.E.1    Black, K.C.2    Krishnamurty, C.3
  • 58
    • 0032904346 scopus 로고    scopus 로고
    • Enhancement of chemotherapy by manipulation of tumour pH
    • Raghunand N., He X., Van S.R., et al. Enhancement of chemotherapy by manipulation of tumour pH. Br J Cancer 1999, 80(7):1005-1011.
    • (1999) Br J Cancer , vol.80 , Issue.7 , pp. 1005-1011
    • Raghunand, N.1    He, X.2    Van, S.R.3
  • 59
    • 0034884690 scopus 로고    scopus 로고
    • Acute metabolic alkalosis enhances response of C3H mouse mammary tumors to the weak base mitoxantrone
    • Raghunand N., Mahoney B., Van S.R., Baggett B., Gillies R.J. Acute metabolic alkalosis enhances response of C3H mouse mammary tumors to the weak base mitoxantrone. Neoplasia 2001, 3(3):227-235.
    • (2001) Neoplasia , vol.3 , Issue.3 , pp. 227-235
    • Raghunand, N.1    Mahoney, B.2    Van, S.R.3    Baggett, B.4    Gillies, R.J.5
  • 60
    • 65549166946 scopus 로고    scopus 로고
    • Bicarbonate increases tumor pH and inhibits spontaneous metastases
    • Robey I.F., Baggett B.K., Kirkpatrick N.D., et al. Bicarbonate increases tumor pH and inhibits spontaneous metastases. Cancer Res 2009, 69(6):2260-2268.
    • (2009) Cancer Res , vol.69 , Issue.6 , pp. 2260-2268
    • Robey, I.F.1    Baggett, B.K.2    Kirkpatrick, N.D.3
  • 61
    • 9744260934 scopus 로고    scopus 로고
    • Effect of proton pump inhibitor pretreatment on resistance of solid tumors to cytotoxic drugs
    • Luciani F., Spada M., De M.A., et al. Effect of proton pump inhibitor pretreatment on resistance of solid tumors to cytotoxic drugs. J Natl Cancer Inst 2004, 96(22):1702-1713.
    • (2004) J Natl Cancer Inst , vol.96 , Issue.22 , pp. 1702-1713
    • Luciani, F.1    Spada, M.2    De, M.A.3
  • 62
    • 0035071662 scopus 로고    scopus 로고
    • The effects of extracellular pH on immune function
    • Lardner A. The effects of extracellular pH on immune function. J Leukoc Biol 2001, 69(4):522-530.
    • (2001) J Leukoc Biol , vol.69 , Issue.4 , pp. 522-530
    • Lardner, A.1
  • 63
    • 0342804262 scopus 로고    scopus 로고
    • An acidic microenvironment inhibits antitumoral non-major histocompatibility complex-restricted cytotoxicity: implications for cancer immunotherapy
    • Fischer B., Muller B., Fisch P., Kreutz W. An acidic microenvironment inhibits antitumoral non-major histocompatibility complex-restricted cytotoxicity: implications for cancer immunotherapy. J Immunother 2000, 23(2):196-207.
    • (2000) J Immunother , vol.23 , Issue.2 , pp. 196-207
    • Fischer, B.1    Muller, B.2    Fisch, P.3    Kreutz, W.4
  • 64
    • 34247352844 scopus 로고    scopus 로고
    • Inhibitory effect of tumor cell-derived lactic acid on human T cells
    • Fischer K., Hoffmann P., Voelkl S., et al. Inhibitory effect of tumor cell-derived lactic acid on human T cells. Blood 2007, 109(9):3812-3819.
    • (2007) Blood , vol.109 , Issue.9 , pp. 3812-3819
    • Fischer, K.1    Hoffmann, P.2    Voelkl, S.3
  • 66
    • 34447513075 scopus 로고    scopus 로고
    • Hypoxic regulation of glucose transport, anaerobic metabolism and angiogenesis in cancer: novel pathways and targets for anticancer therapeutics
    • Airley R.E., Mobasheri A. Hypoxic regulation of glucose transport, anaerobic metabolism and angiogenesis in cancer: novel pathways and targets for anticancer therapeutics. Chemotherapy 2007, 53(4):233-256.
    • (2007) Chemotherapy , vol.53 , Issue.4 , pp. 233-256
    • Airley, R.E.1    Mobasheri, A.2
  • 67
    • 54249098684 scopus 로고    scopus 로고
    • Vitamin C antagonizes the cytotoxic effects of antineoplastic drugs
    • Heaney M.L., Gardner J.R., Karasavvas N., et al. Vitamin C antagonizes the cytotoxic effects of antineoplastic drugs. Cancer Res 2008, 68(19):8031-8038.
    • (2008) Cancer Res , vol.68 , Issue.19 , pp. 8031-8038
    • Heaney, M.L.1    Gardner, J.R.2    Karasavvas, N.3
  • 68
    • 0030983467 scopus 로고    scopus 로고
    • Increased facilitated transport of dehydroascorbic acid without changes in sodium-dependent ascorbate transport in human melanoma cells
    • Spielholz C., Golde D.W., Houghton A.N., Nualart F., Vera J.C. Increased facilitated transport of dehydroascorbic acid without changes in sodium-dependent ascorbate transport in human melanoma cells. Cancer Res 1997, 57(12):2529-2537.
    • (1997) Cancer Res , vol.57 , Issue.12 , pp. 2529-2537
    • Spielholz, C.1    Golde, D.W.2    Houghton, A.N.3    Nualart, F.4    Vera, J.C.5
  • 69
    • 0033567885 scopus 로고    scopus 로고
    • Stromal cell oxidation: a mechanism by which tumors obtain vitamin C
    • Agus D.B., Vera J.C., Golde D.W. Stromal cell oxidation: a mechanism by which tumors obtain vitamin C. Cancer Res 1999, 59(18):4555-4558.
    • (1999) Cancer Res , vol.59 , Issue.18 , pp. 4555-4558
    • Agus, D.B.1    Vera, J.C.2    Golde, D.W.3
  • 70
    • 7444264606 scopus 로고    scopus 로고
    • Plasma membrane gamma-glutamyltransferase activity facilitates the uptake of vitamin C in melanoma cells
    • Corti A., Raggi C., Franzini M., Paolicchi A., Pompella A., Casini A.F. Plasma membrane gamma-glutamyltransferase activity facilitates the uptake of vitamin C in melanoma cells. Free Radical Biol Med 2004, 37(11):1906-1915.
    • (2004) Free Radical Biol Med , vol.37 , Issue.11 , pp. 1906-1915
    • Corti, A.1    Raggi, C.2    Franzini, M.3    Paolicchi, A.4    Pompella, A.5    Casini, A.F.6
  • 71
    • 0035949516 scopus 로고    scopus 로고
    • Dehydroascorbic acid, a blood-brain barrier transportable form of vitamin C, mediates potent cerebroprotection in experimental stroke
    • Huang J., Agus D.B., Winfree C.J., et al. Dehydroascorbic acid, a blood-brain barrier transportable form of vitamin C, mediates potent cerebroprotection in experimental stroke. Proc Natl Acad Sci USA 2001, 98(20):11720-11724.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.20 , pp. 11720-11724
    • Huang, J.1    Agus, D.B.2    Winfree, C.J.3
  • 72
    • 13244281950 scopus 로고    scopus 로고
    • Protective role of dehydroascorbate in rat liver ischemia-reperfusion injury
    • De T.V., Brizzi S., Saviozzi M., et al. Protective role of dehydroascorbate in rat liver ischemia-reperfusion injury. J Surg Res 2005, 123(2):215-221.
    • (2005) J Surg Res , vol.123 , Issue.2 , pp. 215-221
    • De, T.V.1    Brizzi, S.2    Saviozzi, M.3
  • 73
    • 34347170734 scopus 로고
    • Effects of dehydroascorbic acid on tumor metabolism
    • Heise E., Luhrs W., Neunhoeffer O. Effects of dehydroascorbic acid on tumor metabolism. Z Krebsforsch 1958, 62(5):509-515.
    • (1958) Z Krebsforsch , vol.62 , Issue.5 , pp. 509-515
    • Heise, E.1    Luhrs, W.2    Neunhoeffer, O.3
  • 74
    • 0014992566 scopus 로고
    • Antitumor potency of ascorbic, dehydroascorbic or 2,3-diketogulonic acid and their action on deoxyribonucleic acid
    • Yamafuji K., Nakamura Y., Omura H., Soeda T., Gyotoku K. Antitumor potency of ascorbic, dehydroascorbic or 2,3-diketogulonic acid and their action on deoxyribonucleic acid. Z Krebsforsch Klin Onkol Cancer Res Clin Oncol 1971, 76(1):1-7.
    • (1971) Z Krebsforsch Klin Onkol Cancer Res Clin Oncol , vol.76 , Issue.1 , pp. 1-7
    • Yamafuji, K.1    Nakamura, Y.2    Omura, H.3    Soeda, T.4    Gyotoku, K.5
  • 75
    • 0020041158 scopus 로고
    • Inhibiting effect of dehydroascorbic acid on cell division in ascites tumors in mice
    • Poydock M.E., Reikert D., Rice J., Aleandri L. Inhibiting effect of dehydroascorbic acid on cell division in ascites tumors in mice. Exp Cell Biol 1982, 50(1):34-38.
    • (1982) Exp Cell Biol , vol.50 , Issue.1 , pp. 34-38
    • Poydock, M.E.1    Reikert, D.2    Rice, J.3    Aleandri, L.4
  • 76
    • 0022219180 scopus 로고
    • Mitogenic inhibition and effect on survival of mice bearing L1210 leukemia using a combination of dehydroascorbic acid and hydroxycobalamin
    • Poydock M.E., Harguindey S., Hart T., Takita H., Kelly D. Mitogenic inhibition and effect on survival of mice bearing L1210 leukemia using a combination of dehydroascorbic acid and hydroxycobalamin. Am J Clin Oncol 1985, 8(3):266-269.
    • (1985) Am J Clin Oncol , vol.8 , Issue.3 , pp. 266-269
    • Poydock, M.E.1    Harguindey, S.2    Hart, T.3    Takita, H.4    Kelly, D.5
  • 77
    • 0025719367 scopus 로고
    • Effect of combined ascorbic acid and B-12 on survival of mice with implanted Ehrlich carcinoma and L1210 leukemia
    • Poydock M.E. Effect of combined ascorbic acid and B-12 on survival of mice with implanted Ehrlich carcinoma and L1210 leukemia. Am J Clin Nutr 1991, 54(Suppl. 6):1261S-1265S.
    • (1991) Am J Clin Nutr , vol.54 , Issue.SUPPL. 6
    • Poydock, M.E.1
  • 78
    • 41649103853 scopus 로고    scopus 로고
    • Dehydroascorbic acid as an anti-cancer agent
    • Toohey J.I. Dehydroascorbic acid as an anti-cancer agent. Cancer Lett 2008, 263(2):164-169.
    • (2008) Cancer Lett , vol.263 , Issue.2 , pp. 164-169
    • Toohey, J.I.1
  • 79
    • 34548257176 scopus 로고    scopus 로고
    • HIF-dependent antitumorigenic effect of antioxidants in vivo
    • Gao P., Zhang H., Dinavahi R., et al. HIF-dependent antitumorigenic effect of antioxidants in vivo. Cancer Cell 2007, 12(3):230-238.
    • (2007) Cancer Cell , vol.12 , Issue.3 , pp. 230-238
    • Gao, P.1    Zhang, H.2    Dinavahi, R.3
  • 80
    • 37549037040 scopus 로고    scopus 로고
    • Clinical potential of Spirulina as a source of phycocyanobilin
    • McCarty M.F. Clinical potential of Spirulina as a source of phycocyanobilin. J Med Food 2007, 10(4):566-570.
    • (2007) J Med Food , vol.10 , Issue.4 , pp. 566-570
    • McCarty, M.F.1
  • 81
    • 41849088479 scopus 로고    scopus 로고
    • Astaxanthin protects mesangial cells from hyperglycemia-induced oxidative signaling
    • Manabe E., Handa O., Naito Y., et al. Astaxanthin protects mesangial cells from hyperglycemia-induced oxidative signaling. J Cell Biochem 2008, 103(6):1925-1937.
    • (2008) J Cell Biochem , vol.103 , Issue.6 , pp. 1925-1937
    • Manabe, E.1    Handa, O.2    Naito, Y.3
  • 82
    • 67650246073 scopus 로고    scopus 로고
    • Astaxanthin protects neuronal cells against oxidative damage and is a potent candidate for brain food
    • Liu X., Osawa T. Astaxanthin protects neuronal cells against oxidative damage and is a potent candidate for brain food. Forum Nutr 2009, 61:129-135.
    • (2009) Forum Nutr , vol.61 , pp. 129-135
    • Liu, X.1    Osawa, T.2
  • 83
    • 58549103079 scopus 로고    scopus 로고
    • Astaxanthin inhibits reactive oxygen species-mediated cellular toxicity in dopaminergic SH-SY5Y cells via mitochondria-targeted protective mechanism
    • Liu X., Shibata T., Hisaka S., Osawa T. Astaxanthin inhibits reactive oxygen species-mediated cellular toxicity in dopaminergic SH-SY5Y cells via mitochondria-targeted protective mechanism. Brain Res 2009, 1254:18-27.
    • (2009) Brain Res , vol.1254 , pp. 18-27
    • Liu, X.1    Shibata, T.2    Hisaka, S.3    Osawa, T.4
  • 84
    • 77951497956 scopus 로고    scopus 로고
    • Astaxanthin protects mitochondrial redox state and functional integrity against oxidative stress
    • Wolf A.M., Asoh S., Hiranuma H., et al. Astaxanthin protects mitochondrial redox state and functional integrity against oxidative stress. J Nutr Biochem 2010, 21(5):381-389.
    • (2010) J Nutr Biochem , vol.21 , Issue.5 , pp. 381-389
    • Wolf, A.M.1    Asoh, S.2    Hiranuma, H.3
  • 85
    • 43049167532 scopus 로고    scopus 로고
    • Astaxanthin: a novel potential treatment for oxidative stress and inflammation in cardiovascular disease
    • Pashkow F.J., Watumull D.G., Campbell C.L. Astaxanthin: a novel potential treatment for oxidative stress and inflammation in cardiovascular disease. Am J Cardiol 2008, 101(10A):58D-68D.
    • (2008) Am J Cardiol , vol.101 , Issue.10 A
    • Pashkow, F.J.1    Watumull, D.G.2    Campbell, C.L.3
  • 86
    • 71849120171 scopus 로고    scopus 로고
    • Effect of astaxanthin on hepatocellular injury following ischemia/reperfusion
    • Curek G.D., Cort A., Yucel G., et al. Effect of astaxanthin on hepatocellular injury following ischemia/reperfusion. Toxicology 2010, 267(1-3):147-153.
    • (2010) Toxicology , vol.267 , Issue.1-3 , pp. 147-153
    • Curek, G.D.1    Cort, A.2    Yucel, G.3
  • 88
    • 53049103850 scopus 로고    scopus 로고
    • Dichloroacetate (DCA) as a potential metabolic-targeting therapy for cancer
    • Michelakis E.D., Webster L., Mackey J.R. Dichloroacetate (DCA) as a potential metabolic-targeting therapy for cancer. Br J Cancer 2008, 99(7):989-994.
    • (2008) Br J Cancer , vol.99 , Issue.7 , pp. 989-994
    • Michelakis, E.D.1    Webster, L.2    Mackey, J.R.3
  • 89
    • 74849137483 scopus 로고    scopus 로고
    • Reversal of the glycolytic phenotype by dichloroacetate inhibits metastatic breast cancer cell growth in vitro and in vivo
    • Sun R.C., Fadia M., Dahlstrom J.E., Parish C.R., Board P.G., Blackburn A.C. Reversal of the glycolytic phenotype by dichloroacetate inhibits metastatic breast cancer cell growth in vitro and in vivo. Breast Cancer Res Treat 2010, 120(1):253-260.
    • (2010) Breast Cancer Res Treat , vol.120 , Issue.1 , pp. 253-260
    • Sun, R.C.1    Fadia, M.2    Dahlstrom, J.E.3    Parish, C.R.4    Board, P.G.5    Blackburn, A.C.6
  • 90
    • 26444521256 scopus 로고    scopus 로고
    • Pharmacologic ascorbic acid concentrations selectively kill cancer cells: action as a pro-drug to deliver hydrogen peroxide to tissues
    • Chen Q., Espey M.G., Krishna M.C., et al. Pharmacologic ascorbic acid concentrations selectively kill cancer cells: action as a pro-drug to deliver hydrogen peroxide to tissues. Proc Natl Acad Sci USA 2005, 102(38):13604-13609.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.38 , pp. 13604-13609
    • Chen, Q.1    Espey, M.G.2    Krishna, M.C.3
  • 91
    • 34547429599 scopus 로고    scopus 로고
    • Ascorbate in pharmacologic concentrations selectively generates ascorbate radical and hydrogen peroxide in extracellular fluid in vivo
    • Chen Q., Espey M.G., Sun A.Y., et al. Ascorbate in pharmacologic concentrations selectively generates ascorbate radical and hydrogen peroxide in extracellular fluid in vivo. Proc Natl Acad Sci USA 2007, 104(21):8749-8754.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.21 , pp. 8749-8754
    • Chen, Q.1    Espey, M.G.2    Sun, A.Y.3
  • 92
    • 49649115940 scopus 로고    scopus 로고
    • Pharmacologic doses of ascorbate act as a prooxidant and decrease growth of aggressive tumor xenografts in mice
    • Chen Q., Espey M.G., Sun A.Y., et al. Pharmacologic doses of ascorbate act as a prooxidant and decrease growth of aggressive tumor xenografts in mice. Proc Natl Acad Sci USA 2008, 105(32):11105-11109.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.32 , pp. 11105-11109
    • Chen, Q.1    Espey, M.G.2    Sun, A.Y.3
  • 93
    • 79955603438 scopus 로고    scopus 로고
    • Pharmacologic ascorbate synergizes with gemcitabine in preclinical models of pancreatic cancer
    • Espey M.G., Chen P., Chalmers B., et al. Pharmacologic ascorbate synergizes with gemcitabine in preclinical models of pancreatic cancer. Free Radical Biol Med 2011, 50(11):1610-1619.
    • (2011) Free Radical Biol Med , vol.50 , Issue.11 , pp. 1610-1619
    • Espey, M.G.1    Chen, P.2    Chalmers, B.3
  • 94
    • 67349235547 scopus 로고    scopus 로고
    • Pharmacologic concentrations of ascorbate are achieved by parenteral administration and exhibit antitumoral effects
    • Verrax J., Calderon P.B. Pharmacologic concentrations of ascorbate are achieved by parenteral administration and exhibit antitumoral effects. Free Radical Biol Med 2009, 47(1):32-40.
    • (2009) Free Radical Biol Med , vol.47 , Issue.1 , pp. 32-40
    • Verrax, J.1    Calderon, P.B.2
  • 95
    • 34447288953 scopus 로고    scopus 로고
    • A two-phase strategy for treatment of oxidant-dependent cancers
    • McCarty M.F., Barroso-Aranda J., Contreras F. A two-phase strategy for treatment of oxidant-dependent cancers. Med Hypotheses 2007, 69(3):489-496.
    • (2007) Med Hypotheses , vol.69 , Issue.3 , pp. 489-496
    • McCarty, M.F.1    Barroso-Aranda, J.2    Contreras, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.