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Volumn 4, Issue NOV, 2014, Pages

Ascorbate as a cofactor for Fe-and 2-oxoglutarate dependent dioxygenases: Physiological activity in tumour growth and progression

Author keywords

2 oxoglutarate Fe(II) dependent dioxygenase; Ascorbate; Ascorbic acid; Cancer; Hydroxylation; Hypoxia inducible factor 1; TET enzymes; Tumour microenvironment; Vitamin C

Indexed keywords

2 OXOGLUTARIC ACID; ASCORBIC ACID; DIOXYGENASE; DOCETAXEL; ERLOTINIB; FLUOROURACIL; GEMCITABINE;

EID: 84915763059     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2014.00359     Document Type: Review
Times cited : (139)

References (127)
  • 1
    • 0010314023 scopus 로고
    • The chemical nature of vitamin C.
    • Svirbely, J.L. & Szent-Györgyi, A. The chemical nature of vitamin C. Biochem J 27, 279-285 (1933).
    • (1933) Biochem J , vol.27 , pp. 279-285
    • Svirbely, J.L.1    Szent-Györgyi, A.2
  • 3
    • 78650864017 scopus 로고    scopus 로고
    • Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases.
    • Loenarz, C. & Schofield, C.J. Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases. Trends Biochem Sci 36, 7-18 (2011).
    • (2011) Trends Biochem Sci , vol.36 , pp. 7-18
    • Loenarz, C.1    Schofield, C.J.2
  • 6
    • 0017891065 scopus 로고
    • Carnitine biosynthesis. beta-hydroxylation of trimethyllysine by an alpha-ketoglutarate-dependent mitochondrial dioxygenase.
    • Hulse, J.D., Ellis, S.R. & Henderson, L.M. Carnitine biosynthesis. beta-hydroxylation of trimethyllysine by an alpha-ketoglutarate-dependent mitochondrial dioxygenase. J Biol Chem 253, 1654-1659 (1978).
    • (1978) J Biol Chem , vol.253 , pp. 1654-1659
    • Hulse, J.D.1    Ellis, S.R.2    Henderson, L.M.3
  • 7
    • 0014962556 scopus 로고
    • Cofactor requirements of γ-butyrobetaine hydroxylase from rat liver.
    • Lindstedt, G. & Lindstedt, S. Cofactor requirements of γ-butyrobetaine hydroxylase from rat liver. J Biol Chem 245, 4178-4186 (1970).
    • (1970) J Biol Chem , vol.245 , pp. 4178-4186
    • Lindstedt, G.1    Lindstedt, S.2
  • 8
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • Tsukada, Y., et al. Histone demethylation by a family of JmjC domain-containing proteins. Nature 439, 811-816 (2006).
    • (2006) Nature , vol.439 , pp. 811-816
    • Tsukada, Y.1
  • 9
    • 66149146320 scopus 로고    scopus 로고
    • Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1
    • Tahiliani, M., et al. Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1. Science 324, 930-935 (2009).
    • (2009) Science , vol.324 , pp. 930-935
    • Tahiliani, M.1
  • 11
    • 84896511439 scopus 로고    scopus 로고
    • OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation
    • Singleton, R.S., et al. OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation. Proc Natl Acad Sci USA 111, 4031-4036 (2014).
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 4031-4036
    • Singleton, R.S.1
  • 12
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch.
    • Lando, D., Peet, D.J., Whelan, D.A., Gorman, J.J. & Whitelaw, M.L. Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch. Science 295, 858-861 (2002).
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 13
    • 77956189495 scopus 로고    scopus 로고
    • Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal and inner cell mass specification
    • Ito, S., et al. Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal and inner cell mass specification. Nature 466, 1129-1133 (2010).
    • (2010) Nature , vol.466 , pp. 1129-1133
    • Ito, S.1
  • 14
    • 84876463939 scopus 로고    scopus 로고
    • Breathing-in epigenetic change with vitamin C.
    • Monfort, A. & Wutz, A. Breathing-in epigenetic change with vitamin C. EMBO Rep 14, 337-346 (2013).
    • (2013) EMBO Rep , vol.14 , pp. 337-346
    • Monfort, A.1    Wutz, A.2
  • 15
    • 67650072604 scopus 로고    scopus 로고
    • Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing
    • Webby, C.J., et al. Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science 325, 90-93 (2009).
    • (2009) Science , vol.325 , pp. 90-93
    • Webby, C.J.1
  • 16
    • 84894599601 scopus 로고    scopus 로고
    • Sprouts of RNA epigenetics: the discovery of mammalian RNA demethylases
    • Zheng, G., et al. Sprouts of RNA epigenetics: the discovery of mammalian RNA demethylases. RNA Biol 10, 915-918 (2013).
    • (2013) RNA Biol , vol.10 , pp. 915-918
    • Zheng, G.1
  • 17
    • 84860871770 scopus 로고    scopus 로고
    • Kinetic analysis of FTO (fat mass and obesity-associated) reveals that it is unlikely to function as a sensor for 2-oxoglutarate.
    • Ma, M., Harding, H.P., O'Rahilly, S., Ron, D. & Yeo, G.S. Kinetic analysis of FTO (fat mass and obesity-associated) reveals that it is unlikely to function as a sensor for 2-oxoglutarate. Biochem J 444(2012).
    • (2012) Biochem J , vol.444
    • Ma, M.1    Harding, H.P.2    O'Rahilly, S.3    Ron, D.4    Yeo, G.S.5
  • 18
    • 84870308013 scopus 로고    scopus 로고
    • Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans
    • Ge, W., et al. Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans. Nat Chem Biol 8, 960-962 (2012).
    • (2012) Nat Chem Biol , vol.8 , pp. 960-962
    • Ge, W.1
  • 19
    • 0025787824 scopus 로고
    • Multicompartmental secretion of ascorbate and its dual role in dopamine beta-hydroxylation.
    • Diliberto, E.J.J., Daniels, A.J. & Viveros, O.H. Multicompartmental secretion of ascorbate and its dual role in dopamine beta-hydroxylation. Am J Clin Nutr 54, 1163S-1172S (1991).
    • (1991) Am J Clin Nutr , vol.54 , pp. 1163S-1172S
    • Diliberto, E.J.J.1    Daniels, A.J.2    Viveros, O.H.3
  • 20
    • 33847050240 scopus 로고    scopus 로고
    • Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one?
    • Ozer, A. & Bruick, R.K. Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one? Nat Chem Biol 3, 144-153 (2007).
    • (2007) Nat Chem Biol , vol.3 , pp. 144-153
    • Ozer, A.1    Bruick, R.K.2
  • 21
    • 84862819069 scopus 로고    scopus 로고
    • Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases.
    • Mantri, M., Zhang, Z., McDonough, M.A. & Schofield, C.J. Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases. FEBS J 279, 1563-1575 (2012).
    • (2012) FEBS J , vol.279 , pp. 1563-1575
    • Mantri, M.1    Zhang, Z.2    McDonough, M.A.3    Schofield, C.J.4
  • 22
    • 33749542309 scopus 로고    scopus 로고
    • Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase.
    • Hoffart, L.M., Barr, E.W., Guyer, R.B., Bollinger, J.M. & Krebs, C. Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase. Proc Natl Acad Sci USA 103, 14738-14743 (2006).
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14738-14743
    • Hoffart, L.M.1    Barr, E.W.2    Guyer, R.B.3    Bollinger, J.M.4    Krebs, C.5
  • 23
    • 79959450883 scopus 로고    scopus 로고
    • High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq
    • Schödel, J., et al. High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq. Blood 117, e207-217 (2011).
    • (2011) Blood , vol.117 , pp. e207-e217
    • Schödel, J.1
  • 24
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steadystate levels of HIF-1α in normoxia
    • Berra, E., et al. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steadystate levels of HIF-1α in normoxia. EMBO J 22, 4082-4090 (2003).
    • (2003) EMBO J , vol.22 , pp. 4082-4090
    • Berra, E.1
  • 25
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF.
    • Bruick, R.K. & McKnight, S.L. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294, 1337-1340 (2001).
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 26
    • 17944375360 scopus 로고    scopus 로고
    • elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation.
    • Epstein, A.C.R., et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54 (2001).
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.R.1
  • 27
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-1α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • Jaakkola, P., et al. Targeting of HIF-1α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 292, 468-472 (2001).
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 28
    • 0035859692 scopus 로고    scopus 로고
    • HIF-1αbinding to VHL is regulated by stimulus-sensitive prolyl hydroxylation.
    • Yu, F., White, S.B., Zhao, Q. & Lee, F.S. HIF-1α binding to VHL is regulated by stimulus-sensitive prolyl hydroxylation. Proc Natl Acad Sci USA 98, 9630-9635 (2001).
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9630-9635
    • Yu, F.1    White, S.B.2    Zhao, Q.3    Lee, F.S.4
  • 29
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando, D., et al. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev 16, 1466-1471 (2002).
    • (2002) Genes Dev , vol.16 , pp. 1466-1471
    • Lando, D.1
  • 30
    • 84902345994 scopus 로고    scopus 로고
    • TET1-mediated hydroxymethylation facilitates hypoxic gene induction in neuroblastoma
    • Mariani, Christopher J., et al. TET1-mediated hydroxymethylation facilitates hypoxic gene induction in neuroblastoma. Cell Rep 7, 1343-1352 (2014).
    • (2014) Cell Rep , vol.7 , pp. 1343-1352
    • Mariani Christopher, J.1
  • 31
    • 0032877460 scopus 로고    scopus 로고
    • Nickelinduced transformation shifts the balance between HIF-1 and p53 transcription factors.
    • Salnikow, K., An, W.G., Melillo, G., Blagosklonny, M.V. & Costa, M. Nickelinduced transformation shifts the balance between HIF-1 and p53 transcription factors. Carcinogenesis 20, 1819-1823 (1999).
    • (1999) Carcinogenesis , vol.20 , pp. 1819-1823
    • Salnikow, K.1    An, W.G.2    Melillo, G.3    Blagosklonny, M.V.4    Costa, M.5
  • 32
    • 23444447955 scopus 로고    scopus 로고
    • Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway
    • Hirsilä, M., et al. Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway. FASEB J 19, 1308-1310 (2005).
    • (2005) FASEB J , vol.19 , pp. 1308-1310
    • Hirsilä, M.1
  • 33
    • 1642315195 scopus 로고    scopus 로고
    • Catalytic properties of the asparagine hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases.
    • Koivunen, P., Hirsilä, M., Günzler, V., Kivirikko, K.I. & Myllyharju, J. Catalytic properties of the asparagine hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases. J Biol Chem 279, 9899-9904 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 9899-9904
    • Koivunen, P.1    Hirsilä, M.2    Günzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 34
    • 33947520506 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF
    • Koivunen, P., et al. Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF. J Biol Chem 282, 4524-4532 (2007).
    • (2007) J Biol Chem , vol.282 , pp. 4524-4532
    • Koivunen, P.1
  • 35
    • 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., 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 27, 912-925 (2007).
    • (2007) Mol Cell Biol , vol.27 , pp. 912-925
    • Pan, Y.1
  • 36
    • 29644442625 scopus 로고    scopus 로고
    • Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1
    • Lu, H., et al. Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1. J Biol Chem 280, 41928-41939 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 41928-41939
    • Lu, H.1
  • 37
    • 26444570010 scopus 로고    scopus 로고
    • Accumulation of Krebs cycle intermediates and over-expression of HIF1a in tumours which result from germline FH and SDH mutations
    • Pollard, P.J., et al. Accumulation of Krebs cycle intermediates and over-expression of HIF1a in tumours which result from germline FH and SDH mutations. Hum Mol Genet 14, 2231-2239 (2005).
    • (2005) Hum Mol Genet , vol.14 , pp. 2231-2239
    • Pollard, P.J.1
  • 38
    • 64849087954 scopus 로고    scopus 로고
    • Puzzling patterns of predisposition.
    • Pollard, P.J. & Ratcliffe, P.J. Puzzling patterns of predisposition. Science 324, 192-194 (2009).
    • (2009) Science , vol.324 , pp. 192-194
    • Pollard, P.J.1    Ratcliffe, P.J.2
  • 39
    • 84876889621 scopus 로고    scopus 로고
    • What a difference a hydroxyl makes: mutant IDH, (R)- 2-hydroxyglutarate, and cancer.
    • Losman, J.-A. & Kaelin, W.G. What a difference a hydroxyl makes: mutant IDH, (R)- 2-hydroxyglutarate, and cancer. Genes Dev 27, 836-852 (2013).
    • (2013) Genes Dev , vol.27 , pp. 836-852
    • Losman, J.-A.1    Kaelin, W.G.2
  • 40
    • 76049100577 scopus 로고    scopus 로고
    • HIF-1: upstream and downstream of cancer metabolism.
    • Semenza, G.L. HIF-1: upstream and downstream of cancer metabolism. Curr Opin Genet Dev 20, 51-56 (2010).
    • (2010) Curr Opin Genet Dev , vol.20 , pp. 51-56
    • Semenza, G.L.1
  • 41
    • 24144447915 scopus 로고    scopus 로고
    • Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-a activation
    • Mansfield, K.D., et al. Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-a activation. Cell Metab 1, 393-399 (2005).
    • (2005) Cell Metab , vol.1 , pp. 393-399
    • Mansfield, K.D.1
  • 42
    • 0034682786 scopus 로고    scopus 로고
    • Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1a during hypoxia
    • Chandel, N.S., et al. Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1a during hypoxia. J Biol Chem 275, 25130-25138 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 25130-25138
    • Chandel, N.S.1
  • 43
    • 24144467846 scopus 로고    scopus 로고
    • ROS: really involved in oxygen sensing.
    • Kaelin Jr, W.G. ROS: really involved in oxygen sensing. Cell Metab 1, 357-358 (2005).
    • (2005) Cell Metab , vol.1 , pp. 357-358
    • Kaelin Jr., W.G.1
  • 44
    • 49449117608 scopus 로고    scopus 로고
    • Reactive oxygen species regulate hypoxia-inducible factor 1a differentially in cancer and ischemia.
    • Qutub, A.A. & Popel, A.S. Reactive oxygen species regulate hypoxia-inducible factor 1a differentially in cancer and ischemia. Mol Cell Biol 28, 5106-5119 (2008).
    • (2008) Mol Cell Biol , vol.28 , pp. 5106-5119
    • Qutub, A.A.1    Popel, A.S.2
  • 45
    • 33846225260 scopus 로고    scopus 로고
    • Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling.
    • Hoffman, D.L., Salter, J.D. & Brookes, P.S. Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling. Am J Physiol Heart Circ Physiol 292, H101-108 (2007).
    • (2007) Am J Physiol Heart Circ Physiol , vol.292 , pp. H101-H108
    • Hoffman, D.L.1    Salter, J.D.2    Brookes, P.S.3
  • 46
    • 0034235012 scopus 로고    scopus 로고
    • Carcinogenic metals induce hypoxia-inducible factor-stimulated transcription by reactive oxygen speciesindependent mechanism.
    • Salnikow, K., Su, W., Blagosklonny, M.V. & Costa, M. Carcinogenic metals induce hypoxia-inducible factor-stimulated transcription by reactive oxygen speciesindependent mechanism. Cancer Res 60, 3375-3378 (2000).
    • (2000) Cancer Res , vol.60 , pp. 3375-3378
    • Salnikow, K.1    Su, W.2    Blagosklonny, M.V.3    Costa, M.4
  • 47
    • 84857789085 scopus 로고    scopus 로고
    • The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity
    • Masson, N., et al. The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity. EMBO Rep 13, 251-257 (2012).
    • (2012) EMBO Rep , vol.13 , pp. 251-257
    • Masson, N.1
  • 48
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxiainducible factor.
    • Hirsilä, M., Koivunen, P., Günzler, V., Kivirikko, K.I. & Myllyharju, J. Characterization of the human prolyl 4-hydroxylases that modify the hypoxiainducible factor. J Biol Chem 278, 30772-30780 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 30772-30780
    • Hirsilä, M.1    Koivunen, P.2    Günzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 49
    • 0030962028 scopus 로고    scopus 로고
    • Characterization of the iron- and 2-oxoglutaratebinding sites of human prolyl 4-hydroxylase.
    • Myllyharju, J. & Kivirikko, K.I. Characterization of the iron- and 2-oxoglutaratebinding sites of human prolyl 4-hydroxylase. EMBO J 16, 1173-1180 (1997).
    • (1997) EMBO J , vol.16 , pp. 1173-1180
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 50
    • 33645891676 scopus 로고    scopus 로고
    • Structural studies on 2-oxoglutarate oxygenases and related doublestranded ß-helix fold proteins
    • Clifton, I.J., et al. Structural studies on 2-oxoglutarate oxygenases and related doublestranded ß-helix fold proteins. J Inorg Biochem 100, 644-669 (2006).
    • (2006) J Inorg Biochem , vol.100 , pp. 644-669
    • Clifton, I.J.1
  • 51
    • 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 Jong, L., Albracht, S.P.J. & 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 704, 326-332 (1982).
    • (1982) Biochim Biophys Acta , vol.704 , pp. 326-332
    • De Jong, L.1    Albracht, S.P.J.2    Kemp, A.3
  • 52
    • 0023021512 scopus 로고
    • Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase.
    • Majamaa, K., Gunzler, V., Hanauske-Abel, H.M., Myllylä, R. & Kivirikko, K.I. Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase. J Biol Chem 261, 7819-7823 (1986).
    • (1986) J Biol Chem , vol.261 , pp. 7819-7823
    • Majamaa, K.1    Gunzler, V.2    Hanauske-Abel, H.M.3    Myllylä, R.4    Kivirikko, K.I.5
  • 53
    • 0021329173 scopus 로고
    • Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase.
    • Myllylä, R., Majamaa, K., Günzler, V., Hanauske-Abel, H.M. & Kivirikko, K.I. Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J Biol Chem 259, 5403-5405 (1984).
    • (1984) J Biol Chem , vol.259 , pp. 5403-5405
    • Myllylä, R.1    Majamaa, K.2    Günzler, V.3    Hanauske-Abel, H.M.4    Kivirikko, K.I.5
  • 54
    • 0019364028 scopus 로고
    • The function of ascorbate with respect to prolyl 4-hydroxylase activity.
    • Nietfeld, J.J. & Kemp, A. The function of ascorbate with respect to prolyl 4-hydroxylase activity. Biochim Biophys Acta 657, 159-167 (1981).
    • (1981) Biochim Biophys Acta , vol.657 , pp. 159-167
    • Nietfeld, J.J.1    Kemp, A.2
  • 55
    • 0017697003 scopus 로고
    • Mechanism of the prolyl hydroxylase reaction.
    • Tuderman, L., Myllylä, R. & Kivirikko, K.I. Mechanism of the prolyl hydroxylase reaction. Eur J Biochem 80, 341-348 (1977).
    • (1977) Eur J Biochem , vol.80 , pp. 341-348
    • Tuderman, L.1    Myllylä, R.2    Kivirikko, K.I.3
  • 56
    • 56749180745 scopus 로고    scopus 로고
    • Kinetic characterization and identification of a novel inhibitor of hypoxia-inducible factor prolyl hydroxylase 2 using a time-resolved fluorescence resonance energy transfer-based assay technology
    • Dao, J.H., et al. Kinetic characterization and identification of a novel inhibitor of hypoxia-inducible factor prolyl hydroxylase 2 using a time-resolved fluorescence resonance energy transfer-based assay technology. Anal Biochem 384, 213-223 (2009).
    • (2009) Anal Biochem , vol.384 , pp. 213-223
    • Dao, J.H.1
  • 57
    • 84881476916 scopus 로고    scopus 로고
    • Vitamin C induces Tet-dependent DNA demethylation and a blastocyst-like state in ES cells
    • Blaschke, K., et al. Vitamin C induces Tet-dependent DNA demethylation and a blastocyst-like state in ES cells. Nature 500, 222-226 (2013).
    • (2013) Nature , vol.500 , pp. 222-226
    • Blaschke, K.1
  • 58
    • 84888372386 scopus 로고    scopus 로고
    • Vitamin C modulates TET1 function during somatic cell reprogramming.
    • Chen, J., et al. Vitamin C modulates TET1 function during somatic cell reprogramming. Nat Genet (2013).
    • (2013) Nat Genet
    • Chen, J.1
  • 59
    • 84877693964 scopus 로고    scopus 로고
    • Ascorbate induces ten-eleven translocation (Tet) methylcytosine dioxygenase-mediated generation of 5-hydroxymethylcytosine.
    • Minor, E.A., Court, B.L., Young, J.I. & Wang, G. Ascorbate induces ten-eleven translocation (Tet) methylcytosine dioxygenase-mediated generation of 5-hydroxymethylcytosine. J Biol Chem 288, 13669-13674 (2013).
    • (2013) J Biol Chem , vol.288 , pp. 13669-13674
    • Minor, E.A.1    Court, B.L.2    Young, J.I.3    Wang, G.4
  • 60
    • 84880344660 scopus 로고    scopus 로고
    • Ascorbic acid enhances Tet-mediated 5-methylcytosine oxidation and promotes DNA demethylation in mammals
    • Yin, R., et al. Ascorbic acid enhances Tet-mediated 5-methylcytosine oxidation and promotes DNA demethylation in mammals. J Am Chem Soc 135, 10396-10403 (2013).
    • (2013) J Am Chem Soc , vol.135 , pp. 10396-10403
    • Yin, R.1
  • 61
    • 27644578882 scopus 로고    scopus 로고
    • Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate
    • McNeill, L.A., et al. Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate. Mol Biosyst 1, 321-324 (2005).
    • (2005) Mol Biosyst , vol.1 , pp. 321-324
    • McNeill, L.A.1
  • 62
    • 84896740551 scopus 로고    scopus 로고
    • Intracellular ascorbate enhances hypoxia-inducible factor (HIF)-hydroxylase activity and preferentially suppresses the HIF-1 transcriptional response.
    • Kuiper, C., Dachs, G.U., Currie, M.J. & Vissers, M.C.M. Intracellular ascorbate enhances hypoxia-inducible factor (HIF)-hydroxylase activity and preferentially suppresses the HIF-1 transcriptional response. Free Rad Biol Med 69, 308-317 (2014).
    • (2014) Free Rad Biol Med , vol.69 , pp. 308-317
    • Kuiper, C.1    Dachs, G.U.2    Currie, M.J.3    Vissers, M.C.M.4
  • 63
    • 0001101920 scopus 로고
    • Chelation of ferrous sulphate solutions by desferrioxamine B.
    • Goodwin, J.F. & Whitten, C.F. Chelation of ferrous sulphate solutions by desferrioxamine B. Nature 205, 281-283 (1965).
    • (1965) Nature , vol.205 , pp. 281-283
    • Goodwin, J.F.1    Whitten, C.F.2
  • 64
    • 59149091875 scopus 로고    scopus 로고
    • Metal ions-stimulated iron oxidation in hydroxylases facilitates stabilization of HIF-1αprotein
    • Kaczmarek, M., et al. Metal ions-stimulated iron oxidation in hydroxylases facilitates stabilization of HIF-1αprotein. Toxicol Sci 107, 394-403 (2009).
    • (2009) Toxicol Sci , vol.107 , pp. 394-403
    • Kaczmarek, M.1
  • 66
    • 0019231636 scopus 로고
    • Interaction of vitamin C and iron.
    • Lynch, S.R. & Cook, J.D. Interaction of vitamin C and iron. Ann NY Acad Sci 355, 32-44 (1980).
    • (1980) Ann NY Acad Sci , vol.355 , pp. 32-44
    • Lynch, S.R.1    Cook, J.D.2
  • 67
    • 77954623393 scopus 로고    scopus 로고
    • Chelation of intracellular iron enhances endothelial barrier function: a role for vitamin C?
    • May, J.M. & Qu, Z.-c. Chelation of intracellular iron enhances endothelial barrier function: a role for vitamin C? Arch Biochem Biophys 500, 162-168 (2010).
    • (2010) Arch Biochem Biophys , vol.500 , pp. 162-168
    • May, J.M.1    Qu, Z.-c.2
  • 68
    • 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 427, 135-142 (2010).
    • (2010) Biochem J , vol.427 , pp. 135-142
    • Flashman, E.1    Davies, S.L.2    Yeoh, K.K.3    Schofield, C.J.4
  • 69
    • 79956287701 scopus 로고    scopus 로고
    • Vitamin C is dispensable for oxygen sensing in vivo
    • Nytko, K.J., et al. Vitamin C is dispensable for oxygen sensing in vivo. Blood 117, 5485-5493 (2011).
    • (2011) Blood , vol.117 , pp. 5485-5493
    • Nytko, K.J.1
  • 70
    • 0036151286 scopus 로고    scopus 로고
    • Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana
    • Wilmouth, R.C., et al. Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana. Structure 10, 93-103 (2002).
    • (2002) Structure , vol.10 , pp. 93-103
    • Wilmouth, R.C.1
  • 71
    • 84860137867 scopus 로고    scopus 로고
    • Changes in protein dynamics of the DNA repair dioxygenase AlkB upon binding of Fe2+ and 2-oxoglutarate
    • Bleijlevens, B., et al. Changes in protein dynamics of the DNA repair dioxygenase AlkB upon binding of Fe2+ and 2-oxoglutarate. Biochemistry 51, 3334-3341 (2012).
    • (2012) Biochemistry , vol.51 , pp. 3334-3341
    • Bleijlevens, B.1
  • 72
    • 33845717875 scopus 로고    scopus 로고
    • Vitamin C: biosynthesis, recycling and degradation in mammals.
    • Linster, C.L. & Van Schaftingen, E. Vitamin C: biosynthesis, recycling and degradation in mammals. FEBS J 274, 1-22 (2007).
    • (2007) FEBS J , vol.274 , pp. 1-22
    • Linster, C.L.1    Van Schaftingen, E.2
  • 73
    • 84896729677 scopus 로고    scopus 로고
    • Ascorbic acid: properties and determination.
    • (ed. Caballero, B.) (Academic Press, Oxford).
    • Kall, M.A. Ascorbic acid: properties and determination. in Encyclopedia of Food Sciences and Nutrition (ed. Caballero, B.) 316-324 (Academic Press, Oxford, 2003).
    • (2003) Encyclopedia of Food Sciences and Nutrition , pp. 316-324
    • Kall, M.A.1
  • 74
    • 0029939394 scopus 로고    scopus 로고
    • Catalytic metals, ascorbate and free radicals: combinations to avoid.
    • Buettner, G.R. & Jurkiewicz, B.A. Catalytic metals, ascorbate and free radicals: combinations to avoid. Radiat Res 145, 532-541 (1996).
    • (1996) Radiat Res , vol.145 , pp. 532-541
    • Buettner, G.R.1    Jurkiewicz, B.A.2
  • 75
    • 0016586659 scopus 로고
    • Distribution of ascorbic acid, metabolites and analogues in man and animals.
    • Hornig, D. Distribution of ascorbic acid, metabolites and analogues in man and animals. Annal NY Acad Sci 258, 103-118 (1975).
    • (1975) Annal NY Acad Sci , vol.258 , pp. 103-118
    • Hornig, D.1
  • 76
    • 84875704668 scopus 로고    scopus 로고
    • Vitamin C transport and its role in the central nervous system.
    • (ed. Stanger, O.) Springer Netherlands
    • May, J.M. Vitamin C transport and its role in the central nervous system. in Water Soluble Vitamins, Vol. 56 (ed. Stanger, O.) 85-103 (Springer Netherlands, 2012).
    • (2012) Water Soluble Vitamins , vol.56 , pp. 85-103
    • May, J.M.1
  • 77
    • 0033529002 scopus 로고    scopus 로고
    • A family of mammalian Na+-dependent L-ascorbic acid transporters
    • Tsukaguchi, H., et al. A family of mammalian Na+-dependent L-ascorbic acid transporters. Nature 399, 70-75 (1999).
    • (1999) Nature , vol.399 , pp. 70-75
    • Tsukaguchi, H.1
  • 78
    • 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 500, 107-115 (2010).
    • (2010) Arch Biochem Biophys , vol.500 , pp. 107-115
    • Corti, A.1    Casini, A.F.2    Pompella, A.3
  • 79
    • 84866613772 scopus 로고    scopus 로고
    • Ascorbic acid: chemistry, biology and the treatment of cancer.
    • Du, J., Cullen, J.J. & Buettner, G.R. Ascorbic acid: chemistry, biology and the treatment of cancer. Biochim Biophys Acta 1826, 443-457 (2012).
    • (2012) Biochim Biophys Acta , vol.1826 , pp. 443-457
    • Du, J.1    Cullen, J.J.2    Buettner, G.R.3
  • 80
    • 81355134502 scopus 로고    scopus 로고
    • The SLC23 family of ascorbate transporters: ensuring that you get and keep your daily dose of vitamin C.
    • May, J.M. The SLC23 family of ascorbate transporters: ensuring that you get and keep your daily dose of vitamin C. Br J Pharmacol 164, 1793-1801 (2011).
    • (2011) Br J Pharmacol , vol.164 , pp. 1793-1801
    • May, J.M.1
  • 81
    • 0019945384 scopus 로고
    • The distribution of ascorbic acid between various cellular components of blood, in normal individuals, and its relation to the plasma concentration.
    • Evans, R.M., Currie, L. & Campbell, A. The distribution of ascorbic acid between various cellular components of blood, in normal individuals, and its relation to the plasma concentration. Br J Nutr 47, 473-482 (1982).
    • (1982) Br J Nutr , vol.47 , pp. 473-482
    • Evans, R.M.1    Currie, L.2    Campbell, A.3
  • 83
    • 9244219627 scopus 로고    scopus 로고
    • Vitamin C pharmacokinetics in healthy volunteers: evidence for a recommended dietary allowance
    • Levine, M., et al. Vitamin C pharmacokinetics in healthy volunteers: evidence for a recommended dietary allowance. Proc Natl Acad Sci USA 93, 3704-3709 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3704-3709
    • Levine, M.1
  • 84
    • 0019967265 scopus 로고
    • Severe hypovitaminosis C in lung-cancer patients: the utilization of vitamin C in surgical repair and lymphocyte-related host resistance.
    • Anthony, H.M. & Schorah, C.J. Severe hypovitaminosis C in lung-cancer patients: the utilization of vitamin C in surgical repair and lymphocyte-related host resistance. Br J Cancer 46, 354-367 (1982).
    • (1982) Br J Cancer , vol.46 , pp. 354-367
    • Anthony, H.M.1    Schorah, C.J.2
  • 85
    • 38349064996 scopus 로고    scopus 로고
    • Increased levels of 8-hydroxydeoxyguanosine and its relationship with lipid peroxidation and antioxidant vitamins in lung cancer
    • Çaliskan-Can, E., et al. Increased levels of 8-hydroxydeoxyguanosine and its relationship with lipid peroxidation and antioxidant vitamins in lung cancer. Clin Chem Lab Med. 46, 107-112 (2008).
    • (2008) Clin Chem Lab Med. , vol.46 , pp. 107-112
    • Çaliskan-Can, E.1
  • 86
    • 0033001564 scopus 로고    scopus 로고
    • Serum antioxidative vitamin levels and lipid peroxidation in gastric carcinoma patients.
    • Choi, M.-A., Kim, B.-S. & Yu, R. Serum antioxidative vitamin levels and lipid peroxidation in gastric carcinoma patients. Cancer Lett 136, 89-93 (1999).
    • (1999) Cancer Lett , vol.136 , pp. 89-93
    • Choi, M.-A.1    Kim, B.-S.2    Yu, R.3
  • 87
    • 31844454246 scopus 로고    scopus 로고
    • Glutathione, ascorbic acid and antioxidant enzymes in the tumour tissue and blood of patients with oral squamous cell carcinoma.
    • Fiaschi, A.I., Cozzolino, A., Ruggiero, G. & Giorgi, G. Glutathione, ascorbic acid and antioxidant enzymes in the tumour tissue and blood of patients with oral squamous cell carcinoma. Eur Rev Med Pharamcol Sci 9, 361-367 (2005).
    • (2005) Eur Rev Med Pharamcol Sci , vol.9 , pp. 361-367
    • Fiaschi, A.I.1    Cozzolino, A.2    Ruggiero, G.3    Giorgi, G.4
  • 88
    • 84858724196 scopus 로고    scopus 로고
    • Nutritional status, dietary intake and serum levels of vitamin C upon diagnosis of cancer in children and adolescents.
    • Lima de Araújo, L., Maciel Barbosa, J., Gomes Ribeiro, A.P., Oliveira dos Santos, A.C. & Pedrosa, F. Nutritional status, dietary intake and serum levels of vitamin C upon diagnosis of cancer in children and adolescents. Nutr Hosp 27, 496-503 (2012).
    • (2012) Nutr Hosp , vol.27 , pp. 496-503
    • de Araújo, L.L.1    Maciel Barbosa, J.2    Gomes Ribeiro, A.P.3    dos Santos, O.A.C.4    Pedrosa, F.5
  • 89
    • 13444301515 scopus 로고    scopus 로고
    • Vitamin C deficiency in cancer patients.
    • Mayland, C.R., Bennett, M.I. & Allan, K. Vitamin C deficiency in cancer patients. Palliat Med 19, 17-20 (2005).
    • (2005) Palliat Med , vol.19 , pp. 17-20
    • Mayland, C.R.1    Bennett, M.I.2    Allan, K.3
  • 90
    • 3042628499 scopus 로고    scopus 로고
    • Evaluation of antioxidant enzymes activity and concentration of non-enzymatic antioxidants in human brain tumours.
    • Dudek, H., Farbiszewski, R., Rydzewska, M., Michno, T. & Kozlowksi, A. Evaluation of antioxidant enzymes activity and concentration of non-enzymatic antioxidants in human brain tumours. Wiad Lek 57, 16-19 (2004).
    • (2004) Wiad Lek , vol.57 , pp. 16-19
    • Dudek, H.1    Farbiszewski, R.2    Rydzewska, M.3    Michno, T.4    Kozlowksi, A.5
  • 91
    • 0028034176 scopus 로고
    • Levels of water-soluble antioxidants in astrocytoma and in adjacent tumor-free tissue.
    • Landolt, H., Langemann, H., Probst, A. & Gratzl, O. Levels of water-soluble antioxidants in astrocytoma and in adjacent tumor-free tissue. J Neuro-Oncol 21, 127-133 (1994).
    • (1994) J Neuro-Oncol , vol.21 , pp. 127-133
    • Landolt, H.1    Langemann, H.2    Probst, A.3    Gratzl, O.4
  • 92
    • 0035851008 scopus 로고    scopus 로고
    • Antioxidant status and lipid peroxidation in colorectal cancer.
    • Skrzydlewska, E. & Stankiewicz, A. Antioxidant status and lipid peroxidation in colorectal cancer. J Toxicol Env Heal A 64, 213-222 (2001).
    • (2001) J Toxicol Env Heal A , vol.64 , pp. 213-222
    • Skrzydlewska, E.1    Stankiewicz, A.2
  • 93
    • 0024399787 scopus 로고
    • Quantitative determination of water- and lipid-soluble antioxidants in neoplastic and non-neoplastic human breast tissue.
    • Langemann, H., Torhorst, J., Kabiersch, A., Krenger, W. & Honegger, C.G. Quantitative determination of water- and lipid-soluble antioxidants in neoplastic and non-neoplastic human breast tissue. Int J Cancer 43, 1169-1173 (1989).
    • (1989) Int J Cancer , vol.43 , pp. 1169-1173
    • Langemann, H.1    Torhorst, J.2    Kabiersch, A.3    Krenger, W.4    Honegger, C.G.5
  • 94
    • 0017362116 scopus 로고
    • Results and analysis of tumour levels of ascorbic acid.
    • Moriarty, M., Mulgrew, S., Malone, J. & O'Connor, M. Results and analysis of tumour levels of ascorbic acid. Irish J Med Sci 146, 74-78 (1977).
    • (1977) Irish J Med Sci , vol.146 , pp. 74-78
    • Moriarty, M.1    Mulgrew, S.2    Malone, J.3    O'Connor, M.4
  • 95
    • 84896737068 scopus 로고    scopus 로고
    • Increased tumour ascorbate is associated with extended disease-free survival and decreased hypoxia-inducible factor-1 activation in human colorectal cancer.
    • Kuiper, C., et al. Increased tumour ascorbate is associated with extended disease-free survival and decreased hypoxia-inducible factor-1 activation in human colorectal cancer. Front Oncol 4(2014).
    • (2014) Front Oncol , vol.4
    • Kuiper, C.1
  • 96
    • 77955037416 scopus 로고    scopus 로고
    • Low ascorbate levels are associated with increased hypoxiainducible factor-1 activity and an aggressive tumor phenotype in endometrial cancer
    • Kuiper, C., et al. Low ascorbate levels are associated with increased hypoxiainducible factor-1 activity and an aggressive tumor phenotype in endometrial cancer. Cancer Res 70, 5749-5758 (2010).
    • (2010) Cancer Res , vol.70 , pp. 5749-5758
    • Kuiper, C.1
  • 97
    • 84915799201 scopus 로고    scopus 로고
    • SVCT-2 in breast cancer acts as an indicator for L-ascorbate treatment.
    • Hong, S.-W., et al. SVCT-2 in breast cancer acts as an indicator for L-ascorbate treatment. Oncogene (2012).
    • (2012) Oncogene
    • Hong, S.-W.1
  • 98
    • 1842435160 scopus 로고    scopus 로고
    • Vitamin C pharmacokinetics: implications for oral and intravenous use
    • Padayatty, S.J., et al. Vitamin C pharmacokinetics: implications for oral and intravenous use. Ann Intern Med 140, 533-537 (2004).
    • (2004) Ann Intern Med , vol.140 , pp. 533-537
    • Padayatty, S.J.1
  • 99
    • 33847051180 scopus 로고    scopus 로고
    • Modulation of hypoxia-inducible factor-1 alpha in cultured primary cells by intracellular ascorbate.
    • Vissers, M.C.M., 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 Rad Biol Med 42, 765-772 (2007).
    • (2007) Free Rad Biol Med , vol.42 , pp. 765-772
    • Vissers, M.C.M.1    Gunningham, S.P.2    Morrison, M.J.3    Dachs, G.U.4    Currie, M.J.5
  • 100
    • 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 63, 1764-1768 (2003).
    • (2003) Cancer Res , vol.63 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3    Ratcliffe, P.J.4
  • 101
    • 69149090945 scopus 로고    scopus 로고
    • Cobalt-induced oxidant stress in cultured endothelial cells: prevention by ascorbate in relation to HIF-1a.
    • Qiao, H., Li, L., Qu, Z.-c. & May, J.M. Cobalt-induced oxidant stress in cultured endothelial cells: prevention by ascorbate in relation to HIF-1a. Biofactors 35, 306-313 (2009).
    • (2009) Biofactors , vol.35 , pp. 306-313
    • Qiao, H.1    Li, L.2    Qu, Z.-c.3    May, J.M.4
  • 102
    • 34548257176 scopus 로고    scopus 로고
    • HIF-dependent antitumorigenic effects of antioxidants in vivo
    • Gao, P., et al. HIF-dependent antitumorigenic effects of antioxidants in vivo. Cancer Cell 12, 230-238 (2007).
    • (2007) Cancer Cell , vol.12 , pp. 230-238
    • Gao, P.1
  • 103
    • 73049112178 scopus 로고    scopus 로고
    • Vitamin C enhances the generation of mouse and human induced pluripotent stem cells
    • Esteban, M.A., et al. Vitamin C enhances the generation of mouse and human induced pluripotent stem cells. Cell Stem Cell 6, 71-79 (2010).
    • (2010) Cell Stem Cell , vol.6 , pp. 71-79
    • Esteban, M.A.1
  • 104
    • 82755187396 scopus 로고    scopus 로고
    • The histone demethylases Jhdm1a/1b enhance somatic cell reprogramming in a vitamin-C-dependent manner
    • Wang, T., et al. The histone demethylases Jhdm1a/1b enhance somatic cell reprogramming in a vitamin-C-dependent manner. Cell Stem Cell 9, 575-587 (2011).
    • (2011) Cell Stem Cell , vol.9 , pp. 575-587
    • Wang, T.1
  • 105
    • 0006171777 scopus 로고
    • Supplemental ascorbate in the supportive treatment of cancer: prolongation of survival times in terminal human cancer.
    • Cameron, E. & Pauling, L. Supplemental ascorbate in the supportive treatment of cancer: prolongation of survival times in terminal human cancer. Proc Natl Acad Sci USA 73, 3685-3689 (1976).
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 3685-3689
    • Cameron, E.1    Pauling, L.2
  • 106
    • 0012375577 scopus 로고
    • Supplemental ascorbate in the supportive treatment of cancer: reevaluation of prolongation of survival times in terminal human cancer.
    • Cameron, E. & Pauling, L. Supplemental ascorbate in the supportive treatment of cancer: reevaluation of prolongation of survival times in terminal human cancer. Proc Natl Acad Sci USA 75, 4538-4542 (1978).
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4538-4542
    • Cameron, E.1    Pauling, L.2
  • 107
    • 0018669229 scopus 로고
    • Failure of high-dose vitamin C (ascorbic acid) therapy to benefit patients with advanced cancer
    • Creagan, E.T., et al. Failure of high-dose vitamin C (ascorbic acid) therapy to benefit patients with advanced cancer. N Engl J Med 301, 687-690 (1979).
    • (1979) N Engl J Med , vol.301 , pp. 687-690
    • Creagan, E.T.1
  • 108
    • 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 doubleblind comparison.
    • Moertel, C.G., et al. High-dose vitamin C versus placebo in the treatment of patients with advanced cancer who have had no prior chemotherapy. A randomized doubleblind comparison. N Engl J Med 312, 137-141 (1985).
    • (1985) N Engl J Med , vol.312 , pp. 137-141
    • Moertel, C.G.1
  • 109
    • 79960648126 scopus 로고    scopus 로고
    • Prostate imaging modalities that can be used for complementary and alternative medicine clinical studies
    • Dusing, R.W., et al. Prostate imaging modalities that can be used for complementary and alternative medicine clinical studies. Urol Clin N Am 38, 343-357 (2011).
    • (2011) Urol Clin N Am , vol.38 , pp. 343-357
    • Dusing, R.W.1
  • 110
    • 33645555541 scopus 로고    scopus 로고
    • Intravenously administered vitamin C as cancer therapy: three cases
    • Padayatty, S.J., et al. Intravenously administered vitamin C as cancer therapy: three cases. CMAJ 174, 937-942 (2006).
    • (2006) CMAJ , vol.174 , pp. 937-942
    • Padayatty, S.J.1
  • 111
    • 54949089044 scopus 로고    scopus 로고
    • Phase I clinical trial of i.v ascorbic acid in advanced malignancy.
    • Hoffer, L.J., et al. Phase I clinical trial of i.v. ascorbic acid in advanced malignancy. Ann Oncol 19, 1969-1974 (2008).
    • (2008) Ann Oncol , vol.19 , pp. 1969-1974
    • Hoffer, L.J.1
  • 112
    • 33750946406 scopus 로고    scopus 로고
    • A pilot clinical study of continuous intravenous ascorbate in terminal cancer patients
    • Riordan, H.D., et al. A pilot clinical study of continuous intravenous ascorbate in terminal cancer patients. P R Health Sci J 24, 269-276 (2005).
    • (2005) P R Health Sci J , vol.24 , pp. 269-276
    • Riordan, H.D.1
  • 113
    • 77955349971 scopus 로고    scopus 로고
    • Vitamin C: intravenous use by complementary and alternative medicine practitioners and adverse effects
    • Padayatty, S.J., et al. Vitamin C: intravenous use by complementary and alternative medicine practitioners and adverse effects. Plos One 5, e11414 (2010).
    • (2010) Plos One , vol.5
    • Padayatty, S.J.1
  • 114
    • 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., 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 102, 13604-13609 (2005).
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13604-13609
    • Chen, Q.1
  • 115
    • 34547429599 scopus 로고    scopus 로고
    • Ascorbate in pharmacologic concentrations selectively generates ascorbate radical and hydrogen peroxide in extracellular fluid in vivo
    • Chen, Q., et al. Ascorbate in pharmacologic concentrations selectively generates ascorbate radical and hydrogen peroxide in extracellular fluid in vivo. Proc Natl Acad Sci USA 104, 8749-8754 (2007).
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8749-8754
    • Chen, Q.1
  • 116
    • 84860475014 scopus 로고    scopus 로고
    • Antiproliferative effect of ascorbic acid is associated with the inhibition of genes necessary to cell cycle progression
    • Belin, S., et al. Antiproliferative effect of ascorbic acid is associated with the inhibition of genes necessary to cell cycle progression. Plos One 4, e4409 (2009).
    • (2009) Plos One , vol.4 , pp. e4409
    • Belin, S.1
  • 117
    • 84855541345 scopus 로고    scopus 로고
    • Ascorbate depletion increases growth and metastasis of melanoma cells in vitamin C deficient mice
    • Cha, J., et al. Ascorbate depletion increases growth and metastasis of melanoma cells in vitamin C deficient mice. Exp Oncol 33, 226-230 (2011).
    • (2011) Exp Oncol , vol.33 , pp. 226-230
    • Cha, J.1
  • 118
    • 81255200577 scopus 로고    scopus 로고
    • Effects of ascorbic acid on carcinogenicity and acute toxicity of nickel subsulfide, and on tumor transplants growth in gulonolactone oxidase knockout mice and wild-type C57BL mice
    • Kasprzak, K.S., et al. Effects of ascorbic acid on carcinogenicity and acute toxicity of nickel subsulfide, and on tumor transplants growth in gulonolactone oxidase knockout mice and wild-type C57BL mice. Toxicol Appl Pharmacol 257, 32-37 (2011).
    • (2011) Toxicol Appl Pharmacol , vol.257 , pp. 32-37
    • Kasprzak, K.S.1
  • 119
    • 84867335373 scopus 로고    scopus 로고
    • Enhanced antitumor activity of vitamin C via p53 in cancer cells
    • Kim, J., et al. Enhanced antitumor activity of vitamin C via p53 in cancer cells. Free Rad Biol Med 53, 1607-1615 (2012).
    • (2012) Free Rad Biol Med , vol.53 , pp. 1607-1615
    • Kim, J.1
  • 120
    • 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 Rad Biol Med 47, 32-40 (2009).
    • (2009) Free Rad Biol Med , vol.47 , pp. 32-40
    • Verrax, J.1    Calderon, P.B.2
  • 121
    • 49649115940 scopus 로고    scopus 로고
    • Pharmacologic doses of ascorbate act as a prooxidant and decrease growth of aggressive tumor xenografts in mice
    • Chen, Q., et al. Pharmacologic doses of ascorbate act as a prooxidant and decrease growth of aggressive tumor xenografts in mice. Proc Natl Acad Sci USA 105, 11105-11109 (2008).
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11105-11109
    • Chen, Q.1
  • 122
    • 84873683033 scopus 로고    scopus 로고
    • Ascorbate supplementation inhibits growth and metastasis of B16FO melanoma and 4T1 breast cancer cells in vitamin C-deficient mice
    • Cha, J., et al. Ascorbate supplementation inhibits growth and metastasis of B16FO melanoma and 4T1 breast cancer cells in vitamin C-deficient mice. Int J Oncol 42, 55-64 (2013).
    • (2013) Int J Oncol , vol.42 , pp. 55-64
    • Cha, J.1
  • 123
    • 79958191830 scopus 로고    scopus 로고
    • Hypoxia-mediated drug resistance: Novel insights on the functional interaction of HIFs and cell death pathways.
    • Rohwer, N. & Cramer, T. Hypoxia-mediated drug resistance: Novel insights on the functional interaction of HIFs and cell death pathways. Drug Resist Update 14, 191-201 (2011).
    • (2011) Drug Resist Update , vol.14 , pp. 191-201
    • Rohwer, N.1    Cramer, T.2
  • 124
    • 2442501565 scopus 로고    scopus 로고
    • Ascorbic acid suppresses druginduced apoptosis in human colon cancer cells by scavenging mitochondrial superoxide anions.
    • Wenzel, U., Nickel, A., Kuntz, S. & Daniel, H. Ascorbic acid suppresses druginduced apoptosis in human colon cancer cells by scavenging mitochondrial superoxide anions. Carcinogenesis 25, 703-712 (2004).
    • (2004) Carcinogenesis , vol.25 , pp. 703-712
    • Wenzel, U.1    Nickel, A.2    Kuntz, S.3    Daniel, H.4
  • 125
    • 79955603438 scopus 로고    scopus 로고
    • Pharmacologic ascorbate synergizes with gemcitabine in preclinical models of pancreatic cancer
    • Espey, M.G., et al. Pharmacologic ascorbate synergizes with gemcitabine in preclinical models of pancreatic cancer. Free Rad Biol Med 50, 1610-1619 (2011).
    • (2011) Free Rad Biol Med , vol.50 , pp. 1610-1619
    • Espey, M.G.1
  • 126
    • 79955550511 scopus 로고    scopus 로고
    • Ascorbate exerts anti-proliferative effects through cell cycle inhibition and sensitizes tumor cells towards cytostatic drugs
    • Frömberg, A., et al. Ascorbate exerts anti-proliferative effects through cell cycle inhibition and sensitizes tumor cells towards cytostatic drugs. Cancer Chemoth Pharm 67, 1157-1166 (2011).
    • (2011) Cancer Chemoth Pharm , vol.67 , pp. 1157-1166
    • Frömberg, A.1
  • 127
    • 84855858767 scopus 로고    scopus 로고
    • Phase I evaluation of intravenous ascorbic acid in combination with gemcitabine and erlotinib in patients with metastatic pancreatic cancer
    • Monti, D.A., et al. Phase I evaluation of intravenous ascorbic acid in combination with gemcitabine and erlotinib in patients with metastatic pancreatic cancer. Plos One 7, e29794 (2012).
    • (2012) Plos One , vol.7
    • Monti, D.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.