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Volumn 66, Issue 5, 2006, Pages 2749-2756

Effects of transferrin receptor blockade on cancer cell proliferation and hypoxia-inducible factor function and their differential regulation by ascorbate

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; CELL SURFACE RECEPTOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; IRON; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY A27.15; MONOCLONAL ANTIBODY E2.3; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 33645066360     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-3857     Document Type: Article
Times cited : (66)

References (52)
  • 1
    • 0036359548 scopus 로고    scopus 로고
    • Hypoxia - A key regulatory factor in tumour growth
    • Harris AL. Hypoxia - a key regulatory factor in tumour growth. Nat Rev Cancer 2002;2:38-47.
    • (2002) Nat Rev Cancer , vol.2 , pp. 38-47
    • Harris, A.L.1
  • 4
    • 0037449811 scopus 로고    scopus 로고
    • Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1α
    • Elkins JM, Hewitson KS, McNeill LA, et al. Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1α. J Biol Chem 2003;278:1802-6.
    • (2003) J Biol Chem , vol.278 , pp. 1802-1806
    • Elkins, J.M.1    Hewitson, K.S.2    McNeill, L.A.3
  • 5
    • 3843095197 scopus 로고    scopus 로고
    • HIF-1's relationship to oxygen: Simple yet sophisticated
    • Maxwell PH. HIF-1's relationship to oxygen: simple yet sophisticated. Cell Cycle 2004;3:156-9.
    • (2004) Cell Cycle , vol.3 , pp. 156-159
    • Maxwell, P.H.1
  • 6
    • 0029833706 scopus 로고    scopus 로고
    • The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase
    • Cooper CE, Lynagh GR, Hoyes KP, et al. The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase. J Biol Chem 1996;271:20291-9.
    • (1996) J Biol Chem , vol.271 , pp. 20291-20299
    • Cooper, C.E.1    Lynagh, G.R.2    Hoyes, K.P.3
  • 7
    • 7244239197 scopus 로고    scopus 로고
    • Iron chelators with high antiproliferative activity up-regulate the expression of a growth inhibitory and metastasis suppressor gene: A link between iron metabolism and proliferation
    • Le NT, Richardson DR. Iron chelators with high antiproliferative activity up-regulate the expression of a growth inhibitory and metastasis suppressor gene: a link between iron metabolism and proliferation. Blood 2004;104:2967-75.
    • (2004) Blood , vol.104 , pp. 2967-2975
    • Le, N.T.1    Richardson, D.R.2
  • 8
    • 0024819020 scopus 로고
    • Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA
    • Casey JL, Koeller DM, Ramin VC, et al. Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA. EMBO J 1989;8:3693-9.
    • (1989) EMBO J , vol.8 , pp. 3693-3699
    • Casey, J.L.1    Koeller, D.M.2    Ramin, V.C.3
  • 9
    • 0022836508 scopus 로고
    • Structure and function of transferrin receptors and their relationship to cell growth
    • Trowbridge IS, Shackelford DA. Structure and function of transferrin receptors and their relationship to cell growth. Biochem Soc Symp 1986;51:117-29.
    • (1986) Biochem Soc Symp , vol.51 , pp. 117-129
    • Trowbridge, I.S.1    Shackelford, D.A.2
  • 10
    • 0020597630 scopus 로고
    • Transferrin receptors in human tissues: Their distribution and possible clinical relevance
    • Gatter KC, Brown G, Trowbridge IS, et al. Transferrin receptors in human tissues: their distribution and possible clinical relevance. J Clin Pathol 1983;36:539-45.
    • (1983) J Clin Pathol , vol.36 , pp. 539-545
    • Gatter, K.C.1    Brown, G.2    Trowbridge, I.S.3
  • 11
    • 0019506192 scopus 로고
    • Demonstration of the transferrin receptor in human breast cancer tissue. Potential marker for identifying dividing cells
    • Shindelman JE, Ortmeyer AE, Sussman HH. Demonstration of the transferrin receptor in human breast cancer tissue. Potential marker for identifying dividing cells. Int J Cancer 1981;27:329-34.
    • (1981) Int J Cancer , vol.27 , pp. 329-334
    • Shindelman, J.E.1    Ortmeyer, A.E.2    Sussman, H.H.3
  • 12
    • 0025057114 scopus 로고
    • Elevated transferrin receptor content in human prostate cancer cell lines assessed in vitro and in vivo
    • Keer HN, Kozlowski JM, Tsai YC, et al. Elevated transferrin receptor content in human prostate cancer cell lines assessed in vitro and in vivo. J Urol 1990;143:381-5.
    • (1990) J Urol , vol.143 , pp. 381-385
    • Keer, H.N.1    Kozlowski, J.M.2    Tsai, Y.C.3
  • 13
    • 0036678172 scopus 로고    scopus 로고
    • An anti-transferrin receptor-avidin fusion protein exhibits both strong proapoptotic activity and the ability to deliver various molecules into cancer cells
    • Ng PP, Dela Cruz JS, Sorour DN, et al. An anti-transferrin receptor-avidin fusion protein exhibits both strong proapoptotic activity and the ability to deliver various molecules into cancer cells. Proc Natl Acad Sci U S A 2002;99:10706-11.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10706-10711
    • Ng, P.P.1    Dela Cruz, J.S.2    Sorour, D.N.3
  • 14
    • 0019833023 scopus 로고
    • Anti-transferrin receptor monoclonal antibody and toxin-antibody conjugates affect growth of human tumour cells
    • Trowbridge IS, Domingo DL. Anti-transferrin receptor monoclonal antibody and toxin-antibody conjugates affect growth of human tumour cells. Nature 1981;294:171-3.
    • (1981) Nature , vol.294 , pp. 171-173
    • Trowbridge, I.S.1    Domingo, D.L.2
  • 15
    • 0021891360 scopus 로고
    • Transferrin receptor as a target for antibody-drug conjugates
    • Domingo DL, Trowbridge IS. Transferrin receptor as a target for antibody-drug conjugates. Methods Enzymol 1985;112:238-47.
    • (1985) Methods Enzymol , vol.112 , pp. 238-247
    • Domingo, D.L.1    Trowbridge, I.S.2
  • 16
    • 0023125888 scopus 로고
    • Effects of monoclonal antibodies that block transferrin receptor function on the in vivo growth of a syngeneic marine leukemia
    • Sauvage CA, Mendelsohn JC, Lesley JF, et al. Effects of monoclonal antibodies that block transferrin receptor function on the in vivo growth of a syngeneic marine leukemia. Cancer Res 1987;47:747-53.
    • (1987) Cancer Res , vol.47 , pp. 747-753
    • Sauvage, C.A.1    Mendelsohn, J.C.2    Lesley, J.F.3
  • 17
    • 0025005475 scopus 로고
    • Combinations of anti-transferrin receptor monoclonal antibodies inhibit human tumor cell growth in vitro and in vivo: Evidence for synergistic antiproliferative effects
    • White S, Taetle R, Seligman PA, et al. Combinations of anti-transferrin receptor monoclonal antibodies inhibit human tumor cell growth in vitro and in vivo: evidence for synergistic antiproliferative effects. Cancer Res 1990;50:6295-301.
    • (1990) Cancer Res , vol.50 , pp. 6295-6301
    • White, S.1    Taetle, R.2    Seligman, P.A.3
  • 18
    • 0023693103 scopus 로고
    • Characterization of the human transferrin receptor produced in a baculovirus expression system
    • Domingo DL, Trowbridge IS. Characterization of the human transferrin receptor produced in a baculovirus expression system. J Biol Chem 1988;263:13386-92.
    • (1988) J Biol Chem , vol.263 , pp. 13386-13392
    • Domingo, D.L.1    Trowbridge, I.S.2
  • 19
    • 0028111173 scopus 로고
    • Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment
    • Pastorek J, Pastorekova S, Callebaut I, et al. Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment. Oncogene 1994;9:2877-8.
    • (1994) Oncogene , vol.9 , pp. 2877-2878
    • Pastorek, J.1    Pastorekova, S.2    Callebaut, I.3
  • 20
    • 0037902097 scopus 로고    scopus 로고
    • Fluorescence measurements of the labile iron pool of sickle erythrocytes
    • Darbari D, Loyevsky M, Gordeuk V, et al. Fluorescence measurements of the labile iron pool of sickle erythrocytes. Blood 2003;102:357-64.
    • (2003) Blood , vol.102 , pp. 357-364
    • Darbari, D.1    Loyevsky, M.2    Gordeuk, V.3
  • 21
    • 0031570288 scopus 로고    scopus 로고
    • Fluorescence analysis of the labile iron pool of mammalian cells
    • Epsztejn S, Kakhlon O, Glickstein H, et al. Fluorescence analysis of the labile iron pool of mammalian cells. Anal Biochem 1997;248:31-40.
    • (1997) Anal Biochem , vol.248 , pp. 31-40
    • Epsztejn, S.1    Kakhlon, O.2    Glickstein, H.3
  • 22
    • 0027136260 scopus 로고
    • Desferrioxamine induces erythropoietin gene expression and hypoxia-inducible factor 1 DNA-binding activity: Implications for models of hypoxia signal transduction
    • Wang GL, Semenza GL. Desferrioxamine induces erythropoietin gene expression and hypoxia-inducible factor 1 DNA-binding activity: implications for models of hypoxia signal transduction. Blood 1993;82:3610-5.
    • (1993) Blood , vol.82 , pp. 3610-3615
    • Wang, G.L.1    Semenza, G.L.2
  • 23
    • 0000655498 scopus 로고    scopus 로고
    • Identification of a hypoxia response element in the transferrin receptor gene
    • Lok CN, Ponka P. Identification of a hypoxia response element in the transferrin receptor gene. J Biol Chem 1999;274:24147-52.
    • (1999) J Biol Chem , vol.274 , pp. 24147-24152
    • Lok, C.N.1    Ponka, P.2
  • 24
    • 0037446983 scopus 로고    scopus 로고
    • Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells
    • Knowles HJ, Raval RR, Harris AL, et al. Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells. Cancer Res 2003;63:1764-8.
    • (2003) Cancer Res , vol.63 , pp. 1764-1768
    • Knowles, H.J.1    Raval, R.R.2    Harris, A.L.3
  • 25
    • 0025126032 scopus 로고
    • Effects of a single course of deferoxamine in neuroblastoma patients
    • Donfrancesco A, Deb G, Dominici C, et al. Effects of a single course of deferoxamine in neuroblastoma patients. Cancer Res 1990;50:4929-30.
    • (1990) Cancer Res , vol.50 , pp. 4929-4930
    • Donfrancesco, A.1    Deb, G.2    Dominici, C.3
  • 26
    • 0025833784 scopus 로고
    • Continuous infusion gallium nitrate for patients with advanced refractory urothelial tract tumors
    • Seidman AD, Scher HI, Heinemann MH, et al. Continuous infusion gallium nitrate for patients with advanced refractory urothelial tract tumors. Cancer 1991;68:2561-5.
    • (1991) Cancer , vol.68 , pp. 2561-2565
    • Seidman, A.D.1    Scher, H.I.2    Heinemann, M.H.3
  • 28
    • 2942724321 scopus 로고    scopus 로고
    • Desferoxamine (DFO)-mediated iron chelation: Rationale for a novel approach to therapy for brain cancer
    • Dayani PN, Bishop MC, Black K, et al. Desferoxamine (DFO)-mediated iron chelation: rationale for a novel approach to therapy for brain cancer. J Neurooncol 2004;67:367-77.
    • (2004) J Neurooncol , vol.67 , pp. 367-377
    • Dayani, P.N.1    Bishop, M.C.2    Black, K.3
  • 29
    • 0031024826 scopus 로고    scopus 로고
    • Iron deprivation and cancer: A view beginning with studies of monoclonal antibodies against the transferrin receptor
    • Kemp JD. Iron deprivation and cancer: a view beginning with studies of monoclonal antibodies against the transferrin receptor. Histol Histopathol 1997;12:291-6.
    • (1997) Histol Histopathol , vol.12 , pp. 291-296
    • Kemp, J.D.1
  • 30
    • 0023701518 scopus 로고
    • Transferrin receptor as a potential therapeutic target
    • Trowbridge IS. Transferrin receptor as a potential therapeutic target. Prog Allergy 1988;45:121-46.
    • (1988) Prog Allergy , vol.45 , pp. 121-146
    • Trowbridge, I.S.1
  • 31
    • 10744221783 scopus 로고    scopus 로고
    • A neutralizing monoclonal antibody (mAb A24) directed against the transferrin receptor induces apoptosis of tumor T lymphocytes from ATL patients
    • Moura IC, Lepelletier Y, Arnulf B, et al. A neutralizing monoclonal antibody (mAb A24) directed against the transferrin receptor induces apoptosis of tumor T lymphocytes from ATL patients. Blood 2004;103:1838-45.
    • (2004) Blood , vol.103 , pp. 1838-1845
    • Moura, I.C.1    Lepelletier, Y.2    Arnulf, B.3
  • 32
    • 6444230040 scopus 로고    scopus 로고
    • Identification of small molecule inhibitors that distinguish between non-transferrin bound iron uptake and transferrin-mediated iron transport
    • Brown JX, Buckett PD, Wessling-Resnick M. Identification of small molecule inhibitors that distinguish between non-transferrin bound iron uptake and transferrin-mediated iron transport. Chem Biol 2004;11:407-16.
    • (2004) Chem Biol , vol.11 , pp. 407-416
    • Brown, J.X.1    Buckett, P.D.2    Wessling-Resnick, M.3
  • 33
    • 0036238011 scopus 로고    scopus 로고
    • Transferrin/transferrin receptor-mediated drug delivery
    • Li H, Qian ZM. Transferrin/transferrin receptor-mediated drug delivery. Med Res Rev 2002;22:225-50.
    • (2002) Med Res Rev , vol.22 , pp. 225-250
    • Li, H.1    Qian, Z.M.2
  • 34
    • 0029147468 scopus 로고
    • Differing sensitivity of non-hematopoietic human tumors to synergistic anti-transferrin receptor monoclonal antibodies and deferoxamine in vitro
    • Kovar J, Naumann PW, Stewart BC, et al. Differing sensitivity of non-hematopoietic human tumors to synergistic anti-transferrin receptor monoclonal antibodies and deferoxamine in vitro. Pathobiology 1995;63:65-70.
    • (1995) Pathobiology , vol.63 , pp. 65-70
    • Kovar, J.1    Naumann, P.W.2    Stewart, B.C.3
  • 35
    • 0018850974 scopus 로고
    • Transferrin and transferrin receptors in carcinoma of the breast
    • Faulk WP, Hsi BL, Stevens PJ. Transferrin and transferrin receptors in carcinoma of the breast. Lancet 1980;2:390-2.
    • (1980) Lancet , vol.2 , pp. 390-392
    • Faulk, W.P.1    Hsi, B.L.2    Stevens, P.J.3
  • 36
    • 0035171325 scopus 로고    scopus 로고
    • Desferri-exochelin induces death by apoptosis in human breast cancer cells but does not kill normal breast cells
    • Pahl PM, Horwitz MA, Horwitz KB, et al. Desferri-exochelin induces death by apoptosis in human breast cancer cells but does not kill normal breast cells. Breast Cancer Res Treat 2001;69:69-79.
    • (2001) Breast Cancer Res Treat , vol.69 , pp. 69-79
    • Pahl, P.M.1    Horwitz, M.A.2    Horwitz, K.B.3
  • 37
    • 0034903090 scopus 로고    scopus 로고
    • Inhibition of growth of human breast carcinoma cells by an antisense oligonucleotide targeted to the transferrin receptor gene
    • Yang DC, Jiang XP, Elliott RL, et al. Inhibition of growth of human breast carcinoma cells by an antisense oligonucleotide targeted to the transferrin receptor gene. Anticancer Res 2001;21:1777-87.
    • (2001) Anticancer Res , vol.21 , pp. 1777-1787
    • Yang, D.C.1    Jiang, X.P.2    Elliott, R.L.3
  • 38
    • 0025832161 scopus 로고
    • Structure-function analysis of the human transferrin receptor: Effects of anti-receptor monoclonal antibodies on tumor growth
    • Trowbridge IS, Collawn J, Jing S, et al. Structure-function analysis of the human transferrin receptor: effects of anti-receptor monoclonal antibodies on tumor growth. Curr Stud Hematol Blood Transfus 1991;58:139-47.
    • (1991) Curr Stud Hematol Blood Transfus , vol.58 , pp. 139-147
    • Trowbridge, I.S.1    Collawn, J.2    Jing, S.3
  • 39
    • 0029742532 scopus 로고    scopus 로고
    • Upregulation of vascular endothelial growth factor production by iron chelators
    • Beerepoot LV, Shima DT, Kuroki M, et al. Upregulation of vascular endothelial growth factor production by iron chelators. Cancer Res 1996;56:3747-51.
    • (1996) Cancer Res , vol.56 , pp. 3747-3751
    • Beerepoot, L.V.1    Shima, D.T.2    Kuroki, M.3
  • 40
    • 0037054928 scopus 로고    scopus 로고
    • Desferrioxamine enhances AIDS-associated Kaposi's sarcoma tumor development in a xenograft model
    • Simonart T, Boelaert JR, Andrei G, et al. Desferrioxamine enhances AIDS-associated Kaposi's sarcoma tumor development in a xenograft model. Int J Cancer 2002;100:140-3.
    • (2002) Int J Cancer , vol.100 , pp. 140-143
    • Simonart, T.1    Boelaert, J.R.2    Andrei, G.3
  • 41
    • 0037986658 scopus 로고    scopus 로고
    • Iron chelators as anti-neoplastic agents: Current developments and promise of the PIH class of chelators
    • Lovejoy DB, Richardson DR. Iron chelators as anti-neoplastic agents: current developments and promise of the PIH class of chelators. Curr Med Chem 2003;10:1035-49.
    • (2003) Curr Med Chem , vol.10 , pp. 1035-1049
    • Lovejoy, D.B.1    Richardson, D.R.2
  • 42
    • 0028891974 scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents
    • Richardson DR, Tran EH, Ponka P. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents. Blood 1995;86:4295-43065.
    • (1995) Blood , vol.86 , pp. 4295-43065
    • Richardson, D.R.1    Tran, E.H.2    Ponka, P.3
  • 43
    • 0024920255 scopus 로고
    • Iron chelators of the pyridoxal isonicotinoyl hydrazone class. III. Formation constants with calcium(II), magnesium(II) and zinc(II)
    • Richardson DR, Hefter GT, May PM, et al. Iron chelators of the pyridoxal isonicotinoyl hydrazone class. III. Formation constants with calcium(II), magnesium(II) and zinc(II). Biol Methods 1989;2:161-7.
    • (1989) Biol Methods , vol.2 , pp. 161-167
    • Richardson, D.R.1    Hefter, G.T.2    May, P.M.3
  • 44
    • 0042563157 scopus 로고    scopus 로고
    • Phase I and pharmacodynamic study of Triapine, a novel ribonucleotide reductase inhibitor, in patients with advanced leukemia
    • Giles FJ, Fracasso PM, Kantarjian HM, et al. Phase I and pharmacodynamic study of Triapine, a novel ribonucleotide reductase inhibitor, in patients with advanced leukemia. Leuk Res 2003;27:1077-83.
    • (2003) Leuk Res , vol.27 , pp. 1077-1083
    • Giles, F.J.1    Fracasso, P.M.2    Kantarjian, H.M.3
  • 45
    • 2442530651 scopus 로고    scopus 로고
    • Competing pathways of iron chelation: Angiogenesis or anti-tumor activity: Targeting different molecules to induce specific effects
    • Le NT, Richardson DR. Competing pathways of iron chelation: angiogenesis or anti-tumor activity: targeting different molecules to induce specific effects. Int J Cancer 2004;110:468-9.
    • (2004) Int J Cancer , vol.110 , pp. 468-469
    • Le, N.T.1    Richardson, D.R.2
  • 46
    • 0033984094 scopus 로고    scopus 로고
    • BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites
    • Ray R, Chen G, Vande Velde C, et al. BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites. J Biol Chem 2000;275:1439-48.
    • (2000) J Biol Chem , vol.275 , pp. 1439-1448
    • Ray, R.1    Chen, G.2    Vande Velde, C.3
  • 47
    • 4344699403 scopus 로고    scopus 로고
    • Role of carbonic anhydrase IX in human tumor cell growth, survival, and invasion
    • Robertson N, Potter C, Harris AL. Role of carbonic anhydrase IX in human tumor cell growth, survival, and invasion. Cancer Res 2004;64:6160-5.
    • (2004) Cancer Res , vol.64 , pp. 6160-6165
    • Robertson, N.1    Potter, C.2    Harris, A.L.3
  • 48
    • 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 SP, 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;704:326-32.
    • (1982) Biochim Biophys Acta , vol.704 , pp. 326-332
    • De Jong, L.1    Albracht, S.P.2    Kemp, A.3
  • 49
    • 0021329173 scopus 로고
    • Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase
    • Myllyla R, Majamaa K, Gunzler V, et al. Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J Biol Chem 1984;259:5403-5.
    • (1984) J Biol Chem , vol.259 , pp. 5403-5405
    • Myllyla, R.1    Majamaa, K.2    Gunzler, V.3
  • 50
    • 0036151286 scopus 로고    scopus 로고
    • Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana
    • Wilmouth RC, Turnbull JJ, Welford RW, et al. Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana. Structure (Camb) 2002;10:93-103.
    • (2002) Structure (Camb) , vol.10 , pp. 93-103
    • Wilmouth, R.C.1    Turnbull, J.J.2    Welford, R.W.3
  • 51
    • 20144380606 scopus 로고    scopus 로고
    • Sodium ascorbate (vitamin C) induces apoptosis in melanoma cells via the down-regulation of transferrin receptor dependent iron uptake
    • Kang JS, Cho D, Kim YI, et al. Sodium ascorbate (vitamin C) induces apoptosis in melanoma cells via the down-regulation of transferrin receptor dependent iron uptake. J Cell Physiol 2005;204:192-7.
    • (2005) J Cell Physiol , vol.204 , pp. 192-197
    • Kang, J.S.1    Cho, D.2    Kim, Y.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.