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Volumn 75, Issue 10-11, 1997, Pages 1164-1180

Potential of iron chelators as effective antiproliferative agents

Author keywords

Cancer cells; Iron; Iron chelators; Proliferation

Indexed keywords

1,2 DIETHYL 3 HYDROXY 4 PYRIDONE; CHELATING AGENT; DEFERIPRONE; DEFEROXAMINE; IRON; PARABACTIN; PICOLINIC ACID; PYRIDOXAL ISONICOTINOYLHYDRAZONE; THIOSEMICARBAZONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0031436976     PISSN: 00084212     EISSN: None     Source Type: Journal    
DOI: 10.1139/y97-156     Document Type: Review
Times cited : (68)

References (158)
  • 1
    • 0006264020 scopus 로고
    • Some physiochemical aspects of iron metabolism
    • Elsevier, North Holland, Amsterdam
    • Aisen, P. 1977. Some physiochemical aspects of iron metabolism. In Iron metabolism. Ciba Foundation Symposium 51, New Series. Elsevier, North Holland, Amsterdam, pp. 1-17.
    • (1977) Iron Metabolism. Ciba Foundation Symposium 51, New Series , pp. 1-17
    • Aisen, P.1
  • 2
    • 0027930931 scopus 로고
    • Iron at the cell surface controls DNA synthesis in CC1 39 cells
    • Alcain, F.J., Löw, H., and Crane, F.L. 1994a. Iron at the cell surface controls DNA synthesis in CC1 39 cells. Biochem. Biophys. Res. Commun. 203: 16-21.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 16-21
    • Alcain, F.J.1    Löw, H.2    Crane, F.L.3
  • 3
    • 0027989957 scopus 로고
    • Iron reverses impermeable chelator inhibition of DNA synthesis in CC1 39 cells
    • Alcain, F.J., Löw, H., and Crane, F.L. 1994b. Iron reverses impermeable chelator inhibition of DNA synthesis in CC1 39 cells. Proc. Natl. Acad. Sci. U.S.A. 91: 7903-7906.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7903-7906
    • Alcain, F.J.1    Löw, H.2    Crane, F.L.3
  • 4
    • 0002360572 scopus 로고
    • Structural studies of Fe(III) and Cu(II) complexes of salicylaldehyde benzoyl hydrazone, a synthetic chelating agent exhibiting diverse biological properties
    • Aruffo, A., Murphy, T.B., Johnson, D.K., Rose, N.J., and Schomaker, V. 1982. Structural studies of Fe(III) and Cu(II) complexes of salicylaldehyde benzoyl hydrazone, a synthetic chelating agent exhibiting diverse biological properties. Inorg. Chim. Acta, 67: L25-L27.
    • (1982) Inorg. Chim. Acta , vol.67
    • Aruffo, A.1    Murphy, T.B.2    Johnson, D.K.3    Rose, N.J.4    Schomaker, V.5
  • 5
    • 0022386084 scopus 로고
    • Iron chelation by pyridoxal isonicotinoyl hydrazone and analogues in hepatocytes in culture
    • Baker, E., Vitolo, M.L., and Webb, J.M. 1985. Iron chelation by pyridoxal isonicotinoyl hydrazone and analogues in hepatocytes in culture. Biochem. Pharmacol. 34: 3011-3017.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 3011-3017
    • Baker, E.1    Vitolo, M.L.2    Webb, J.M.3
  • 6
    • 0023763818 scopus 로고
    • Iron metabolism and the effect of iron chelators in rat hepatoma cells
    • Baker, E., Lloyd, D.A., Morgan, E.H., and Yeoh, G.C.T. 1988. Iron metabolism and the effect of iron chelators in rat hepatoma cells. Birth Defects, 23(5B): 89-95.
    • (1988) Birth Defects , vol.23 , Issue.5 B , pp. 89-95
    • Baker, E.1    Lloyd, D.A.2    Morgan, E.H.3    Yeoh, G.C.T.4
  • 7
    • 0026575576 scopus 로고
    • Evaluation of the iron chelation potential of pyridoxal, salicylaldehyde and 2-hydroxy-1-naphthylaldehyde using the hepatocyte in culture
    • Baker, E., Richardson, D.R., Gross, S., and Ponka, P. 1992. Evaluation of the iron chelation potential of pyridoxal, salicylaldehyde and 2-hydroxy-1-naphthylaldehyde using the hepatocyte in culture. Hepatology, 15: 492-501.
    • (1992) Hepatology , vol.15 , pp. 492-501
    • Baker, E.1    Richardson, D.R.2    Gross, S.3    Ponka, P.4
  • 9
    • 0024241764 scopus 로고
    • Deferoxamine inhibition of human neuroblastoma viability and proliferation
    • Becton, D.L., and Bryles, P. 1988. Deferoxamine inhibition of human neuroblastoma viability and proliferation. Cancer Res. 48: 7189-7192.
    • (1988) Cancer Res. , vol.48 , pp. 7189-7192
    • Becton, D.L.1    Bryles, P.2
  • 10
    • 0024343393 scopus 로고
    • Antileukemic effects of desferrioxamine on human myeloid leukemia cell lines
    • Becton, D.L., and Roberts, B. 1989. Antileukemic effects of desferrioxamine on human myeloid leukemia cell lines. Cancer Res. 49: 4809-4812.
    • (1989) Cancer Res. , vol.49 , pp. 4809-4812
    • Becton, D.L.1    Roberts, B.2
  • 11
    • 0029742532 scopus 로고    scopus 로고
    • Up-regulation of vascular endothelial growth factor production by iron chelators
    • Becrepoot, L.V., Shima, D.T., Kuroki, M., Yeo, K.T., and Voest, E.E. 1996. Up-regulation of vascular endothelial growth factor production by iron chelators. Cancer Res. 56: 3747-3751.
    • (1996) Cancer Res. , vol.56 , pp. 3747-3751
    • Becrepoot, L.V.1    Shima, D.T.2    Kuroki, M.3    Yeo, K.T.4    Voest, E.E.5
  • 12
    • 0023605740 scopus 로고
    • Microbial iron chelator-induced cell cycle synchronisation in L1210 cells: Potential in combination chemotherapy
    • Bergeron, R.J., and Ingeno, M.J. 1987. Microbial iron chelator-induced cell cycle synchronisation in L1210 cells: potential in combination chemotherapy. Cancer Res. 47: 6010-6016.
    • (1987) Cancer Res. , vol.47 , pp. 6010-6016
    • Bergeron, R.J.1    Ingeno, M.J.2
  • 13
    • 0014278271 scopus 로고
    • Studies on the mode of action of the copper(II) chelate of 2-keto-3-ethoxybutyraldehyde bis(thiosemicarbazone)
    • Bhuyan, B., and Betz, T. 1968. Studies on the mode of action of the copper(II) chelate of 2-keto-3-ethoxybutyraldehyde bis(thiosemicarbazone). Cancer Res. 28: 758-763.
    • (1968) Cancer Res. , vol.28 , pp. 758-763
    • Bhuyan, B.1    Betz, T.2
  • 14
    • 0023092624 scopus 로고
    • Antineuroblastoma activity of desferrioxamine in human cell lines
    • Blatt, J., and Stitely, S. 1987. Antineuroblastoma activity of desferrioxamine in human cell lines. Cancer Res. 47: 1749-1750.
    • (1987) Cancer Res. , vol.47 , pp. 1749-1750
    • Blatt, J.1    Stitely, S.2
  • 15
    • 0023689207 scopus 로고
    • Mechanism of antineuroblastoma activity of deferoxamine in vitro
    • Blatt, J., Taylor, S.R., and Stitely, S. 1988. Mechanism of antineuroblastoma activity of deferoxamine in vitro. J. Lab. Clin. Med. 112: 433-436.
    • (1988) J. Lab. Clin. Med. , vol.112 , pp. 433-436
    • Blatt, J.1    Taylor, S.R.2    Stitely, S.3
  • 16
    • 0024348430 scopus 로고
    • Comparison of activity of deferoxamine with that of oral iron chelators against human neuroblastoma cell lines
    • Blatt, J., Taylor, S.R., and Kontoghiorghes, G.J. 1989. Comparison of activity of deferoxamine with that of oral iron chelators against human neuroblastoma cell lines. Cancer Res. 49: 2925-2927.
    • (1989) Cancer Res. , vol.49 , pp. 2925-2927
    • Blatt, J.1    Taylor, S.R.2    Kontoghiorghes, G.J.3
  • 17
    • 0022651531 scopus 로고
    • The effect of desferrioxamine on transferrin receptors, the cell cycle and growth rates of human leukemic cells
    • Bomford, A., Isaac, J., Roberts, S., Edwards, A., Young, S., and Williams, R. 1986. The effect of desferrioxamine on transferrin receptors, the cell cycle and growth rates of human leukemic cells. Biochem. J. 236: 243-249.
    • (1986) Biochem. J. , vol.236 , pp. 243-249
    • Bomford, A.1    Isaac, J.2    Roberts, S.3    Edwards, A.4    Young, S.5    Williams, R.6
  • 18
    • 0014003948 scopus 로고
    • Synergistic action of kethoxal bis(thiosemicarbazone) and cupric ions in Sarcoma 180
    • Booth, B., and Sartorelli, A. 1966. Synergistic action of kethoxal bis(thiosemicarbazone) and cupric ions in Sarcoma 180. Nature (London), 210: 104-105.
    • (1966) Nature (London) , vol.210 , pp. 104-105
    • Booth, B.1    Sartorelli, A.2
  • 19
    • 0000844115 scopus 로고
    • Metabolic effects of copper in intact cells: Comparative activity of cupric chloride and kethoxal bis(thiosemicarbazone)
    • Booth, B., and Sartorelli, A. 1967. Metabolic effects of copper in intact cells: comparative activity of cupric chloride and kethoxal bis(thiosemicarbazone). Mol. Pharmacol. 3: 290-302.
    • (1967) Mol. Pharmacol. , vol.3 , pp. 290-302
    • Booth, B.1    Sartorelli, A.2
  • 20
    • 0015155548 scopus 로고
    • Metabolic effects of zinc in intact cells: Comparative studies of zinc chloride and the zinc chelate of kethoxal bis(thiosemicarbazone)
    • Booth, B., Donnelly, T., Zettner, A., and Sartorelli, A. 1971. Metabolic effects of zinc in intact cells: comparative studies of zinc chloride and the zinc chelate of kethoxal bis(thiosemicarbazone). Biochem. Pharmacol. 20: 3109-3118.
    • (1971) Biochem. Pharmacol. , vol.20 , pp. 3109-3118
    • Booth, B.1    Donnelly, T.2    Zettner, A.3    Sartorelli, A.4
  • 21
    • 0022256894 scopus 로고
    • Iron metabolism in K562 erythroleukemia cells
    • Bottomley, S.S., Wolfe, L.C., and Bridges, K.R. 1985. Iron metabolism in K562 erythroleukemia cells. J. Biol. Chem. 260: 6811-6815.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6811-6815
    • Bottomley, S.S.1    Wolfe, L.C.2    Bridges, K.R.3
  • 22
    • 0028834446 scopus 로고
    • Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II)
    • Breuer, W., Epsztejn, S., and Cabantchik, Z.I. 1995. Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II). J. Biol. Chem. 270: 24 207-24 215.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24207-24215
    • Breuer, W.1    Epsztejn, S.2    Cabantchik, Z.I.3
  • 23
    • 0021746936 scopus 로고
    • Effect of iron chelators on the transferrin receptor in K562 cells
    • Bridges, K.R., and Cudkowicz, A. 1984. Effect of iron chelators on the transferrin receptor in K562 cells. J. Biol. Chem. 259: 12 970-12 977.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12970-12977
    • Bridges, K.R.1    Cudkowicz, A.2
  • 24
    • 0021261878 scopus 로고
    • Amplification of N-myc in untreated human neuroblastomas correlates with advanced disease stage
    • Washington, D.C.
    • Brodeur, G.M., Seeger, R.C., Schwab, M., Varmus, H.E., and Bishop, J.M. 1984. Amplification of N-myc in untreated human neuroblastomas correlates with advanced disease stage. Science (Washington, D.C.), 224: 1121-1124.
    • (1984) Science , vol.224 , pp. 1121-1124
    • Brodeur, G.M.1    Seeger, R.C.2    Schwab, M.3    Varmus, H.E.4    Bishop, J.M.5
  • 26
    • 0019888660 scopus 로고
    • Activated bleomycin: A transient complex of drug, iron and oxygen that degrades DNA
    • Burger, R.M., Peisach, J., and Horwitz, S.B. 1981. Activated bleomycin: a transient complex of drug, iron and oxygen that degrades DNA. J. Biol. Chem. 256: 11 636-11 644.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11636-11644
    • Burger, R.M.1    Peisach, J.2    Horwitz, S.B.3
  • 28
    • 0022839492 scopus 로고
    • Effects of different transferrin forms on transferrin receptor expression, iron uptake, and cellular proliferation of human leukemic HL60 cells: Mechanisms responsible for the specific cytotoxicity of transferrin-gallium
    • Chitamber, C.R., and Seligman, P.A. 1986. Effects of different transferrin forms on transferrin receptor expression, iron uptake, and cellular proliferation of human leukemic HL60 cells: mechanisms responsible for the specific cytotoxicity of transferrin-gallium. J. Clin. Invest. 78: 1538-1546.
    • (1986) J. Clin. Invest. , vol.78 , pp. 1538-1546
    • Chitamber, C.R.1    Seligman, P.A.2
  • 29
    • 0029929672 scopus 로고    scopus 로고
    • Hypersensitivity of human testicular tumors to etoposide-induced apoptosis is associated with functional p53 and a high Bax:Bcl-2 ratio
    • Chresta, C.M., Masters, J.R.W., and Hickman, J.A. 1996. Hypersensitivity of human testicular tumors to etoposide-induced apoptosis is associated with functional p53 and a high Bax:Bcl-2 ratio. Cancer Res. 56: 1834-1841.
    • (1996) Cancer Res. , vol.56 , pp. 1834-1841
    • Chresta, C.M.1    Masters, J.R.W.2    Hickman, J.A.3
  • 30
    • 0018831805 scopus 로고
    • Biliary iron excretion in rats following pyridoxal isonicotinoyl hydrazone
    • Cikrt, M., Ponka, P., Necas, E., and Neuwirt, J. 1980. Biliary iron excretion in rats following pyridoxal isonicotinoyl hydrazone. Br. J. Haematol. 45: 275-283.
    • (1980) Br. J. Haematol. , vol.45 , pp. 275-283
    • Cikrt, M.1    Ponka, P.2    Necas, E.3    Neuwirt, J.4
  • 31
    • 0029833706 scopus 로고    scopus 로고
    • The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase
    • Cooper, C.E., Lynagh, G.R., Hoyes, K.P., Hider, R.C., Cammack, R., and Porter, J.B. 1996. The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase. J. Biol. Chem. 271: 20 291-20 299.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20291-20299
    • Cooper, C.E.1    Lynagh, G.R.2    Hoyes, K.P.3    Hider, R.C.4    Cammack, R.5    Porter, J.B.6
  • 38
    • 0026683009 scopus 로고
    • Deferoxamine, cyclophosphamide, etoposide, carboplatin, and thiotepa (D-CECat): A new cytoreductive chelation-chemotherapy regimen in patients with advanced neuroblastoma
    • Donfrancesco, A., Deb, G., Dominici, C., Angioni, A., Caniglia, M., De Sio, L., Fidani, P., Amici, A., and Helson, L. 1992. Deferoxamine, cyclophosphamide, etoposide, carboplatin, and thiotepa (D-CECat): a new cytoreductive chelation-chemotherapy regimen in patients with advanced neuroblastoma. Am. J. Clin. Oncol. 15: 319-322.
    • (1992) Am. J. Clin. Oncol. , vol.15 , pp. 319-322
    • Donfrancesco, A.1    Deb, G.2    Dominici, C.3    Angioni, A.4    Caniglia, M.5    De Sio, L.6    Fidani, P.7    Amici, A.8    Helson, L.9
  • 39
  • 41
    • 0022461970 scopus 로고
    • Murine cytotoxic activated macrophages inhibit aconitase in tumor cells. Inhibition involved the iron sulphur prosthetic group and is reversible
    • Drapier, J.C., and Hibbs, J.B., Jr. 1986. Murine cytotoxic activated macrophages inhibit aconitase in tumor cells. Inhibition involved the iron sulphur prosthetic group and is reversible. J. Clin. Invest. 78: 790-797.
    • (1986) J. Clin. Invest. , vol.78 , pp. 790-797
    • Drapier, J.C.1    Hibbs Jr., J.B.2
  • 43
    • 0023752206 scopus 로고
    • Synergistic antiproliferative effects on HL-60 cells: Deferoxamine enhances cytosine arabinoside, methotrexate, and daunorubicin cytotoxicity
    • Estrov, Z., Cohen, A., Gelfand, E.W., and Freedman, M.H. 1988. Synergistic antiproliferative effects on HL-60 cells: deferoxamine enhances cytosine arabinoside, methotrexate, and daunorubicin cytotoxicity. Am. J. Pediatr. Hematol. Oncol. 10: 288-291.
    • (1988) Am. J. Pediatr. Hematol. Oncol. , vol.10 , pp. 288-291
    • Estrov, Z.1    Cohen, A.2    Gelfand, E.W.3    Freedman, M.H.4
  • 47
    • 0017726547 scopus 로고
    • Selective toxicity induced by picolinic acid in simian virus 4-transformed cells in tissue culture
    • Fernandez-Pol, J.A., and Johnson, G.S. 1977. Selective toxicity induced by picolinic acid in simian virus 4-transformed cells in tissue culture. Cancer Res. 37: 4276-4279.
    • (1977) Cancer Res. , vol.37 , pp. 4276-4279
    • Fernandez-Pol, J.A.1    Johnson, G.S.2
  • 48
    • 0006113383 scopus 로고
    • Control of growth by picolinic acid: Differential response of normal and transformed cells
    • Fernandez-Pol, J.A., Bono, V.H., Jr., and Johnson, G.S. 1977. Control of growth by picolinic acid: differential response of normal and transformed cells. Proc. Natl. Acad. Sci. U.S.A. 74: 2889-2893.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 2889-2893
    • Fernandez-Pol, J.A.1    Bono Jr., V.H.2    Johnson, G.S.3
  • 49
    • 4344561207 scopus 로고
    • Differential ferrioxamine test for measuring chelatable body iron
    • Fielding, J. 1965. Differential ferrioxamine test for measuring chelatable body iron. J. Clin. Pathol. 18: 88-97.
    • (1965) J. Clin. Pathol. , vol.18 , pp. 88-97
    • Fielding, J.1
  • 50
    • 0023577562 scopus 로고
    • Variation in iron accumulation, transferrin membrane binding and DNA synthesis in the K-562 and U-937 cell lines induced by chelators and their iron complexes
    • Forsbeck, K., Nilsson, K., and Kontoghiorghes, G.J. 1987. Variation in iron accumulation, transferrin membrane binding and DNA synthesis in the K-562 and U-937 cell lines induced by chelators and their iron complexes. Eur. J. Haematol. 39: 318-325.
    • (1987) Eur. J. Haematol. , vol.39 , pp. 318-325
    • Forsbeck, K.1    Nilsson, K.2    Kontoghiorghes, G.J.3
  • 53
    • 0013805463 scopus 로고
    • The carcinostatic activity of alpha-(N) heterocyclic carboxaldehyde thiosemicarbazones. I. Isoquinoline-1-carboxaldehyde thiosemicarbazone
    • French, F.A., and Blanz, E.J., Jr. 1965. The carcinostatic activity of alpha-(N) heterocyclic carboxaldehyde thiosemicarbazones. I. Isoquinoline-1-carboxaldehyde thiosemicarbazone. Cancer Res. 25: 1454-1458.
    • (1965) Cancer Res. , vol.25 , pp. 1454-1458
    • French, F.A.1    Blanz Jr., E.J.2
  • 56
    • 0020558257 scopus 로고
    • Iron uptake and regulation of ferritin synthesis by hepatoma cells in hormone-supplemented serum-free medium
    • Goto, Y., Paterson, M., and Listowsky, I. 1983. Iron uptake and regulation of ferritin synthesis by hepatoma cells in hormone-supplemented serum-free medium. J. Biol. Chem. 258: 5248-5255.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5248-5255
    • Goto, Y.1    Paterson, M.2    Listowsky, I.3
  • 57
    • 0016107787 scopus 로고
    • The identification of 2,3-dihydroxybenzoic acid as a potentially useful iron chelating drug
    • Graziano, J.H., Grady, R.W., and Cerami, A. 1974. The identification of 2,3-dihydroxybenzoic acid as a potentially useful iron chelating drug. J. Pharmacol. Exp. Ther. 190: 570-575.
    • (1974) J. Pharmacol. Exp. Ther. , vol.190 , pp. 570-575
    • Graziano, J.H.1    Grady, R.W.2    Cerami, A.3
  • 59
    • 0027269545 scopus 로고
    • A structural role for metal ions in "wild type" conformation of the tumor suppressor protein p53
    • Hainaut, P., and Milner, J. 1993. A structural role for metal ions in "wild type" conformation of the tumor suppressor protein p53. Cancer Res. 53: 1739-1742.
    • (1993) Cancer Res. , vol.53 , pp. 1739-1742
    • Hainaut, P.1    Milner, J.2
  • 60
    • 0028838002 scopus 로고
    • Temperature sensitivity for conformation is an intrinsic property of wild-type p53
    • Hainaut, P., Butcher, S., and Milner, J. 1995. Temperature sensitivity for conformation is an intrinsic property of wild-type p53. Br. J. Cancer, 71: 227-231.
    • (1995) Br. J. Cancer , vol.71 , pp. 227-231
    • Hainaut, P.1    Butcher, S.2    Milner, J.3
  • 61
    • 0018837540 scopus 로고
    • Serum ferritin as a guide to therapy in neuroblastoma
    • Hann, H.-W.L., Howard, M.L., and Evans, A.E. 1980. Serum ferritin as a guide to therapy in neuroblastoma. Cancer Res. 40: 1411-1413.
    • (1980) Cancer Res. , vol.40 , pp. 1411-1413
    • Hann, H.-W.L.1    Howard, M.L.2    Evans, A.E.3
  • 62
    • 0022593176 scopus 로고
    • Source of increased ferritin in neuroblastoma: Studies with concanavalin A - Sepharose binding
    • Hann, H.-W.L., Stahlhut, M.W., and Evans, A.E. 1986. Source of increased ferritin in neuroblastoma: studies with concanavalin A - Sepharose binding. J. Natl. Cancer Inst. 76: 1031-1033.
    • (1986) J. Natl. Cancer Inst. , vol.76 , pp. 1031-1033
    • Hann, H.-W.L.1    Stahlhut, M.W.2    Evans, A.E.3
  • 63
    • 0025332680 scopus 로고
    • Effects of iron and desferrioxamine on cell growth and in vitro ferritin synthesis in human hepatoma cell lines
    • Hann, H.L., Stahlhut, M.W., and Hann, C.L. 1990. Effects of iron and desferrioxamine on cell growth and in vitro ferritin synthesis in human hepatoma cell lines. Hepatology, 11: 566-569.
    • (1990) Hepatology , vol.11 , pp. 566-569
    • Hann, H.L.1    Stahlhut, M.W.2    Hann, C.L.3
  • 64
    • 0026699860 scopus 로고
    • Antitumor effect of deferoxamine on human hepatocellular carcinoma growing in athymic nude mice
    • Hann, H.-W.L., Stahlhut, M.W., Rubin, R., and Maddrey, W.C. 1992. Antitumor effect of deferoxamine on human hepatocellular carcinoma growing in athymic nude mice. Cancer, 70: 2051-2056.
    • (1992) Cancer , vol.70 , pp. 2051-2056
    • Hann, H.-W.L.1    Stahlhut, M.W.2    Rubin, R.3    Maddrey, W.C.4
  • 65
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P.M., and Arosio, P. 1996. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta, 1275: 161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 66
    • 0026059699 scopus 로고
    • Mechanisms of bleomycin-induced lung damage
    • Hay, J., Shahzeidi, S., and Laurent, G. 1991. Mechanisms of bleomycin-induced lung damage. Arch. Toxicol. 65: 81-94.
    • (1991) Arch. Toxicol. , vol.65 , pp. 81-94
    • Hay, J.1    Shahzeidi, S.2    Laurent, G.3
  • 67
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress
    • Hentze, M.W., and Kühn, L.C. 1996. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 93: 8175-8182.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 68
    • 0019518135 scopus 로고
    • Mechanisms of in vivo chelation by pyridoxal isonicotinoyl hydrazone and other imino derivatives of pyridoxal
    • Hershko, C., Avramovici-Grisaru, S., Link, G., Gelfand, L., and Sarel, S. 1981. Mechanisms of in vivo chelation by pyridoxal isonicotinoyl hydrazone and other imino derivatives of pyridoxal. J. Lab. Clin. Med. 98: 99-108.
    • (1981) J. Lab. Clin. Med. , vol.98 , pp. 99-108
    • Hershko, C.1    Avramovici-Grisaru, S.2    Link, G.3    Gelfand, L.4    Sarel, S.5
  • 69
    • 0021128761 scopus 로고
    • Iron depletion. Possible cause of tumor cell cytotoxicity induced by activated macrophages
    • Hibbs, J.B., Jr., Taintor, R.R., and Vavrin, Z. 1984. Iron depletion. Possible cause of tumor cell cytotoxicity induced by activated macrophages. Biochem. Biophys. Res. Commun. 123: 716-723.
    • (1984) Biochem. Biophys. Res. Commun. , vol.123 , pp. 716-723
    • Hibbs Jr., J.B.1    Taintor, R.R.2    Vavrin, Z.3
  • 71
    • 0028931345 scopus 로고
    • Iron chelators induce apoptosis in proliferating cells
    • Hileti, D., Panayiotidis, P., and Hoffbrand, A.V. 1995. Iron chelators induce apoptosis in proliferating cells. Br. J. Haematol. 89: 181-187.
    • (1995) Br. J. Haematol. , vol.89 , pp. 181-187
    • Hileti, D.1    Panayiotidis, P.2    Hoffbrand, A.V.3
  • 72
    • 0018567483 scopus 로고
    • Effective iron chelation following oral adminstration of an isoniazid pyridoxal hydrazone
    • Hoy, T., Humphreys, J., Jacobs, A., Williams, A., and Ponka, P. 1979. Effective iron chelation following oral adminstration of an isoniazid pyridoxal hydrazone. Br. J. Haematol. 43: 443-449.
    • (1979) Br. J. Haematol. , vol.43 , pp. 443-449
    • Hoy, T.1    Humphreys, J.2    Jacobs, A.3    Williams, A.4    Ponka, P.5
  • 73
    • 0027486590 scopus 로고
    • Subcellular distribution of desferrioxamine and hydroxypyridin-4-one chelators in K562 cells affects chelation of intracellular iron pools
    • Hoyes, K.P., and Porter, J.B. 1993. Subcellular distribution of desferrioxamine and hydroxypyridin-4-one chelators in K562 cells affects chelation of intracellular iron pools. Br. J. Haematol. 85: 393-400.
    • (1993) Br. J. Haematol. , vol.85 , pp. 393-400
    • Hoyes, K.P.1    Porter, J.B.2
  • 74
    • 0026782447 scopus 로고
    • Cell cycle synchronization and growth inhibition by 3-hydroxypyridin-4-one iron chelators in leukemic cell lines
    • Hoyes, K.P., Hider, R.C., and Porter, J.B. 1992. Cell cycle synchronization and growth inhibition by 3-hydroxypyridin-4-one iron chelators in leukemic cell lines. Cancer Res. 52: 4591-4599.
    • (1992) Cancer Res. , vol.52 , pp. 4591-4599
    • Hoyes, K.P.1    Hider, R.C.2    Porter, J.B.3
  • 77
    • 0020961007 scopus 로고
    • The kinetics of transferrin endocytosis and iron uptake from transferrin in rabbit reticulocytes
    • Iacopetta, B.J., and Morgan, E.H. 1983. The kinetics of transferrin endocytosis and iron uptake from transferrin in rabbit reticulocytes. J. Biol. Chem. 258: 9108-9115.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9108-9115
    • Iacopetta, B.J.1    Morgan, E.H.2
  • 78
    • 0023898916 scopus 로고
    • Neuroblastomas contain iron-rich ferritin
    • Iancu, T.C., Shiloh, H., and Kedar, A. 1988. Neuroblastomas contain iron-rich ferritin. Cancer, 61: 2497-2502.
    • (1988) Cancer , vol.61 , pp. 2497-2502
    • Iancu, T.C.1    Shiloh, H.2    Kedar, A.3
  • 79
    • 0017700831 scopus 로고
    • Low molecular weight intracellular iron transport compounds
    • Jacobs, A. 1977. Low molecular weight intracellular iron transport compounds. Blood, 50: 433-439.
    • (1977) Blood , vol.50 , pp. 433-439
    • Jacobs, A.1
  • 80
    • 0001525013 scopus 로고
    • Cytotoxic chelators and chelates. I. Inhibition of DNA synthesis in cultured rodent and human cells by aroylhydrazones and by a copper(II) complex of salicylaldehyde benzoyl hydrazone
    • Johnson, D.K., Murphy, T.B., Rose, N.J., Goodwin, W.H., and Pickart, L. 1982. Cytotoxic chelators and chelates. I. Inhibition of DNA synthesis in cultured rodent and human cells by aroylhydrazones and by a copper(II) complex of salicylaldehyde benzoyl hydrazone. Inorg. Chim. Acta, 67: 159-165.
    • (1982) Inorg. Chim. Acta , vol.67 , pp. 159-165
    • Johnson, D.K.1    Murphy, T.B.2    Rose, N.J.3    Goodwin, W.H.4    Pickart, L.5
  • 81
    • 7444249085 scopus 로고
    • The biochemistry of deferoxamine and its relation to iron metabolism
    • Keberle, H. 1964. The biochemistry of deferoxamine and its relation to iron metabolism. Ann. N.Y. Acad. Sci. U.S.A. 119: 758-768.
    • (1964) Ann. N.Y. Acad. Sci. U.S.A. , vol.119 , pp. 758-768
    • Keberle, H.1
  • 82
    • 0025125020 scopus 로고
    • Synergistic inhibition of lymphoid tumor growth in vitro by combined treatment with the iron chelator deferoxamine and an immunoglobulin G monoclonal antibody against the transferrin receptor
    • Kemp, J.D., Smith, K.M., Kanner, L.J., Gomez, F., Thorson, J.A., and Naumann, P.W. 1990. Synergistic inhibition of lymphoid tumor growth in vitro by combined treatment with the iron chelator deferoxamine and an immunoglobulin G monoclonal antibody against the transferrin receptor. Blood, 76: 991-995.
    • (1990) Blood , vol.76 , pp. 991-995
    • Kemp, J.D.1    Smith, K.M.2    Kanner, L.J.3    Gomez, F.4    Thorson, J.A.5    Naumann, P.W.6
  • 83
    • 0026701955 scopus 로고
    • Inhibition of hematopoietic tumor growth by combined treatment with deferoxamine and an IgG monoclonal antibody against the transferrin receptor: Evidence for a threshold model of iron deprivation toxicity
    • Kemp, J.D., Thorson, J.A., Stewart, B.C., and Naumann, P.W. 1992. Inhibition of hematopoietic tumor growth by combined treatment with deferoxamine and an IgG monoclonal antibody against the transferrin receptor: evidence for a threshold model of iron deprivation toxicity. Cancer Res. 52: 4144-4148.
    • (1992) Cancer Res. , vol.52 , pp. 4144-4148
    • Kemp, J.D.1    Thorson, J.A.2    Stewart, B.C.3    Naumann, P.W.4
  • 85
    • 0025271438 scopus 로고
    • Induction of the heme oxygenase gene in human skin fibroblasts by hydrogen peroxide and UVA (365 nm) radiation: Evidence for the involvement of the hydroxyl radical
    • Keyes, S.M., and Tyrrell, R.M. 1990. Induction of the heme oxygenase gene in human skin fibroblasts by hydrogen peroxide and UVA (365 nm) radiation: evidence for the involvement of the hydroxyl radical. Carcinogenesis, 11: 787-791.
    • (1990) Carcinogenesis , vol.11 , pp. 787-791
    • Keyes, S.M.1    Tyrrell, R.M.2
  • 86
    • 0023115572 scopus 로고
    • Effectiveness of oral iron chelators assayed in the rat
    • Kim, B.K., Huebers, H.A., and Finch, C.A. 1987. Effectiveness of oral iron chelators assayed in the rat. Am. J. Hematol. 24: 277-284.
    • (1987) Am. J. Hematol. , vol.24 , pp. 277-284
    • Kim, B.K.1    Huebers, H.A.2    Finch, C.A.3
  • 89
    • 0022453348 scopus 로고
    • Iron mobilisation from ferritin using α-oxohydroxy heteroaromatic chelators
    • Kontoghiorghes, G.J. 1986. Iron mobilisation from ferritin using α-oxohydroxy heteroaromatic chelators. Biochem. J. 233: 299-302.
    • (1986) Biochem. J. , vol.233 , pp. 299-302
    • Kontoghiorghes, G.J.1
  • 90
    • 0021932825 scopus 로고
    • Site specificity of iron removal from transferrin by α-ketohydroxypyridone chelators
    • Kontoghiorghes, G.J., and Evans, R.W. 1985. Site specificity of iron removal from transferrin by α-ketohydroxypyridone chelators. FEBS Lett. 189: 141-144.
    • (1985) FEBS Lett. , vol.189 , pp. 141-144
    • Kontoghiorghes, G.J.1    Evans, R.W.2
  • 91
    • 0022871715 scopus 로고
    • Cytotoxic and DNA-inhibitory effects of iron chelators on human leukemic cell lines
    • Kontoghiorghes, G.J., Piga, A., and Hoffbrand, A.V. 1986a. Cytotoxic and DNA-inhibitory effects of iron chelators on human leukemic cell lines. Hematol. Oncol. 4: 195-204.
    • (1986) Hematol. Oncol. , vol.4 , pp. 195-204
    • Kontoghiorghes, G.J.1    Piga, A.2    Hoffbrand, A.V.3
  • 92
    • 0023009651 scopus 로고
    • Cytotoxic effects of the lipophilic iron chelator, omadine
    • Kontoghiorghes, G.J., Piga, A., and Hoffbrand, A.V. 1986b. Cytotoxic effects of the lipophilic iron chelator, omadine. FEBS Lett. 204: 208-212.
    • (1986) FEBS Lett. , vol.204 , pp. 208-212
    • Kontoghiorghes, G.J.1    Piga, A.2    Hoffbrand, A.V.3
  • 93
    • 0016236741 scopus 로고
    • Clinical trial of 5-hydroxypicolinaldehyde thiosemicarbazone (5-HP: NSC-107392), with special reference to its Fe chelating properties
    • Krakoff, I.H., Etcubanas, E., Tan, C., Mayer, K., Bethune, V., and Burchenai, J.H. 1974. Clinical trial of 5-hydroxypicolinaldehyde thiosemicarbazone (5-HP: NSC-107392), with special reference to its Fe chelating properties. Cancer Chemother. Rep. 53: 207-212.
    • (1974) Cancer Chemother. Rep. , vol.53 , pp. 207-212
    • Krakoff, I.H.1    Etcubanas, E.2    Tan, C.3    Mayer, K.4    Bethune, V.5    Burchenai, J.H.6
  • 94
    • 0021840709 scopus 로고
    • Sequential expression of genes involved in human T lymphocyte growth and differentiation
    • Kronke, M., Leonard, W.J., Depper, J.M., and Greene, W.C. 1985. Sequential expression of genes involved in human T lymphocyte growth and differentiation. J. Exp. Med. 161: 1593-1598.
    • (1985) J. Exp. Med. , vol.161 , pp. 1593-1598
    • Kronke, M.1    Leonard, W.J.2    Depper, J.M.3    Greene, W.C.4
  • 95
    • 0000622023 scopus 로고
    • Iron-transferrin requirements and transferrin receptor expression in proliferating cells
    • Edited by P. Ponka, H.M. Schulman, and R.C. Woodworth. CRC Press, Boca Raton, Fla.
    • Kühn, L.C., Schulman, H.M., and Ponka, P. 1990. Iron-transferrin requirements and transferrin receptor expression in proliferating cells. In Iron transport and storage. Edited by P. Ponka, H.M. Schulman, and R.C. Woodworth. CRC Press, Boca Raton, Fla. pp. 141-191.
    • (1990) Iron Transport and Storage , pp. 141-191
    • Kühn, L.C.1    Schulman, H.M.2    Ponka, P.3
  • 96
    • 0021813287 scopus 로고
    • Cellular pharmacology of deferrioxamine B and derivatives in cultured rat hepatocytes in relation to iron mobilisation
    • Laub, R., Schneider, Y.-J., Octave, J.-N., Trouet, A., and Crichton, R.R. 1985. Cellular pharmacology of deferrioxamine B and derivatives in cultured rat hepatocytes in relation to iron mobilisation. Biochem. Pharmacol. 34: 1175-1183.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1175-1183
    • Laub, R.1    Schneider, Y.-J.2    Octave, J.-N.3    Trouet, A.4    Crichton, R.R.5
  • 97
    • 0021259518 scopus 로고
    • Deferoxamine: A reversible S phase inhibitor of human lymphocyte proliferation
    • Lederman, H.M., Cohen, A., Lee, J.W.W., Freedman, M.H., and Gelfand, E. W. 1984. Deferoxamine: a reversible S phase inhibitor of human lymphocyte proliferation. Blood, 64: 748-753.
    • (1984) Blood , vol.64 , pp. 748-753
    • Lederman, H.M.1    Cohen, A.2    Lee, J.W.W.3    Freedman, M.H.4    Gelfand, E.W.5
  • 99
  • 100
    • 0016724542 scopus 로고
    • Measurement of serum ferritin by radioimmunoassay: Results in normal individuals and patients with breast cancer
    • Marcus, D.M., and Zinberg, N. 1975. Measurement of serum ferritin by radioimmunoassay: results in normal individuals and patients with breast cancer. J. Natl. Cancer Inst. 55: 791-795.
    • (1975) J. Natl. Cancer Inst. , vol.55 , pp. 791-795
    • Marcus, D.M.1    Zinberg, N.2
  • 103
    • 0026770310 scopus 로고
    • Increased expression of cytokeratin and ferritin-H genes in tumorigenic clones of the SW613-S human colon carcinoma cell line
    • Modjtahedi, N., Frebourg, T., Fossar, N., Lavialle, C., Cremisi, C., and Brison, O. 1992. Increased expression of cytokeratin and ferritin-H genes in tumorigenic clones of the SW613-S human colon carcinoma cell line. Exp. Cell. Res. 201: 74-82.
    • (1992) Exp. Cell. Res. , vol.201 , pp. 74-82
    • Modjtahedi, N.1    Frebourg, T.2    Fossar, N.3    Lavialle, C.4    Cremisi, C.5    Brison, O.6
  • 105
    • 0024276911 scopus 로고
    • A stem-loop in the 3′ untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm
    • Müllner, E.W., and Kühn, L.C. 1988. A stem-loop in the 3′ untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm. Cell, 53: 815-825.
    • (1988) Cell , vol.53 , pp. 815-825
    • Müllner, E.W.1    Kühn, L.C.2
  • 106
    • 0018236898 scopus 로고
    • Ferritin: Structure, biosynthesis and role in iron metabolism
    • Munro, H.N., and Linder, M.C. 1978. Ferritin: structure, biosynthesis and role in iron metabolism. Physiol. Rev. 58: 317-396.
    • (1978) Physiol. Rev. , vol.58 , pp. 317-396
    • Munro, H.N.1    Linder, M.C.2
  • 107
    • 0023445376 scopus 로고
    • Conservation of ferritin heavy subunit gene structure: Implications for the regulation of ferritin gene expression
    • Murray, M.T., White, K., and Munro, H.N. 1987. Conservation of ferritin heavy subunit gene structure: implications for the regulation of ferritin gene expression. Proc. Natl. Acad. Sci. U.S.A. 84: 7438-7442.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7438-7442
    • Murray, M.T.1    White, K.2    Munro, H.N.3
  • 109
    • 0027521831 scopus 로고
    • Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators
    • Nyholm, S., Mann, G.J., Johansson, A.G., Bergeron, R.J., Gräslund, A., and Thelander, L. 1993. Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators. J. Biol. Chem. 268: 26 200-26 205.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26200-26205
    • Nyholm, S.1    Mann, G.J.2    Johansson, A.G.3    Bergeron, R.J.4    Gräslund, A.5    Thelander, L.6
  • 110
    • 0017194077 scopus 로고
    • Chelate mediated transfer of iron from transferrin to desferrioxamine
    • Pollack, S., Aisen, P., Laskey, F.D., and Vanderhoff, G. 1976. Chelate mediated transfer of iron from transferrin to desferrioxamine. Br. J. Haematol. 34: 231-235.
    • (1976) Br. J. Haematol. , vol.34 , pp. 231-235
    • Pollack, S.1    Aisen, P.2    Laskey, F.D.3    Vanderhoff, G.4
  • 111
    • 0018394556 scopus 로고
    • Mobilization of iron from reticulocytes. Identification of pyridoxal isonicotinoyl hydrazone as a new iron chelating agent
    • Ponka, P., Borova, J., Neuwirt, J., and Fuchs, O. 1979a. Mobilization of iron from reticulocytes. Identification of pyridoxal isonicotinoyl hydrazone as a new iron chelating agent. FEBS Lett. 97: 317-321.
    • (1979) FEBS Lett. , vol.97 , pp. 317-321
    • Ponka, P.1    Borova, J.2    Neuwirt, J.3    Fuchs, O.4
  • 112
    • 0018798539 scopus 로고
    • A study of intracellular iron metabolism using pyridoxal isonicotinoyl hydrazone and other synthetic chelating agents
    • Ponka, P., Borova, J., Neuwirt, J., Fuchs, O., and Necas, E. 1979b. A study of intracellular iron metabolism using pyridoxal isonicotinoyl hydrazone and other synthetic chelating agents. Biochim. Biophys. Acta, 586: 278-297.
    • (1979) Biochim. Biophys. Acta , vol.586 , pp. 278-297
    • Ponka, P.1    Borova, J.2    Neuwirt, J.3    Fuchs, O.4    Necas, E.5
  • 113
    • 0023780401 scopus 로고
    • Effect of pyridoxal isonicotinoyl hydrazone and other hydrazones on iron release from macrophages, reticulocytes and hepatocytes
    • Ponka, P., Richardson, D., Baker, E., Schulman, H.M., and Edward, J.T. 1988. Effect of pyridoxal isonicotinoyl hydrazone and other hydrazones on iron release from macrophages, reticulocytes and hepatocytes. Biochim. Biophys. Acta, 967: 122-129.
    • (1988) Biochim. Biophys. Acta , vol.967 , pp. 122-129
    • Ponka, P.1    Richardson, D.2    Baker, E.3    Schulman, H.M.4    Edward, J.T.5
  • 114
    • 0031963449 scopus 로고    scopus 로고
    • Function and regulation of transferrin and ferritin
    • Ponka, P., Beaumont, C., and Richardson, D.R. 1998. Function and regulation of transferrin and ferritin. Semin. Hematol. 35: 1-21.
    • (1998) Semin. Hematol. , vol.35 , pp. 1-21
    • Ponka, P.1    Beaumont, C.2    Richardson, D.R.3
  • 115
    • 0023811903 scopus 로고
    • Iron mobilization from hepatocyte monolayer cultures by chelators: The importance of membrane permeability and the iron-binding constant
    • Porter, J.B., Gyparaki, M., Burke, L.C., Huehns, E.R., Sarpong, P., Saez, V., and Hider, R.C. 1988. Iron mobilization from hepatocyte monolayer cultures by chelators: the importance of membrane permeability and the iron-binding constant. Blood, 72: 1497-1503.
    • (1988) Blood , vol.72 , pp. 1497-1503
    • Porter, J.B.1    Gyparaki, M.2    Burke, L.C.3    Huehns, E.R.4    Sarpong, P.5    Saez, V.6    Hider, R.C.7
  • 116
    • 0030998296 scopus 로고    scopus 로고
    • Mobilization of iron from neoplastic cells by some iron chelators is an energy-dependent process
    • Richardson, D.R. 1997. Mobilization of iron from neoplastic cells by some iron chelators is an energy-dependent process. Biochim. Biophys. Acta, 1320: 45-67.
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 45-67
    • Richardson, D.R.1
  • 117
    • 0025341256 scopus 로고
    • The uptake of iron and transferrin by the human melanoma cell
    • Richardson, D.R., and Baker, E. 1990. The uptake of iron and transferrin by the human melanoma cell. Biochim. Biophys. Acta, 1053: 1-12.
    • (1990) Biochim. Biophys. Acta , vol.1053 , pp. 1-12
    • Richardson, D.R.1    Baker, E.2
  • 118
    • 0026081935 scopus 로고
    • The release of iron and transferrin from the human melanoma cell
    • Richardson, D.R., and Baker, E. 1991. The release of iron and transferrin from the human melanoma cell. Biochim. Biophys. Acta, 1091: 294-302.
    • (1991) Biochim. Biophys. Acta , vol.1091 , pp. 294-302
    • Richardson, D.R.1    Baker, E.2
  • 119
    • 0026690909 scopus 로고
    • Two mechanisms of iron uptake from transferrin by melanoma cells. The effect of desferrioxamine and ferric ammonium citrate
    • Richardson, D.R., and Baker, E. 1992. Two mechanisms of iron uptake from transferrin by melanoma cells. The effect of desferrioxamine and ferric ammonium citrate. J. Biol. Chem. 267: 13 972-13 979.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13972-13979
    • Richardson, D.R.1    Baker, E.2
  • 120
    • 0027944830 scopus 로고
    • Two saturable mechanisms of iron uptake from transferrin human melanoma cells: The effect of transferrin concentration, chelators and metabolic probes on transferrin and iron uptake
    • Richardson, D.R., and Baker, E. 1994. Two saturable mechanisms of iron uptake from transferrin human melanoma cells: the effect of transferrin concentration, chelators and metabolic probes on transferrin and iron uptake. J. Cell. Physiol. 161: 160-168.
    • (1994) J. Cell. Physiol. , vol.161 , pp. 160-168
    • Richardson, D.R.1    Baker, E.2
  • 121
    • 0030894798 scopus 로고    scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents. II. The mechanism of action of ligands derived from salicylaldehyde benzoyl hydrazone and 2-hydroxy-1-naphthylaldehyde benzoyl hydrazone
    • Richardson, D.R., and Milnes, K. 1997. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents. II. The mechanism of action of ligands derived from salicylaldehyde benzoyl hydrazone and 2-hydroxy-1-naphthylaldehyde benzoyl hydrazone. Blood, 89: 3025-3038.
    • (1997) Blood , vol.89 , pp. 3025-3038
    • Richardson, D.R.1    Milnes, K.2
  • 122
    • 0028535112 scopus 로고
    • The iron metabolism of the human neuroblastoma cell. Lack of relationship between the efficacy of iron chelation and the inhibition of DNA synthesis
    • Richardson, D.R., and Ponka, P. 1994. The iron metabolism of the human neuroblastoma cell. Lack of relationship between the efficacy of iron chelation and the inhibition of DNA synthesis. J. Lab. Clin. Med. 124: 660-671.
    • (1994) J. Lab. Clin. Med. , vol.124 , pp. 660-671
    • Richardson, D.R.1    Ponka, P.2
  • 123
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson, D.R., and Ponka, P. 1997. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta, 1331: 1-40.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 124
    • 0023800613 scopus 로고
    • Effects of pyridoxal isonicotinoyl hydrazone and analogs on iron metabolism in hepatocytes and macrophages in culture
    • Richardson, D., Baker, E., Ponka, P., Wilairat, P., Vitolo, M.L., and Webb, J. 1988. Effects of pyridoxal isonicotinoyl hydrazone and analogs on iron metabolism in hepatocytes and macrophages in culture. Birth Defects, 23(5B): 81-88.
    • (1988) Birth Defects , vol.23 , Issue.5 B , pp. 81-88
    • Richardson, D.1    Baker, E.2    Ponka, P.3    Wilairat, P.4    Vitolo, M.L.5    Webb, J.6
  • 125
    • 0028158768 scopus 로고
    • The effect of the iron(III) chelator, desferrioxamine, on iron and transferrin uptake by the human malignant melanoma cell
    • Richardson, D., Ponka, P., and Baker, E. 1994. The effect of the iron(III) chelator, desferrioxamine, on iron and transferrin uptake by the human malignant melanoma cell. Cancer Res. 54: 685-689.
    • (1994) Cancer Res. , vol.54 , pp. 685-689
    • Richardson, D.1    Ponka, P.2    Baker, E.3
  • 126
    • 0029030330 scopus 로고
    • Nitrogen monoxide decreases iron uptake from transferrin but does not mobilize iron from prelabelled neoplastic cells
    • Richardson, D.R., Neumannova, V., and Ponka, P. 1995a. Nitrogen monoxide decreases iron uptake from transferrin but does not mobilize iron from prelabelled neoplastic cells. Biochim. Biophys. Acta, 1266: 250-260.
    • (1995) Biochim. Biophys. Acta , vol.1266 , pp. 250-260
    • Richardson, D.R.1    Neumannova, V.2    Ponka, P.3
  • 127
    • 0028891974 scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents
    • Richardson, D.R., Tran, E., and Ponka, P. 1995b. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents. Blood, 86: 4295-4306.
    • (1995) Blood , vol.86 , pp. 4295-4306
    • Richardson, D.R.1    Tran, E.2    Ponka, P.3
  • 128
    • 0029865751 scopus 로고    scopus 로고
    • Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: Examination of the intermediates of iron metabolism
    • Richardson, D.R., Ponka, P., and Vyoral, D. 1996. Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: examination of the intermediates of iron metabolism. Blood, 87: 3477-3488.
    • (1996) Blood , vol.87 , pp. 3477-3488
    • Richardson, D.R.1    Ponka, P.2    Vyoral, D.3
  • 129
    • 0000553206 scopus 로고
    • Nicotinoyl and isonicotinoyl hydrazones of pyridoxal
    • Sah, P. 1954. Nicotinoyl and isonicotinoyl hydrazones of pyridoxal. J. Am. Chem. Soc. 76: 300.
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 300
    • Sah, P.1
  • 131
    • 0015153126 scopus 로고
    • Mechanism of inhibition of ribonucleoside diphosphate reductase by α-(N)-heterocyclic aldehyde thiosemicarbazones
    • Sartorelli, A.C., Agrawal, K.C., and Moore, E.C. 1971. Mechanism of inhibition of ribonucleoside diphosphate reductase by α-(N)-heterocyclic aldehyde thiosemicarbazones. Biochem. Pharmacol. 20: 3119-3123.
    • (1971) Biochem. Pharmacol. , vol.20 , pp. 3119-3123
    • Sartorelli, A.C.1    Agrawal, K.C.2    Moore, E.C.3
  • 132
    • 0027320660 scopus 로고
    • Effects of agents that inhibit cellular iron incorporation on bladder cell proliferation
    • Seligman, P.A., Schleicher, R.B., Siriwardana, G., Domenico, J., and Gelfand, E.W. 1993. Effects of agents that inhibit cellular iron incorporation on bladder cell proliferation. Blood, 82: 1608-1617.
    • (1993) Blood , vol.82 , pp. 1608-1617
    • Seligman, P.A.1    Schleicher, R.B.2    Siriwardana, G.3    Domenico, J.4    Gelfand, E.W.5
  • 134
    • 0026763165 scopus 로고
    • A low-spin iron complex in human melanoma and rat hepatoma cells and a high spin iron(II) complex in rat hepatoma cells
    • St.Pierre, T., Richardson, D.R., Baker, E., and Webb, J. 1992. A low-spin iron complex in human melanoma and rat hepatoma cells and a high spin iron(II) complex in rat hepatoma cells. Biochim. Biophys. Acta, 1135: 154-158.
    • (1992) Biochim. Biophys. Acta , vol.1135 , pp. 154-158
    • St.Pierre, T.1    Richardson, D.R.2    Baker, E.3    Webb, J.4
  • 135
    • 0018777993 scopus 로고
    • Studies of desferrioxamine and ferrioxamine metabolism in normal and iron-loaded subjects
    • Summers, M.R., Jacobs, A., Tudway, D., Perera, P., and Ricketts, C. 1979. Studies of desferrioxamine and ferrioxamine metabolism in normal and iron-loaded subjects. Br. J. Hematol. 42: 547-555.
    • (1979) Br. J. Hematol. , vol.42 , pp. 547-555
    • Summers, M.R.1    Jacobs, A.2    Tudway, D.3    Perera, P.4    Ricketts, C.5
  • 137
    • 0019586989 scopus 로고
    • Ubiquitous cell-surface glycoprotein on tumor cells is proliferation-associated receptor for transferrin
    • Sutherland, R., Delia, D., Schneider, C., Newman, R., Kemshead, J., and Greaves, M. 1981. Ubiquitous cell-surface glycoprotein on tumor cells is proliferation-associated receptor for transferrin. Proc. Natl. Acad. Sci. U.S.A. 78: 4515-4519.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 4515-4519
    • Sutherland, R.1    Delia, D.2    Schneider, C.3    Newman, R.4    Kemshead, J.5    Greaves, M.6
  • 138
    • 0021917196 scopus 로고
    • Role of transferrin, Fe, and transferrin receptors in myeloid leukemia cell growth
    • Taetle, R., Rhyner, K., Castagnola, D., and Mendelsohn, J. 1985. Role of transferrin, Fe, and transferrin receptors in myeloid leukemia cell growth. J. Clin. Invest. 75: 1061-1067.
    • (1985) J. Clin. Invest. , vol.75 , pp. 1061-1067
    • Taetle, R.1    Rhyner, K.2    Castagnola, D.3    Mendelsohn, J.4
  • 140
    • 0025879338 scopus 로고
    • Differential regulation of the tumor suppressor molecules, retinoblastoma susceptibility gene product (Rb) and p53, during cell cycle progression of normal human T cells
    • Terada, N., Lucas, J.J., and Gelfand, E.W. 1991. Differential regulation of the tumor suppressor molecules, retinoblastoma susceptibility gene product (Rb) and p53, during cell cycle progression of normal human T cells. J. Immunol. 147: 698-704.
    • (1991) J. Immunol. , vol.147 , pp. 698-704
    • Terada, N.1    Lucas, J.J.2    Gelfand, E.W.3
  • 141
    • 0020567471 scopus 로고
    • Mechanism of inhibition of mammalian ribonucleotide reductase by the iron chelate of 1-formylisoquinoline thiosemicarbazone
    • Thelander, L., and Gräslund, A. 1983. Mechanism of inhibition of mammalian ribonucleotide reductase by the iron chelate of 1-formylisoquinoline thiosemicarbazone. J. Biol. Chem. 258: 4063-4066.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4063-4066
    • Thelander, L.1    Gräslund, A.2
  • 142
  • 143
    • 0021099095 scopus 로고
    • Continual presence of oxygen and iron is required for mammalian ribonucleotide reduction: Possible regulation mechanism
    • Thelander, L., Gräslund, A., and Thelander, M. 1983. Continual presence of oxygen and iron is required for mammalian ribonucleotide reduction: possible regulation mechanism. Biochem. Biophys. Res. Commun. 110: 859-865.
    • (1983) Biochem. Biophys. Res. Commun. , vol.110 , pp. 859-865
    • Thelander, L.1    Gräslund, A.2    Thelander, M.3
  • 144
    • 0025306383 scopus 로고
    • Release of iron from diferric transferrin in the presence of rat liver membranes: No evidence of a diferric transferrin reductase
    • Thorstensen, K., and Aisen, P. 1990. Release of iron from diferric transferrin in the presence of rat liver membranes: no evidence of a diferric transferrin reductase. Biochim. Biophys. Acta, 1052: 29-35.
    • (1990) Biochim. Biophys. Acta , vol.1052 , pp. 29-35
    • Thorstensen, K.1    Aisen, P.2
  • 146
    • 0029953577 scopus 로고    scopus 로고
    • Transferrin receptor-independent uptake of diferric transferrin by human hepatoma cells with antisense inhibition of receptor expression
    • Trinder, D., Zak, O., and Aisen, P. 1996. Transferrin receptor-independent uptake of diferric transferrin by human hepatoma cells with antisense inhibition of receptor expression. Hepatology, 23: 1512-1520.
    • (1996) Hepatology , vol.23 , pp. 1512-1520
    • Trinder, D.1    Zak, O.2    Aisen, P.3
  • 147
    • 0000302649 scopus 로고
    • Monoclonal antibody to transferrin receptor blocks transferrin binding and inhibits tumor cell growth in vitro
    • Trowbridge, I.S., and Lopez, F. 1982. Monoclonal antibody to transferrin receptor blocks transferrin binding and inhibits tumor cell growth in vitro. Proc. Natl. Acad. Sci. U.S.A. 79: 1175-1179.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 1175-1179
    • Trowbridge, I.S.1    Lopez, F.2
  • 148
    • 0019570604 scopus 로고
    • Human cell surface glycoprotein related to cell proliferation is the receptor for transferrin
    • Trowbridge, I.S., and Omary, M.B. 1981. Human cell surface glycoprotein related to cell proliferation is the receptor for transferrin. Proc. Natl. Acad. Sci. U.S.A. 78: 3039-3043.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 3039-3043
    • Trowbridge, I.S.1    Omary, M.B.2
  • 149
    • 0027450457 scopus 로고
    • Preferential repression of the H-subunit of ferritin by adenovirus E1A in NIH-3T3 mouse fibroblasts
    • Tsuji, Y., Kwak, E., Saika, T., Torti, S.V., and Torti, F.M. 1993. Preferential repression of the H-subunit of ferritin by adenovirus E1A in NIH-3T3 mouse fibroblasts. J. Biol. Chem. 268: 7270-7275.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7270-7275
    • Tsuji, Y.1    Kwak, E.2    Saika, T.3    Torti, S.V.4    Torti, F.M.5
  • 150
    • 0029155970 scopus 로고
    • FER-1, an enhancer of the ferritin H gene and a target of E1A-mediated transcriptional repression
    • Tsuji, Y., Akebi, N., Lam, T.K., Nakabeppu, Y., Torti, S.V., and Torti, F.M. 1995. FER-1, an enhancer of the ferritin H gene and a target of E1A-mediated transcriptional repression. Mol. Cell. Biol. 15: 5152-5164.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5152-5164
    • Tsuji, Y.1    Akebi, N.2    Lam, T.K.3    Nakabeppu, Y.4    Torti, S.V.5    Torti, F.M.6
  • 151
    • 0030970287 scopus 로고    scopus 로고
    • Approaches to define pathways of redox regulation of a eukaryotic gene: The heme oxygenase 1 example
    • Tyrrell, R.M. 1997. Approaches to define pathways of redox regulation of a eukaryotic gene: the heme oxygenase 1 example. Methods, 11: 313-318.
    • (1997) Methods , vol.11 , pp. 313-318
    • Tyrrell, R.M.1
  • 152
    • 0029016627 scopus 로고
    • Induction of apoptosis by iron deprivation in human leukemic CCRF-CEM cells
    • Ul-Haq, R., Wereley, J.P., and Chitambar, C.R. 1995. Induction of apoptosis by iron deprivation in human leukemic CCRF-CEM cells. Exp. Hematol. 23: 428-432.
    • (1995) Exp. Hematol. , vol.23 , pp. 428-432
    • Ul-Haq, R.1    Wereley, J.P.2    Chitambar, C.R.3
  • 154
    • 0000515888 scopus 로고
    • Release of iron from ferritin by pyridoxal isonicotinoyl hydrazone and related compounds
    • Vitolo, M.L., Webb, J., and Saltman, P. 1984. Release of iron from ferritin by pyridoxal isonicotinoyl hydrazone and related compounds. J. Inorg. Biochem. 20: 255-262.
    • (1984) J. Inorg. Biochem. , vol.20 , pp. 255-262
    • Vitolo, M.L.1    Webb, J.2    Saltman, P.3
  • 155
    • 0021356806 scopus 로고
    • Iron withholding a defense against infection and neoplasia
    • Weinberg, E.D. 1984. Iron withholding a defense against infection and neoplasia. Physiol. Rev. 64: 65-102.
    • (1984) Physiol. Rev. , vol.64 , pp. 65-102
    • Weinberg, E.D.1
  • 156
    • 0017135357 scopus 로고
    • The effect of chelating agents on cellular iron metabolism
    • White, G.P., Bailey-Wood, R., and Jacobs, A. 1976. The effect of chelating agents on cellular iron metabolism. Clin. Sci. Mol. Med. 50: 145-150.
    • (1976) Clin. Sci. Mol. Med. , vol.50 , pp. 145-150
    • White, G.P.1    Bailey-Wood, R.2    Jacobs, A.3
  • 157
    • 0018955647 scopus 로고
    • The pathogenesis of rat liver cancer caused by chemical carcinogens
    • Williams, G.M. 1980. The pathogenesis of rat liver cancer caused by chemical carcinogens. Biochim. Biophys. Acta, 605: 167-189.
    • (1980) Biochim. Biophys. Acta , vol.605 , pp. 167-189
    • Williams, G.M.1
  • 158
    • 0025602528 scopus 로고
    • Regulation and drug resistance mechanisms of mammalian ribonucleotide reductase, and the significance to DNA synthesis
    • Wright, J.A., Chan, A.K., Choy, B.K., Hurta, R.A., McClarty, G.A., and Tagger, A.Y. 1990. Regulation and drug resistance mechanisms of mammalian ribonucleotide reductase, and the significance to DNA synthesis. Biochem. Cell. Biol. 68: 1364-1371.
    • (1990) Biochem. Cell. Biol. , vol.68 , pp. 1364-1371
    • Wright, J.A.1    Chan, A.K.2    Choy, B.K.3    Hurta, R.A.4    McClarty, G.A.5    Tagger, A.Y.6


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