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Volumn 270, Issue 8, 2003, Pages 1689-1698

Multidentate pyridinones inhibit the metabolism of nontransferrin-bound iron by hepatocytes and hepatoma cells

Author keywords

Chemotherapy; Iron chelation therapy; Liver cells; Non transferrin bound iron

Indexed keywords

DEFERIPRONE; DEFEROXAMINE; N,N,N TRIS[3 HYDROXY 1 METHYL 2(1H) PYRIDINONE 4 CARBOXAMINOETHYL]AMINE; PYRIDONE DERIVATIVE; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 0037733128     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03525.x     Document Type: Article
Times cited : (19)

References (48)
  • 1
    • 0018894715 scopus 로고
    • A non-transferrin-bound serum iron in idiopathic hemochromatosis
    • Batey, R.G., Fong, P.L.C., Shamir, S. & Sherlock, S. (1980) A non-transferrin-bound serum iron in idiopathic hemochromatosis. Dig. Dis. Sci. 25, 340-346.
    • (1980) Dig. Dis. Sci. , vol.25 , pp. 340-346
    • Batey, R.G.1    Fong, P.L.C.2    Shamir, S.3    Sherlock, S.4
  • 2
    • 0021910539 scopus 로고
    • Low-molecular-weight iron complexes and oxygen radical reactions in idiopathic hemochromatosis
    • Gutteridge, J.M.C., Rowley, D.A., Griffiths, E. & Halliwell, B. (1985) Low-molecular-weight iron complexes and oxygen radical reactions in idiopathic hemochromatosis. Clin. Sci. 68, 463-467.
    • (1985) Clin. Sci. , vol.68 , pp. 463-467
    • Gutteridge, J.M.C.1    Rowley, D.A.2    Griffiths, E.3    Halliwell, B.4
  • 3
    • 0024564712 scopus 로고
    • Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis. Characterization by high performance liquid chromatography and nuclear magnetic resonance spectroscopy
    • Grootveld, M., Bell, J.D., Halliwell, B., Aruoma, O.I., Bomford, A. & Sadler, P.J. (1989) Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis. Characterization by high performance liquid chromatography and nuclear magnetic resonance spectroscopy. J. Biol. Chem. 264, 4417-4422.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4417-4422
    • Grootveld, M.1    Bell, J.D.2    Halliwell, B.3    Aruoma, O.I.4    Bomford, A.5    Sadler, P.J.6
  • 4
    • 0018164919 scopus 로고
    • Non-specific serum iron in thalassaemia: An abnormal serum iron fraction of potential toxicity
    • Hershko, C., Graham, G., Bates, G. & Rachmilewitz, E.A. (1978) Non-specific serum iron in thalassaemia: an abnormal serum iron fraction of potential toxicity. Br. J. Haematol. 40, 235-263.
    • (1978) Br. J. Haematol. , vol.40 , pp. 235-263
    • Hershko, C.1    Graham, G.2    Bates, G.3    Rachmilewitz, E.A.4
  • 5
    • 0018570169 scopus 로고
    • Nonspecific serum iron in thalassaemia: Quantitation and chemical reactivity
    • Graham, G., Bates, G.W., Rachmilewitz, E.A. & Hershko, C. (1979) Nonspecific serum iron in thalassaemia: quantitation and chemical reactivity. Am. J. Hematol. 6, 207-217.
    • (1979) Am. J. Hematol. , vol.6 , pp. 207-217
    • Graham, G.1    Bates, G.W.2    Rachmilewitz, E.A.3    Hershko, C.4
  • 7
    • 0029127994 scopus 로고
    • Presence of iron catalytic for free radical reactions in patients undergoing chemotherapy: Implications for therapeutic management
    • Carmine, T.C., Evans, P., Bruchelt, G., Evans, R., Handgretinger, R., Niethammer, D. & Halliwell, B. (1995) Presence of iron catalytic for free radical reactions in patients undergoing chemotherapy: implications for therapeutic management. Cancer Lett. 94, 219-226.
    • (1995) Cancer Lett. , vol.94 , pp. 219-226
    • Carmine, T.C.1    Evans, P.2    Bruchelt, G.3    Evans, R.4    Handgretinger, R.5    Niethammer, D.6    Halliwell, B.7
  • 8
    • 0033677772 scopus 로고    scopus 로고
    • The importance of non-transferrin bound iron in disorders of iron metabolism
    • Breuer, W., Hershko, C. & Cabantchik, Z.I. (2000) The importance of non-transferrin bound iron in disorders of iron metabolism. Transfus. Sci. 23, 185-192.
    • (2000) Transfus. Sci. , vol.23 , pp. 185-192
    • Breuer, W.1    Hershko, C.2    Cabantchik, Z.I.3
  • 9
    • 0014907456 scopus 로고
    • State of Fe (III) in normal human serum: Low molecular weight and protein ligands besides transferrin
    • Sarkar, B. (1970) State of Fe (III) in normal human serum: low molecular weight and protein ligands besides transferrin. Can. J. Biochem. 48, 1339-1350.
    • (1970) Can. J. Biochem. , vol.48 , pp. 1339-1350
    • Sarkar, B.1
  • 10
    • 0032510294 scopus 로고    scopus 로고
    • Characterisation of non-transferrin-bound iron (ferric citrate) uptake by rat hepatocytes in culture
    • Baker, E., Baker, S.M. & Morgan, E.H. (1998) Characterisation of non-transferrin-bound iron (ferric citrate) uptake by rat hepatocytes in culture. Biochim. Biophys. Acta 1380, 21-30.
    • (1998) Biochim. Biophys. Acta , vol.1380 , pp. 21-30
    • Baker, E.1    Baker, S.M.2    Morgan, E.H.3
  • 11
    • 0028586693 scopus 로고
    • Control of disease by selective iron depletion: A novel therapeutic strategy utilizing iron chelators
    • Hershko, C. (1994) Control of disease by selective iron depletion: a novel therapeutic strategy utilizing iron chelators. Baillieres Clin. Haematol. 7, 965-1000.
    • (1994) Baillieres Clin. Haematol. , vol.7 , pp. 965-1000
    • Hershko, C.1
  • 15
    • 0017157055 scopus 로고
    • Isolation and characterization of iron-binding proteins from rat intestinal mucosa
    • Huebers, H., Huebers, E., Rummel, W. & Crichton, R.R. (1976) Isolation and characterization of iron-binding proteins from rat intestinal mucosa. Eur. J. Biochem. 66, 447-455.
    • (1976) Eur. J. Biochem. , vol.66 , pp. 447-455
    • Huebers, H.1    Huebers, E.2    Rummel, W.3    Crichton, R.R.4
  • 16
    • 0021901499 scopus 로고
    • Transferrin and iron release from rat hepatocytes in culture
    • Baker, E., Page, M. & Morgan, E.H. (1985) Transferrin and iron release from rat hepatocytes in culture. Am. J. Physiol. 248, G93-G97.
    • (1985) Am. J. Physiol. , vol.248
    • Baker, E.1    Page, M.2    Morgan, E.H.3
  • 17
    • 0026690909 scopus 로고
    • Two mechanisms of iron uptake from transferrin by melanoma cells: The effect of desferrioxamine and ferric ammonium citrate
    • Richardson, D.R. & 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, 13972-13979.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13972-13979
    • Richardson, D.R.1    Baker, E.2
  • 18
    • 0014978068 scopus 로고
    • An improved fluorometric assay for DNA
    • Hinegardner, R.T. (1971) An improved fluorometric assay for DNA. Anal. Biochem. 39, 197-201.
    • (1971) Anal. Biochem. , vol.39 , pp. 197-201
    • Hinegardner, R.T.1
  • 19
    • 0018375735 scopus 로고
    • Hepatocte differentiation in culture. Appearance of tyrosine aminotransferase
    • Yeoh, G.C.T., Bennett, F.A. & Oliver, I.T. (1979) Hepatocte differentiation in culture. Appearance of tyrosine aminotransferase. Biochem. J. 180, 153-160.
    • (1979) Biochem. J. , vol.180 , pp. 153-160
    • Yeoh, G.C.T.1    Bennett, F.A.2    Oliver, I.T.3
  • 21
    • 0024240556 scopus 로고
    • Process of carbonyl iron absorption from the rat duodenal mucosa
    • Nakamura, T., Mori, M. & Awai, M. (1988) Process of carbonyl iron absorption from the rat duodenal mucosa. Acta Physiol. Jpn. 38, 1377-1390.
    • (1988) Acta Physiol. Jpn. , vol.38 , pp. 1377-1390
    • Nakamura, T.1    Mori, M.2    Awai, M.3
  • 22
    • 0036129599 scopus 로고    scopus 로고
    • Acquisition, storage and release of iron by cultured hepatoma cells
    • Hirsh, M., Konijn, A.M. & Iancu, T.C. (2002) Acquisition, storage and release of iron by cultured hepatoma cells. J. Hepatol. 36, 30-38.
    • (2002) J. Hepatol. , vol.36 , pp. 30-38
    • Hirsh, M.1    Konijn, A.M.2    Iancu, T.C.3
  • 23
    • 0023804636 scopus 로고
    • Characteristics of iron exchange between transferrin and hepatocytes in culture
    • Fucharoen, S., Rawley, P.T. & Paul, N.W., eds. Alan R. Liss, New York, USA
    • Baker, E., Trinder, D., Torrance, J., Page, M. & Morgan, E.H. (1988) Characteristics of iron exchange between transferrin and hepatocytes in culture. In Thalassaemia, Pathophysiology and Management (Fucharoen, S., Rawley, P.T. & Paul, N.W., eds), pp. 41-61. Alan R. Liss, New York, USA.
    • (1988) Thalassaemia, Pathophysiology and Management , pp. 41-61
    • Baker, E.1    Trinder, D.2    Torrance, J.3    Page, M.4    Morgan, E.H.5
  • 24
    • 0025151812 scopus 로고
    • Effect of cellular iron concentration on iron uptake by hepatocytes
    • Trinder, D., Batey, R., Morgan, E.H. & Baker, E. (1990) Effect of cellular iron concentration on iron uptake by hepatocytes. Am. J. Physiol. 259, G611-G617.
    • (1990) Am. J. Physiol. , vol.259
    • Trinder, D.1    Batey, R.2    Morgan, E.H.3    Baker, E.4
  • 25
    • 0026575576 scopus 로고
    • Evaluation of the iron chelation potential of hydrazones of pyridoxal, salicylaldehyde and 2-hydroxy-1-naphthylaldehyde using the hepatocyte in culture
    • Baker, E., Richardson, D.R., Gross, S. & Ponka, P. (1992) Evaluation of the iron chelation potential of hydrazones of pyridoxal, salicylaldehyde and 2-hydroxy-1-naphthylaldehyde using the hepatocyte in culture. Hepatol. 15, 492-501.
    • (1992) Hepatol. , vol.15 , pp. 492-501
    • Baker, E.1    Richardson, D.R.2    Gross, S.3    Ponka, P.4
  • 26
    • 0032190945 scopus 로고    scopus 로고
    • Characterisation of citrate and iron citrate uptake by cultured rat hepatocytes
    • Graham, R.M., Morgan, E.H. & Baker, E. (1998) Characterisation of citrate and iron citrate uptake by cultured rat hepatocytes. J. Hepatol. 29, 603-613.
    • (1998) J. Hepatol. , vol.29 , pp. 603-613
    • Graham, R.M.1    Morgan, E.H.2    Baker, E.3
  • 27
    • 0030761075 scopus 로고    scopus 로고
    • Inhibition of uptake of transferrin-bound iron by hepatoma cells by non-transferrin bound iron
    • Trinder, D. & Morgan, E.H. (1997) Inhibition of uptake of transferrin-bound iron by hepatoma cells by non-transferrin bound iron. Hepatol. 26, 691-698.
    • (1997) Hepatol. , vol.26 , pp. 691-698
    • Trinder, D.1    Morgan, E.H.2
  • 28
    • 0001950424 scopus 로고    scopus 로고
    • New multidentate chelators for iron
    • Saratoga Publishing Group, Ponte Vedra, Florida, USA
    • O'Sullivan, B., Xu, J. & Raymond, K.N. (2000) New multidentate chelators for iron. In Iron Chelators: New Development Strategies, pp. 177-208. Saratoga Publishing Group, Ponte Vedra, Florida, USA.
    • (2000) Iron Chelators: New Development Strategies , pp. 177-208
    • O'Sullivan, B.1    Xu, J.2    Raymond, K.N.3
  • 29
    • 0033820935 scopus 로고    scopus 로고
    • The hydroxypyridononate Tren-(Me-3,2-HOPO) is a more orally active iron chelator than its bidentate analaogue
    • Yokel, R.A., Fredenburg, A.M., Durbin, P.W., Xu, J., Rayens, M.K. & Raymond, K.N. (2000) The hydroxypyridononate Tren-(Me-3,2-HOPO) is a more orally active iron chelator than its bidentate analaogue. J. Pharm. Sci. 89, 545-555.
    • (2000) J. Pharm. Sci. , vol.89 , pp. 545-555
    • Yokel, R.A.1    Fredenburg, A.M.2    Durbin, P.W.3    Xu, J.4    Rayens, M.K.5    Raymond, K.N.6
  • 30
    • 0028158768 scopus 로고
    • The effect of the iron (III) chelator, desferrioxamine, on iron and transferrin uptake by the human malignant melanoma cell
    • Richardson, D.R., Ponka, P. & 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.R.1    Ponka, P.2    Baker, E.3
  • 31
    • 0019990842 scopus 로고    scopus 로고
    • Hepatocytes iron kinetics in the rat explored with an iron chelator
    • Pippard, M.J., Johnson, D.K. & Finch, C.A. Hepatocytes iron kinetics in the rat explored with an iron chelator. Br. J. Haematol. 52, 221-224.
    • Br. J. Haematol. , vol.52 , pp. 221-224
    • Pippard, M.J.1    Johnson, D.K.2    Finch, C.A.3
  • 32
    • 0022976445 scopus 로고
    • Iron uptake and metabolism by hepatocytes
    • Morgan, E.H. & Baker, E. (1986) Iron uptake and metabolism by hepatocytes. Fed. Proc. 45, 2801-2816.
    • (1986) Fed. Proc. , vol.45 , pp. 2801-2816
    • Morgan, E.H.1    Baker, E.2
  • 33
    • 0027313329 scopus 로고
    • Effects of iron loading on uptake, speciation, and chelation of iron in cultured myocardial cells
    • Parkes, J.G., Hussain, R.A., Olivieri, N.F. & Templeton, D.M. (1993) Effects of iron loading on uptake, speciation, and chelation of iron in cultured myocardial cells. J. Laboratory Clin. Med. 122, 36-47.
    • (1993) J. Laboratory Clin. Med. , vol.122 , pp. 36-47
    • Parkes, J.G.1    Hussain, R.A.2    Olivieri, N.F.3    Templeton, D.M.4
  • 34
    • 0028933888 scopus 로고
    • Modulation of iron loading and chelation of the uptake of non-transferrin-bound iron by human liver cells
    • Parkes, J.G., Randell, E.W., Olivieri, N.F. & Templeton, D.M. (1995) Modulation of iron loading and chelation of the uptake of non-transferrin-bound iron by human liver cells. Biochim. Biophys. Acta 1243, 373-380.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 373-380
    • Parkes, J.G.1    Randell, E.W.2    Olivieri, N.F.3    Templeton, D.M.4
  • 36
    • 0028244452 scopus 로고
    • Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron
    • Randell, E.W., Parkes, J.G., Olivieri, N.F. & Templeton, D.M. (1994) Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron. J. Biol. Chem. 269, 16046-16053.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16046-16053
    • Randell, E.W.1    Parkes, J.G.2    Olivieri, N.F.3    Templeton, D.M.4
  • 37
    • 0028875152 scopus 로고
    • Identification of a mechanism of iron uptake by cells which is stimulated by hydroxyl radicals generated via the iron-catalysed Haber-Weiss reaction
    • Richardson, D.R. & Ponka, P. (1995) Identification of a mechanism of iron uptake by cells which is stimulated by hydroxyl radicals generated via the iron-catalysed Haber-Weiss reaction. Biochim. Biophys. Acta 1269, 105-114.
    • (1995) Biochim. Biophys. Acta , vol.1269 , pp. 105-114
    • Richardson, D.R.1    Ponka, P.2
  • 39
  • 40
    • 0032887054 scopus 로고    scopus 로고
    • Deferiprone (L1) associated neutropenia in beta thalassaemia major: An Indian experience
    • Pati, H.P. & Choudhury, V.P. (1999) Deferiprone (L1) associated neutropenia in beta thalassaemia major: an Indian experience. Eur. J. Haematol. 63, 267-268.
    • (1999) Eur. J. Haematol. , vol.63 , pp. 267-268
    • Pati, H.P.1    Choudhury, V.P.2
  • 42
    • 0035336822 scopus 로고    scopus 로고
    • The controversial role of deferiprone in the treatment of thalassemia
    • Richardson, D.R. (2001) The controversial role of deferiprone in the treatment of thalassemia. J. Laboratory Clin. Med. 137, 324-329.
    • (2001) J. Laboratory Clin. Med. , vol.137 , pp. 324-329
    • Richardson, D.R.1
  • 43
    • 0032820582 scopus 로고    scopus 로고
    • Sequential use of deferiprone and desferrioxamine in primary school children with thalassaemia major in Turkey
    • Aydinok, Y., Nisli, G., Kavakli, K., Coker, C., Kantar, M. & Cetingul, N. (1999) Sequential use of deferiprone and desferrioxamine in primary school children with thalassaemia major in Turkey. Acta Haematol. 102, 17-21.
    • (1999) Acta Haematol. , vol.102 , pp. 17-21
    • Aydinok, Y.1    Nisli, G.2    Kavakli, K.3    Coker, C.4    Kantar, M.5    Cetingul, N.6
  • 44
    • 0033025760 scopus 로고    scopus 로고
    • An investigation into variability in the therapeutic response to deferiprone in patients with thalassaemia major
    • Diav-Citrin, O., Anatackovic, G. & Koren, G. (1999) An investigation into variability in the therapeutic response to deferiprone in patients with thalassaemia major. Ther. Drug Monit. 21, 74-81.
    • (1999) Ther. Drug Monit. , vol.21 , pp. 74-81
    • Diav-Citrin, O.1    Anatackovic, G.2    Koren, G.3
  • 45
    • 0032771863 scopus 로고    scopus 로고
    • Efficacy and side effects of deferiprone (L1) in thalassaerma patients not compliant with deferoxamine
    • Taher, A., Chamoun, F.M., Koussa, S., Saad, M.A., Khoriaty, A.I., Neeman, R. & Mourad, F.H. (1999) Efficacy and side effects of deferiprone (L1) in thalassaerma patients not compliant with deferoxamine. Acta Haematol. 101, 173-177.
    • (1999) Acta Haematol. , vol.101 , pp. 173-177
    • Taher, A.1    Chamoun, F.M.2    Koussa, S.3    Saad, M.A.4    Khoriaty, A.I.5    Neeman, R.6    Mourad, F.H.7
  • 46
    • 0031784438 scopus 로고    scopus 로고
    • Combined therapy with deferiprone and desferrioxamine
    • Wonke, B., Wright, C. & Hoffbrand, A.V. (1998) Combined therapy with deferiprone and desferrioxamine. Br. J. Haematol. 361-364.
    • (1998) Br. J. Haematol. , pp. 361-364
    • Wonke, B.1    Wright, C.2    Hoffbrand, A.V.3
  • 48
    • 0032528402 scopus 로고    scopus 로고
    • The iron chelator L1 potentiates oxidative DNA damage in iron-loaded liver cells
    • Cragg, L., Hebbel, R.P., Miller, W., Solovery, A., Selby, S. & Enright, H. (1998) The iron chelator L1 potentiates oxidative DNA damage in iron-loaded liver cells. Blood 92, 632-638.
    • (1998) Blood , vol.92 , pp. 632-638
    • Cragg, L.1    Hebbel, R.P.2    Miller, W.3    Solovery, A.4    Selby, S.5    Enright, H.6


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