메뉴 건너뛰기




Volumn 17, Issue 4, 2004, Pages 443-450

Effects of AZT on cellular iron homeostasis

Author keywords

3 azido 3 deoxythymidine (AZT); chelatable; glycosylation; iron; transferrin receptor (TfR)

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; ERYTHROPOIETIN; IRON; MULTIDRUG RESISTANCE PROTEIN 1; PROTEINASE INHIBITOR; TRANSFERRIN RECEPTOR; ZIDOVUDINE;

EID: 3042801970     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:BIOM.0000029478.18225.a0     Document Type: Short Survey
Times cited : (6)

References (83)
  • 1
    • 0022212903 scopus 로고
    • Heme metabolism and erythropoiesis in abnormal iron states: Role of delta-aminolevulinic acid synthase and heme oxygenase
    • Abraham NG, Lutton JD, Levere RD. 1985 Heme metabolism and erythropoiesis in abnormal iron states: role of delta-aminolevulinic acid synthase and heme oxygenase. Exp Hematol 13, 838-843.
    • (1985) Exp Hematol , vol.13 , pp. 838-843
    • Abraham, N.G.1    Lutton, J.D.2    Levere, R.D.3
  • 2
    • 0027135249 scopus 로고
    • Evidence of in vitro development of drug resistance to azido-thymidine in T-lymphocytic leukemia cell lines (Jurkat E61/AZT-100) and in pediatric patients with HIV-infection
    • Avramis VI, Kwock R, Solorzano MM, Gomperts E. 1993 Evidence of in vitro development of drug resistance to azido-thymidine in T-lymphocytic leukemia cell lines (Jurkat E61/AZT-100) and in pediatric patients with HIV-infection. J AIDS 6, 1287-1296.
    • (1993) J AIDS , vol.6 , pp. 1287-1296
    • Avramis, V.I.1    Kwock, R.2    Solorzano, M.M.3    Gomperts, E.4
  • 3
    • 0023868605 scopus 로고
    • The in vitro and in vivo antiretrovirus activity, and intracellular metabolism of 3′-azido-2′,3′-dideoxythymidine and 2′,3′-dideoxycithydine are highly dependent on the cell species
    • Balzarini J, Pauwels R, Baba M, et al. 1988 The in vitro and in vivo antiretrovirus activity, and intracellular metabolism of 3′-azido- 2′,3′-dideoxythymidine and 2′,3′-dideoxycithydine are highly dependent on the cell species. Biochem Pharmacol 37, 897-903.
    • (1988) Biochem Pharmacol , vol.37 , pp. 897-903
    • Balzarini, J.1    Pauwels, R.2    Baba, M.3
  • 4
    • 0030045401 scopus 로고    scopus 로고
    • Altered iron metabolism in HIV infection: Mechanism, possible consequences, and proposals for management
    • Boelaert JR, Weinberg GA, Weinberg ED. 1996 Altered iron metabolism in HIV infection: Mechanism, possible consequences, and proposals for management. Infect Agents Dis 5, 36-16.
    • (1996) Infect Agents Dis , vol.5 , pp. 36-116
    • Boelaert, J.R.1    Weinberg, G.A.2    Weinberg, E.D.3
  • 5
    • 0028834446 scopus 로고
    • Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron (II)
    • Breuer W, Epsztejn S, Cabantchik ZI. 1995 Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron (II). J Biol Chem 270, 24209-24215.
    • (1995) J Biol Chem , vol.270 , pp. 24209-24215
    • Breuer, W.1    Epsztejn, S.2    Cabantchik, Z.I.3
  • 6
    • 0029937713 scopus 로고    scopus 로고
    • Dynamics of the cytosolic chelatable iron pool of K562 cells
    • Brever W, Epsztejn S, Cabantchik ZI. 1996 Dynamics of the cytosolic chelatable iron pool of K562 cells. FEBS Lett 382, 304-308.
    • (1996) FEBS Lett , vol.382 , pp. 304-308
    • Brever, W.1    Epsztejn, S.2    Cabantchik, Z.I.3
  • 7
    • 0029865226 scopus 로고    scopus 로고
    • 3′-azido-3′-deoxythymidine inhibits erythroid-specific transcription factors in human erythroid K562 leukemia cells
    • Bridges EG, Trentesaux C, Lahlil R, Spiga MG, Jeannesson P, Sommadossi JP. 1996 3′-azido-3′-deoxythymidine inhibits erythroid-specific transcription factors in human erythroid K562 leukemia cells. Eur J Haematol 56, 62-67.
    • (1996) Eur J Haematol , vol.56 , pp. 62-67
    • Bridges, E.G.1    Trentesaux, C.2    Lahlil, R.3    Spiga, M.G.4    Jeannesson, P.5    Sommadossi, J.P.6
  • 8
    • 0023882711 scopus 로고
    • Iron-responsive elements: Regulatory RNA sequences that control mRNA levels and translation
    • Casey JL, Hentze MW, Koeller DM, et al. 1988 Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation. Science 240, 924-928.
    • (1988) Science , vol.240 , pp. 924-928
    • Casey, J.L.1    Hentze, M.W.2    Koeller, D.M.3
  • 9
    • 0027506202 scopus 로고
    • Induction of multidrug resistance in human cells by transient exposure to different chemotherapeutic drugs
    • Chaudary PM and Roninson IB. 1993 Induction of multidrug resistance in human cells by transient exposure to different chemotherapeutic drugs. J Natl Cancer Inst 85, 632-639.
    • (1993) J Natl Cancer Inst , vol.85 , pp. 632-639
    • Chaudary, P.M.1    Roninson, I.B.2
  • 10
    • 0021213545 scopus 로고
    • Molecular basis of the antineoplastic activity of 3′-amino- 3′-deoxythymidine
    • Chen MS, Woods KL, Prusoff WH. 1984 Molecular basis of the antineoplastic activity of 3′-amino-3′-deoxythymidine. Mol Pharmacol 25, 441-445.
    • (1984) Mol Pharmacol , vol.25 , pp. 441-445
    • Chen, M.S.1    Woods, K.L.2    Prusoff, W.H.3
  • 11
    • 0023189465 scopus 로고
    • Human immunodeficiency virus reverse transcriptase: General properties and its interactions with nucleoside triphosphate analogs
    • Cheng YC, Dutschman GE, Bastow KF, Sarngadharan MG, Ting RY. 1987 Human immunodeficiency virus reverse transcriptase: general properties and its interactions with nucleoside triphosphate analogs. J Biol Chem 262, 2187-2189.
    • (1987) J Biol Chem , vol.262 , pp. 2187-2189
    • Cheng, Y.C.1    Dutschman, G.E.2    Bastow, K.F.3    Sarngadharan, M.G.4    Ting, R.Y.5
  • 12
    • 0025914297 scopus 로고
    • GATA-1 transactivates erythropoietin receptor gene, and erythropoietin receptor-mediated signals enhance GATA-1 gene expression
    • Chiba T, Ikawa Y, Todokoro K. 1991 GATA-1 transactivates erythropoietin receptor gene, and erythropoietin receptor-mediated signals enhance GATA-1 gene expression. Nucleic Acids Res 19, 3843-3848.
    • (1991) Nucleic Acids Res , vol.19 , pp. 3843-3848
    • Chiba, T.1    Ikawa, Y.2    Todokoro, K.3
  • 13
    • 0028249115 scopus 로고
    • The MDR super-family of genes and its biological implications
    • De Vita VT, Hellmann S, Rosenberg SA eds. JB Lippincott Co, Philadelphia
    • Childs S and Ling V. 1994 The MDR super-family of genes and its biological implications. In: De Vita VT, Hellmann S, Rosenberg SA eds. Important Advances in Oncology. JB Lippincott Co, Philadelphia: 21-36.
    • (1994) Important Advances in Oncology , pp. 21-36
    • Childs, S.1    Ling, V.2
  • 14
    • 0026019284 scopus 로고
    • Sensitivity of erythroid progenitor colonies to erythropoietin in azidothymidine treated immunodeficient mice
    • Chow FPR, Sutton PA, Hamburger AW. 1991 Sensitivity of erythroid progenitor colonies to erythropoietin in azidothymidine treated immunodeficient mice. Br J Haematol 77, 139-144.
    • (1991) Br J Haematol , vol.77 , pp. 139-144
    • Chow, F.P.R.1    Sutton, P.A.2    Hamburger, A.W.3
  • 15
    • 0026071379 scopus 로고
    • Catabolism of 3′-azido-3′-deoxythymidine in hepatocytes and liver microsomes, with evidence of formation of 3′-amino-3′- deoxythymidine, a highly toxic catabolite for human bone marrow cells
    • Cretton EM, Xie MY, Bevan RJ, Goudgaon NM, Schinazi RF, Sommadossi JP. 1991 Catabolism of 3′-azido-3′-deoxythymidine in hepatocytes and liver microsomes, with evidence of formation of 3′-amino-3′- deoxythymidine, a highly toxic catabolite for human bone marrow cells. Mol Pharmacol 39, 258-266.
    • (1991) Mol Pharmacol , vol.39 , pp. 258-266
    • Cretton, E.M.1    Xie, M.Y.2    Bevan, R.J.3    Goudgaon, N.M.4    Schinazi, R.F.5    Sommadossi, J.P.6
  • 16
    • 0032983429 scopus 로고    scopus 로고
    • 3′-azido-3′-deoxythymidine reduces the rate of transferrin receptor endocytosis in K562 cells
    • D'Alessandro AM, D'Andrea G, Di Ciccio L, et al. 1999 3′-azido-3′-deoxythymidine reduces the rate of transferrin receptor endocytosis in K562 cells. Biochim Biophys Acta 1450, 232-241.
    • (1999) Biochim Biophys Acta , vol.1450 , pp. 232-241
    • D'Alessandro, A.M.1    D'Andrea, G.2    Di Ciccio, L.3
  • 17
    • 0033839223 scopus 로고    scopus 로고
    • Evidences that zidovudine (AZT) could not be directly responsible for iron overload in AZT-treated patients: An in vitro study
    • D'Alessandro AM, Rinaldi AC, D'Andrea G, et al. 2000 Evidences that zidovudine (AZT) could not be directly responsible for iron overload in AZT-treated patients: an in vitro study. Clin Chim Acta 300, 119-130.
    • (2000) Clin Chim Acta , vol.300 , pp. 119-130
    • D'Alessandro, A.M.1    Rinaldi, A.C.2    D'Andrea, G.3
  • 18
    • 3042859021 scopus 로고    scopus 로고
    • Effect of AZT on human transfenin receptor sislylation process in K562 cells
    • World Congress on Iron Metabolism. Sorrento, Italy
    • D'Andrea G, D'Alessandro AM, Brisdelli F, et al. 1999 Effect of AZT on human transfenin receptor sislylation process in K562 cells. In: World Congress on Iron Metabolism. Bioiron 99, Sorrento, Italy.
    • (1999) Bioiron 99
    • D'Andrea, G.1    D'Alessandro, A.M.2    Brisdelli, F.3
  • 20
    • 0141728493 scopus 로고    scopus 로고
    • Protein glycans alteration and a different distribution of some enzymatic activities involved in the glycan processing are found in AZT-treated K562 cells
    • D'Andrea G, Lizzi AR, Brisdelli F, D'Alessandro AM, Bozzi A, Oratore A. 2003 Protein glycans alteration and a different distribution of some enzymatic activities involved in the glycan processing are found in AZT-treated K562 cells. Mol Cell Biochem 252, 45-51.
    • (2003) Mol Cell Biochem , vol.252 , pp. 45-51
    • D'Andrea, G.1    Lizzi, A.R.2    Brisdelli, F.3    D'Alessandro, A.M.4    Bozzi, A.5    Oratore, A.6
  • 22
    • 0030725330 scopus 로고    scopus 로고
    • Intracellular metabolism of 3′-azido-3′-deoxythymidine (AZT): A Nuclear Magnetic Resonance study on T-lymphoblastoid cell lines with different resistance to AZT
    • Di Vito M, Bozzi A, Ferretti A, et al. 1997 Intracellular metabolism of 3′-azido-3′-deoxythymidine (AZT): A Nuclear Magnetic Resonance study on T-lymphoblastoid cell lines with different resistance to AZT. Biochem Phannacol 54, 979-990.
    • (1997) Biochem Phannacol , vol.54 , pp. 979-990
    • Di Vito, M.1    Bozzi, A.2    Ferretti, A.3
  • 23
    • 0028149110 scopus 로고
    • Zidovudine induces the expression of cellular resistance affecting its antiviral activity
    • Dianzani F, Antonelli G, Turriziani O, et al. 1994 Zidovudine induces the expression of cellular resistance affecting its antiviral activity. AIDS Res Hum Retrov 10, 1471-1478.
    • (1994) AIDS Res Hum Retrov , vol.10 , pp. 1471-1478
    • Dianzani, F.1    Antonelli, G.2    Turriziani, O.3
  • 24
    • 0023924092 scopus 로고
    • Purine nucleo-base transport in human erythrocytes: Reinvestigation with a novel 'inhibitor-stop' assay
    • Domin BA, Mahony WB, Zimmerman TP. 1988 Purine nucleo-base transport in human erythrocytes: reinvestigation with a novel 'inhibitor-stop' assay. J Biol Chem 263, 9276-9284.
    • (1988) J Biol Chem , vol.263 , pp. 9276-9284
    • Domin, B.A.1    Mahony, W.B.2    Zimmerman, T.P.3
  • 25
    • 0022996630 scopus 로고
    • Phosphorylation of 3′-azido-3′-deoxythymidine and selective interaction of the 5′-triphosphate with human immunodeficiency virus reverse transcriptase
    • Furman PA, Fyfe JA, St. Clair MH. 1986 Phosphorylation of 3′-azido-3′-deoxythymidine and selective interaction of the 5′-triphosphate with human immunodeficiency virus reverse transcriptase. Proc Natl Acad Sci USA 83, 8333-8337.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8333-8337
    • Furman, P.A.1    Fyfe, J.A.2    St. Clair, M.H.3
  • 27
    • 0023636395 scopus 로고
    • Azidothymidine associated with bone marrow failure in the acquired immunodeficiency syndrome (AIDS)
    • Gill PS, Rarick M, Brynes RK, Causey D, Loureiro C, Levine AM. 1987 Azidothymidine associated with bone marrow failure in the acquired immunodeficiency syndrome (AIDS). Ann Intern Med 107, 502-505.
    • (1987) Ann Intern Med , vol.107 , pp. 502-505
    • Gill, P.S.1    Rarick, M.2    Brynes, R.K.3    Causey, D.4    Loureiro, C.5    Levine, A.M.6
  • 28
    • 0026785019 scopus 로고
    • Zidovudine-induced blockade of the expression and function of the erythropoietin receptor
    • Gogu SR, Malter JS, Agrawal KC. 1992 Zidovudine-induced blockade of the expression and function of the erythropoietin receptor. Biochem Pharmacol 44, 1009-1012.
    • (1992) Biochem Pharmacol , vol.44 , pp. 1009-1012
    • Gogu, S.R.1    Malter, J.S.2    Agrawal, K.C.3
  • 29
    • 0027453751 scopus 로고
    • Iron overload in multiply transfused patients who are HIV seropositive
    • Goldin RD, Wilkins M, Dourakis S, Parkin J, Lindley R. 1993 Iron overload in multiply transfused patients who are HIV seropositive. J Clin Pathol 46, 1036-1038.
    • (1993) J Clin Pathol , vol.46 , pp. 1036-1038
    • Goldin, R.D.1    Wilkins, M.2    Dourakis, S.3    Parkin, J.4    Lindley, R.5
  • 30
    • 0025276615 scopus 로고
    • Isolation and characterization of an ether glucuronide of zidovudine, a major metabolite in monkeys and humans
    • Good SS, Koble CS, Crouch R, Johnson RL, Rideout JL, de Miranda P. 1990 Isolation and characterization of an ether glucuronide of zidovudine, a major metabolite in monkeys and humans. Drug Metab Dispos 18, 321-326.
    • (1990) Drug Metab Dispos , vol.18 , pp. 321-326
    • Good, S.S.1    Koble, C.S.2    Crouch, R.3    Johnson, R.L.4    Rideout, J.L.5    De Miranda, P.6
  • 31
    • 0035139289 scopus 로고    scopus 로고
    • Iron status and the outcome of HIV infection: An overview
    • Gordeuk V, Delanghe J, Langlois M, Boelaert J. 2001 Iron status and the outcome of HIV infection: an overview. J Clin Virol 20, 111-115.
    • (2001) J Clin Virol , vol.20 , pp. 111-115
    • Gordeuk, V.1    Delanghe, J.2    Langlois, M.3    Boelaert, J.4
  • 32
    • 0030756793 scopus 로고    scopus 로고
    • Impact of transfusion on viral load in human immunodeficiency virus infection
    • Groopman J. 1997 Impact of transfusion on viral load in human immunodeficiency virus infection. Semin Hematol 34, 27-33.
    • (1997) Semin Hematol , vol.34 , pp. 27-33
    • Groopman, J.1
  • 33
    • 0028332852 scopus 로고
    • 3′-azido-3′-deoxythymidine potentially inhibits protein glycosylation
    • Hall ET, Yan JP, Melançon P, Kuchta RD. 1994 3′-azido- 3′-deoxythymidine potentially inhibits protein glycosylation. J Biol Chem 269, 14355-14358.
    • (1994) J Biol Chem , vol.269 , pp. 14355-14358
    • Hall, E.T.1    Yan, J.P.2    Melançon, P.3    Kuchta, R.D.4
  • 34
    • 0026788501 scopus 로고
    • Recombinant human erythropoietin in the treatment of anemia associated with HTV infection and zidovudine therapy. Overview of four clinical trials
    • Henry DH, Beall GN, Benson CA, et al. 1992 Recombinant human erythropoietin in the treatment of anemia associated with HTV infection and zidovudine therapy. Overview of four clinical trials. Ann Intern Med 117, 739-748.
    • (1992) Ann Intern Med , vol.117 , pp. 739-748
    • Henry, D.H.1    Beall, G.N.2    Benson, C.A.3
  • 35
    • 0000112890 scopus 로고
    • Kaposi's sarcoma in patients infected with human virus (HIV): An overview
    • Hermans P and Clumeck N. 1995 Kaposi's sarcoma in patients infected with human virus (HIV): an overview. Cell Mol Biol 3, 357-364.
    • (1995) Cell Mol Biol , vol.3 , pp. 357-364
    • Hermans, P.1    Clumeck, N.2
  • 37
    • 0020354532 scopus 로고
    • Transferrin receptors and iron uptake during erythroid development
    • Jacopetta BJ, Morgan EH, Yeoh GCT. 1982 Transferrin receptors and iron uptake during erythroid development. Biochim Biophys Acta 687, 204-210.
    • (1982) Biochim Biophys Acta , vol.687 , pp. 204-210
    • Jacopetta, B.J.1    Morgan, E.H.2    Yeoh, G.C.T.3
  • 38
    • 73649205621 scopus 로고
    • The plasma-to-cell cycle of transferrin
    • Jandl JH and Katz JH. 1963 The plasma-to-cell cycle of transferrin. J Clin Invest 42, 314-326.
    • (1963) J Clin Invest , vol.42 , pp. 314-326
    • Jandl, J.H.1    Katz, J.H.2
  • 39
    • 0020578356 scopus 로고
    • Cell surface P-glycoprotein associated with multidrug resistance in mammalian cell lines
    • Kartner N, Riordan JR, Ling V. 1983 Cell surface P-glycoprotein associated with multidrug resistance in mammalian cell lines. Science 221, 1058-1088.
    • (1983) Science , vol.221 , pp. 1058-1088
    • Kartner, N.1    Riordan, J.R.2    Ling, V.3
  • 40
    • 0025344525 scopus 로고
    • Mechanism of HIV reverse transcriptase: Enzyme-primer interaction as revealed through studies of a dNTP analogue, 3′-azidothymidine-5′- triphosphate
    • Kedar PS, Abbots J, Kovacs T, Lesiak K, Torrence W, Wilson SH. 1990 Mechanism of HIV reverse transcriptase: enzyme-primer interaction as revealed through studies of a dNTP analogue, 3′-azidothymidine-5′- triphosphate. Biochemistry 29, 3603-3611.
    • (1990) Biochemistry , vol.29 , pp. 3603-3611
    • Kedar, P.S.1    Abbots, J.2    Kovacs, T.3    Lesiak, K.4    Torrence, W.5    Wilson, S.H.6
  • 42
    • 0030780871 scopus 로고    scopus 로고
    • Pathogenesis and pathophysiology of anemia in HIV infection
    • Kreutzer KA and Rockstrom JK. 1997 Pathogenesis and pathophysiology of anemia in HIV infection. Ann Hematol 75, 179-187.
    • (1997) Ann Hematol , vol.75 , pp. 179-187
    • Kreutzer, K.A.1    Rockstrom, J.K.2
  • 43
    • 0024654431 scopus 로고
    • Zidovudine. A review of its pharmacodynamic and pharmacokinetic properties, and therapeutic efficacy
    • Langtry HD and Campoli-Richards DM. 1989 Zidovudine. A review of its pharmacodynamic and pharmacokinetic properties, and therapeutic efficacy. Drugs 37, 408-450.
    • (1989) Drugs , vol.37 , pp. 408-450
    • Langtry, H.D.1    Campoli-Richards, D.M.2
  • 45
    • 0024419785 scopus 로고
    • Iron deposition in liver in zidovudine-related transfusion-dependent anaemia
    • Lindley R, Parkin J, Dourakis S, Goldin R. 1989 Iron deposition in liver in zidovudine-related transfusion-dependent anaemia. Lancet 11, 681.
    • (1989) Lancet , vol.11 , pp. 681
    • Lindley, R.1    Parkin, J.2    Dourakis, S.3    Goldin, R.4
  • 46
    • 0030569292 scopus 로고    scopus 로고
    • AZT-induced hypermethylation of human thymidine kinase gene in the absence of total DNA hypermethylation
    • Lucarelli M, Palitti M, Carotti D, et al. 1996 AZT-induced hypermethylation of human thymidine kinase gene in the absence of total DNA hypermethylation. FEBS Lett 396, 323-326.
    • (1996) FEBS Lett , vol.396 , pp. 323-326
    • Lucarelli, M.1    Palitti, M.2    Carotti, D.3
  • 47
    • 0034993236 scopus 로고    scopus 로고
    • Symptomatology of anemia
    • Ludwig H and Strasser K. 2001 Symptomatology of anemia. Semin Oncol 28, 7-14.
    • (2001) Semin Oncol , vol.28 , pp. 7-14
    • Ludwig, H.1    Strasser, K.2
  • 49
    • 0024560650 scopus 로고
    • Increased γ-globin expression in a nondeletion HPFH mediated by an erythroid-specific DNA-binding factor
    • Martin DK, Tsai SF, Orkin SH. 1989 Increased γ-globin expression in a nondeletion HPFH mediated by an erythroid-specific DNA-binding factor. Nature 338, 435-438.
    • (1989) Nature , vol.338 , pp. 435-438
    • Martin, D.K.1    Tsai, S.F.2    Orkin, S.H.3
  • 50
    • 0027751714 scopus 로고
    • Iron regulatory factor - The conductor of cellular iron regulation
    • Melefors Ö and Hentze MW. 1993 Iron regulatory factor - the conductor of cellular iron regulation. Blood Rev 7, 251-258.
    • (1993) Blood Rev , vol.7 , pp. 251-258
    • Melefors, Ö.1    Hentze, M.W.2
  • 51
    • 0024365045 scopus 로고
    • A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA
    • Müllner EW, Neupert B, Kühn LC. 1989 A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA. Cell 58, 373-382.
    • (1989) Cell , vol.58 , pp. 373-382
    • Müllner, E.W.1    Neupert, B.2    Kühn, L.C.3
  • 52
    • 0024371560 scopus 로고
    • Increased erythroid-specific expression of a mutated HPFH γ-globin promoter requires the erythroid factor GATA-1
    • Nicolis S, Ronchi A, Malgaretti N, Mantovani R, Giglioni B, Ottolenghi S. 1989 Increased erythroid-specific expression of a mutated HPFH γ-globin promoter requires the erythroid factor GATA-1. Nucleic Acids Res 17, 5509-5516.
    • (1989) Nucleic Acids Res , vol.17 , pp. 5509-5516
    • Nicolis, S.1    Ronchi, A.2    Malgaretti, N.3    Mantovani, R.4    Giglioni, B.5    Ottolenghi, S.6
  • 53
    • 0025954915 scopus 로고
    • An erythroid specific enhancer upstream to the gene encoding the cell-type specific transcription factor GATA-1
    • Nicolis S, Bertini C, Ronchi A, et al. 1991 An erythroid specific enhancer upstream to the gene encoding the cell-type specific transcription factor GATA-1. Nucleic Acids Res 19, 5285-5291.
    • (1991) Nucleic Acids Res , vol.19 , pp. 5285-5291
    • Nicolis, S.1    Bertini, C.2    Ronchi, A.3
  • 54
    • 0027530945 scopus 로고
    • Epigenetic mechanisms of drug resistance: Drug-induced DNA hypermethylation and drug resistance
    • Nyce J, Leonard S, Canupp D, Schulz S, Wong S. 1993 Epigenetic mechanisms of drug resistance: drug-induced DNA hypermethylation and drug resistance. Proc Natl Acad Sci USA 90, 2960-2964.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2960-2964
    • Nyce, J.1    Leonard, S.2    Canupp, D.3    Schulz, S.4    Wong, S.5
  • 55
    • 0023336087 scopus 로고
    • Noncoding 3′ sequences of the transferrin receptor gene are required for mRNA regulation by iron
    • Owen D and Kühn LC. 1987 Noncoding 3′ sequences of the transferrin receptor gene are required for mRNA regulation by iron. EMBO J 6, 1287-1293.
    • (1987) EMBO J , vol.6 , pp. 1287-1293
    • Owen, D.1    Kühn, L.C.2
  • 56
    • 0020376041 scopus 로고
    • Hemin regulates the expression of transferrin receptors in human hematopoietic cell lines
    • Pelicci PG, Tabilio A, Thomopoulos P. 1982 Hemin regulates the expression of transferrin receptors in human hematopoietic cell lines. FEBS Lett 145, 350-354.
    • (1982) FEBS Lett , vol.145 , pp. 350-354
    • Pelicci, P.G.1    Tabilio, A.2    Thomopoulos, P.3
  • 57
    • 0022480663 scopus 로고
    • Expression of transferrin receptors in human erythroleukemia lines: Regulation in the plateau and exponential phase of growth
    • Pelosi-Testa E, Testa U, Samoggia G, Salvo A, Camagna A, Peschle C. 1986 Expression of transferrin receptors in human erythroleukemia lines: Regulation in the plateau and exponential phase of growth. Cancer Res 46, 5330-5334.
    • (1986) Cancer Res , vol.46 , pp. 5330-5334
    • Pelosi-Testa, E.1    Testa, U.2    Samoggia, G.3    Salvo, A.4    Camagna, A.5    Peschle, C.6
  • 58
    • 0027273553 scopus 로고
    • Azidothymidine (AZT)-induced siderosis
    • Pollack S and Weaver J. 1993 Azidothymidine (AZT)-induced siderosis. Am J Hematol 43, 230-233.
    • (1993) Am J Hematol , vol.43 , pp. 230-233
    • Pollack, S.1    Weaver, J.2
  • 59
    • 0024577652 scopus 로고
    • Glucuronidation of 3′-azido-3′-deoxythymidine: Human and rat enzyme specificity
    • Resetar A and Spector T. 1989 Glucuronidation of 3′-azido-3′- deoxythymidine: human and rat enzyme specificity. Biochem Pharmacol, 1389-1393.
    • (1989) Biochem Pharmacol , pp. 1389-1393
    • Resetar, A.1    Spector, T.2
  • 60
    • 0023266214 scopus 로고
    • The toxicity of azidothymidine (AZT) in the treatment of patients with AIDS and AIDS-related complex: A double-blind placebo-controlled trial
    • Richmann DD, Fischl MA, Grieco MH, et al. 1987 The toxicity of azidothymidine (AZT) in the treatment of patients with AIDS and AIDS-related complex: a double-blind placebo-controlled trial. N Engl J Med 317, 192-197.
    • (1987) N Engl J Med , vol.317 , pp. 192-197
    • Richmann, D.D.1    Fischl, M.A.2    Grieco, M.H.3
  • 61
    • 0026710009 scopus 로고
    • The role of iron in oxygen-mediated toxicities
    • Ryan TR and Aust SD. 1992 The role of iron in oxygen-mediated toxicities. Crit Rev Toxicol 22, 119-141.
    • (1992) Crit Rev Toxicol , vol.22 , pp. 119-141
    • Ryan, T.R.1    Aust, S.D.2
  • 62
    • 0032529609 scopus 로고    scopus 로고
    • Serum ferritin, desferrioxamine, and evolution of HPV-1 infection in thalassemic patients
    • Salhi Y, Costagliola D, Rebulla P, et al. 1998 Serum ferritin, desferrioxamine, and evolution of HPV-1 infection in thalassemic patients. J AIDS Hum Retrovirol 18, 473-478.
    • (1998) J AIDS Hum Retrovirol , vol.18 , pp. 473-478
    • Salhi, Y.1    Costagliola, D.2    Rebulla, P.3
  • 63
    • 0026210867 scopus 로고
    • Multidrug resistance mediated by P-glycoproteins
    • Schinkel AH and Borst P. 1991 Multidrug resistance mediated by P-glycoproteins. Semin Cancer Biol 2, 213-226.
    • (1991) Semin Cancer Biol , vol.2 , pp. 213-226
    • Schinkel, A.H.1    Borst, P.2
  • 64
    • 0028952409 scopus 로고
    • Mechanism of transferrin receptor down-regulation in K562 cells in response to protein kinase C activation
    • Schonhorn JE, Akompong T, Wessling-Resnick M. 1995 Mechanism of transferrin receptor down-regulation in K562 cells in response to protein kinase C activation. J Biol Chem 270, 3698-3705.
    • (1995) J Biol Chem , vol.270 , pp. 3698-3705
    • Schonhorn, J.E.1    Akompong, T.2    Wessling-Resnick, M.3
  • 65
    • 0018579827 scopus 로고
    • Isolation and characterization of the transferrin receptor from human placenta
    • Seligman PA, Schleicher RB, Allen RH. 1979 Isolation and characterization of the transferrin receptor from human placenta. J Biol Chem 254, 9943-9946.
    • (1979) J Biol Chem , vol.254 , pp. 9943-9946
    • Seligman, P.A.1    Schleicher, R.B.2    Allen, R.H.3
  • 67
    • 0031975144 scopus 로고    scopus 로고
    • Epidemiology of anaemia in HTV-infected persons: Results from the multistate adult and adolescent spectrum of HIV disease surveillance project
    • Sullivan PS, Hanson DL, Chu SY, Jones JL, Ward JW. 1998 Epidemiology of anaemia in HTV-infected persons: Results from the multistate adult and adolescent spectrum of HIV disease surveillance project. Blood 91, 301-308.
    • (1998) Blood , vol.91 , pp. 301-308
    • Sullivan, P.S.1    Hanson, D.L.2    Chu, S.Y.3    Jones, J.L.4    Ward, J.W.5
  • 68
    • 0024991859 scopus 로고
    • Oxygen-derived free radicals in reperfusion injury
    • Sussman MS and Bulkley GB. 1990 Oxygen-derived free radicals in reperfusion injury. Methods Enzymol 186, 711-722.
    • (1990) Methods Enzymol , vol.186 , pp. 711-722
    • Sussman, M.S.1    Bulkley, G.B.2
  • 69
    • 0028920558 scopus 로고
    • Cytotoxicity of 3′-azido-3′-deoxythymidine correlates with 3′-azidothymidine-5′-monophosphate (AZTMP) levels, whereas anti-human immunodeficiency virus (HIV) activity correlated with 3′-azidothymidine-5′-triphosphate (AZTTP) levels in cultured CEM T-lymphoblastoid cells
    • Tornevik Y, Ullman B, Balzarini J, Wahren B, Eriksson S. 1995 cytotoxicity of 3′-azido-3′-deoxythymidine correlates with 3′-azidothymidine-5′-monophosphate (AZTMP) levels, whereas anti-human immunodeficiency virus (HIV) activity correlated with 3′-azidothymidine-5′-triphosphate (AZTTP) levels in cultured CEM T-lymphoblastoid cells. Biochem Pharmacol 49, 829-837.
    • (1995) Biochem Pharmacol , vol.49 , pp. 829-837
    • Tornevik, Y.1    Ullman, B.2    Balzarini, J.3    Wahren, B.4    Eriksson, S.5
  • 70
    • 0019570604 scopus 로고
    • Human cell surface glycoprotein related to cell proliferation is the receptor for transferrin
    • Trowbridge IS and Omary MB. 1981 Human cell surface glycoprotein related to cell proliferation is the receptor for transferrin. Proc Natl Acad Sci USA 78, 3039-3043.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3039-3043
    • Trowbridge, I.S.1    Omary, M.B.2
  • 71
    • 0033810233 scopus 로고    scopus 로고
    • Consensus statement: Anemia in HIV infection - Current trends, treatment options and practice strategies
    • Anemia in HIV Working Group
    • Volberding P. 2000 Consensus statement: anemia in HIV infection - Current trends, treatment options and practice strategies. Anemia in HIV Working Group. Clin Ther 22, 1004-1020.
    • (2000) Clin Ther , vol.22 , pp. 1004-1020
    • Volberding, P.1
  • 73
    • 0021719812 scopus 로고
    • Heme regulation of HeLa cell transferrin receptor number
    • Ward IH, Jordan I, Kushner JP, Kaplan J. 1984 Heme regulation of HeLa cell transferrin receptor number. J Biol Chem 259, 13235-13240.
    • (1984) J Biol Chem , vol.259 , pp. 13235-13240
    • Ward, I.H.1    Jordan, I.2    Kushner, J.P.3    Kaplan, J.4
  • 74
    • 0024473778 scopus 로고
    • Low-Mr iron isolated from guinea pig reticulocytes as AMP-Fe and ATP-Fe complexes
    • Weaver J and Pollack S. 1989 Low-Mr iron isolated from guinea pig reticulocytes as AMP-Fe and ATP-Fe complexes. Biochem J 261, 787-792.
    • (1989) Biochem J , vol.261 , pp. 787-792
    • Weaver, J.1    Pollack, S.2
  • 75
    • 0025061013 scopus 로고
    • Mitochondria have Fe (III) receptors
    • Weaver J, Zhan H, Pollack S. 1990 Mitochondria have Fe (III) receptors. Biochem J 265, 415-419.
    • (1990) Biochem J , vol.265 , pp. 415-419
    • Weaver, J.1    Zhan, H.2    Pollack, S.3
  • 76
    • 0025694701 scopus 로고
    • 3′-azido-3′-deoxythymidine inhibits globin gene transcription in butyric acid-induced K562 human leukemia cells
    • Weider DA and Sommadossi JP. 1990 3′-azido-3′-deoxythymidine inhibits globin gene transcription in butyric acid-induced K562 human leukemia cells. Mol Pharmacol 38, 397-804.
    • (1990) Mol Pharmacol , vol.38 , pp. 397-804
    • Weider, D.A.1    Sommadossi, J.P.2
  • 77
    • 0026605083 scopus 로고
    • Comparative effects of 3′-azido-3′-deoxythymidine and its metabolite, 3′-amino-3′-deoxythymidine, on hemoglobin synthesis in K562 human leukemia cells
    • Weidner DA and Sommadossi JP. 1991 Comparative effects of 3′-azido-3′-deoxythymidine and its metabolite, 3′-amino- 3′-deoxythymidine, on hemoglobin synthesis in K562 human leukemia cells. Mol Pharmacol 41, 252-258.
    • (1991) Mol Pharmacol , vol.41 , pp. 252-258
    • Weidner, D.A.1    Sommadossi, J.P.2
  • 78
    • 0028815254 scopus 로고
    • Development of zidovudine (AZT) resistance in Jurkat T cells is associated with decreased expression of the thymidine kinase (TK) gene and hypermethylation of the 5′ end of human TK gene
    • Wu S, Liu X, Solorzano MM, Kwock R, Avramis VI. 1995 Development of zidovudine (AZT) resistance in Jurkat T cells is associated with decreased expression of the thymidine kinase (TK) gene and hypermethylation of the 5′ end of human TK gene. J AIDS Hum Retrovirol 8, 1-9.
    • (1995) J AIDS Hum Retrovirol , vol.8 , pp. 1-9
    • Wu, S.1    Liu, X.2    Solorzano, M.M.3    Kwock, R.4    Avramis, V.I.5
  • 79
    • 0029157098 scopus 로고
    • Azidothymidine (Zidovudine) inhibits glycosylation and dramatically alters glycosphingolipid synthesis in whole cells at clinically relevant concentrations
    • Yan JP, Ilsley D, Frohlick C, et al. 1995 Azidothymidine (Zidovudine) inhibits glycosylation and dramatically alters glycosphingolipid synthesis in whole cells at clinically relevant concentrations. J Biol Chem 270, 22836-22841.
    • (1995) J Biol Chem , vol.270 , pp. 22836-22841
    • Yan, J.P.1    Ilsley, D.2    Frohlick, C.3
  • 80
    • 0024436217 scopus 로고
    • Clinical pharmacology of 3′-azido-2′,3′- dideoxythymidine (zidovudine) and related dideoxynucleosides
    • Yarchoan R, Mitsuya H, Myers CE, Broder S. 1989 Clinical pharmacology of 3′-azido-2′,3′-dideoxythymidine (zidovudine) and related dideoxynucleosides. N Engl J Med 321, 726-738.
    • (1989) N Engl J Med , vol.321 , pp. 726-738
    • Yarchoan, R.1    Mitsuya, H.2    Myers, C.E.3    Broder, S.4
  • 81
    • 0028120808 scopus 로고
    • Iterative endocytosis of transferrin by K562 cells
    • Young SP and Bomford A. 1994 Iterative endocytosis of transferrin by K562 cells. Biochem J 298, 165-170.
    • (1994) Biochem J , vol.298 , pp. 165-170
    • Young, S.P.1    Bomford, A.2
  • 83
    • 0023258934 scopus 로고
    • 3′-azido-3′-deoxythymidine: An unusual nucleoside analog that permeates the membrane of human erythrocytes and lymphocytes by non-facilitated diffusion
    • Zimmerman TP, Mahony WB, Prus KL. 1987 3′-azido-3′- deoxythymidine: an unusual nucleoside analog that permeates the membrane of human erythrocytes and lymphocytes by non-facilitated diffusion. J Biol Chem 262, 5748-5754.
    • (1987) J Biol Chem , vol.262 , pp. 5748-5754
    • Zimmerman, T.P.1    Mahony, W.B.2    Prus, K.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.