메뉴 건너뛰기




Volumn 55, Issue 69, 1999, Pages

Cellular iron metabolism

Author keywords

Endosomal acidification; Heme biosynthesis; Iron metabolism; Oxidative stress; Toxic oxygen radicals; Transferrin

Indexed keywords

FERRITIN; HEME; IRON; IRON REGULATORY FACTOR; MESSENGER RNA; OXYGEN RADICAL; TRANSFERRIN; IRON REGULATORY PROTEIN 1; IRON REGULATORY PROTEIN 2; IRON SULFUR PROTEIN; RNA BINDING PROTEIN; TRANSFERRIN RECEPTOR;

EID: 0032964289     PISSN: 00986577     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1523-1755.1999.055suppl.69002.x     Document Type: Review
Times cited : (210)

References (62)
  • 1
    • 0242303463 scopus 로고
    • Iron-dependent enzymes in mammalian systems
    • edited by PONKA P, SCHULMAN HM, WOODWORTH RD, Boca Raton, CRC Press
    • CAMMACK R, WRIGGLESWORTH JH, BAUM H: Iron-dependent enzymes in mammalian systems, in Iron Transport and Storage, edited by PONKA P, SCHULMAN HM, WOODWORTH RD, Boca Raton, CRC Press. 1990, p 17
    • (1990) Iron Transport and Storage , pp. 17
    • Cammack, R.1    Wrigglesworth, J.H.2    Baum, H.3
  • 2
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • RICHARDSON DR, PONKA P: The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim Biophys Acta 1331:1-40, 1997
    • (1997) Biochim Biophys Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 3
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: Distinct control mechanisms in erythroid cells
    • PONKA P: Tissue-specific regulation of iron metabolism and heme synthesis: Distinct control mechanisms in erythroid cells. Blood 89:1-25, 1997
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 4
    • 0031963449 scopus 로고    scopus 로고
    • Function and regulation of transferrin and ferritin
    • PONKA P, BEAUMONT C, RICHARDSON DR: Function and regulation of transferrin and ferritin. Semin Hematol 35:35-54, 1998
    • (1998) Semin Hematol , vol.35 , pp. 35-54
    • Ponka, P.1    Beaumont, C.2    Richardson, D.R.3
  • 5
    • 0031963619 scopus 로고    scopus 로고
    • Iron, free radicals and oxidative injury
    • McCORD J: Iron, free radicals and oxidative injury. Semin Hematol 35:5-12, 1998
    • (1998) Semin Hematol , vol.35 , pp. 5-12
    • Mccord, J.1
  • 6
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • HALLIWELL B, GUTTERIDGE JM: Role of free radicals and catalytic metal ions in human disease: An overview. Methods Enzymol 186:1-85, 1990
    • (1990) Methods Enzymol , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 7
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution
    • ANDERSON BF, BAKER HM, NORRIS GE, RICE DW, BAKER EN: Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution. J Mol Biol 209:711-734, 1989
    • (1989) J Mol Biol , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 8
    • 0026646617 scopus 로고
    • New perspectives on the structure and function of transferrin
    • BAKER EN, LINDLEY PF: New perspectives on the structure and function of transferrin. J Inorg Biochem 47:147-160, 1992
    • (1992) J Inorg Biochem , vol.47 , pp. 147-160
    • Baker, E.N.1    Lindley, P.F.2
  • 10
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • MAINES MD: The heme oxygenase system: A regulator of second messenger gases. Annu Rev Pharmacol Toxicol 37:517-554, 1997
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 12
    • 0028834446 scopus 로고
    • Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II)
    • BREUER W, EPSZTEIN S, CABANTCHIK ZI: Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II). J Biol Chem 270:24209-24215, 1995
    • (1995) J Biol Chem , vol.270 , pp. 24209-24215
    • Breuer, W.1    Epsztein, S.2    Cabantchik, Z.I.3
  • 13
    • 0028058038 scopus 로고
    • The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
    • ASKWITH C, EIDE D, VAN HO A, BERNARD PS, LIL, DAVIS-KAPLAN S, SIPE OH, KAPLAN J: The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76:403-410, 1994
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.1    Eide, D.2    Van Ho, A.3    Bernard, P.S.4    Lil5    Davis-Kaplan, S.6    Sipe, O.H.7    Kaplan, J.8
  • 15
    • 0028358438 scopus 로고
    • The relationship of erythropoietin and iron metabolism to red blood cell production in humans
    • ADAMSON JW: The relationship of erythropoietin and iron metabolism to red blood cell production in humans. Semin Oncol 21(Suppl 3):9-15, 1994
    • (1994) Semin Oncol , vol.21 , Issue.3 SUPPL. , pp. 9-15
    • Adamson, J.W.1
  • 16
    • 0018164919 scopus 로고
    • Non-specific serum iron in thalassemia: Abnormal serum iron fraction of potential toxicity
    • HERSHKO C, GRAHAM G, BATES GW, RACHMILEWITZ EA: Non-specific serum iron in thalassemia: Abnormal serum iron fraction of potential toxicity. Br J Haematol 40:255-263, 1978
    • (1978) Br J Haematol , vol.40 , pp. 255-263
    • Hershko, C.1    Graham, G.2    Bates, G.W.3    Rachmilewitz, E.A.4
  • 17
    • 0011938460 scopus 로고
    • Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse: A rodent model for hemochromatosis
    • CRAVEN CM, ALEXANDER J, ELDRIDGE M, KUSHNER HP, BERNSTEIN S. KAPLAN J: Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse: A rodent model for hemochromatosis. Proc Natl Acad Sci USA 84:3457-3461, 1987
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3457-3461
    • Craven, C.M.1    Alexander, J.2    Eldridge, M.3    Kushner, H.P.4    Bernstein, S.5    Kaplan, J.6
  • 18
    • 0028182255 scopus 로고
    • 59Fe into spleen, liver, kidney and some soft tissues in normal and hypotransferrinaemic mice: Influence of an antibody against the transferrin receptor
    • 59Fe into spleen, liver, kidney and some soft tissues in normal and hypotransferrinaemic mice: Influence of an antibody against the transferrin receptor. Biochem Pharmacol 47:969-974, 1994
    • (1994) Biochem Pharmacol , vol.47 , pp. 969-974
    • Bradbury, M.W.B.1    Raja, K.2    Veda, I.3
  • 19
    • 0019860059 scopus 로고
    • Transferrin, biochemistry, physiology and clinical significance
    • MORGAN EH: Transferrin, biochemistry, physiology and clinical significance. Mol Aspects Med 4:1-123, 1981
    • (1981) Mol Aspects Med , vol.4 , pp. 1-123
    • Morgan, E.H.1
  • 20
    • 0026458234 scopus 로고
    • Regulation of transferrin gene expression
    • ZAKIN MM: Regulation of transferrin gene expression. FASEB J 6:325-328, 1992
    • (1992) FASEB J , vol.6 , pp. 325-328
    • Zakin, M.M.1
  • 21
    • 0026794561 scopus 로고
    • Iron uptake in relation to transferrin degradation in brain and other tissues of rats
    • Regul Integrative Comp Physiol 32
    • STRAHAM ME, CROWE A, MORGAN EH: Iron uptake in relation to transferrin degradation in brain and other tissues of rats. Am J Physiol 263(Regul Integrative Comp Physiol 32):R924-R929, 1992
    • (1992) Am J Physiol , vol.263
    • Straham, M.E.1    Crowe, A.2    Morgan, E.H.3
  • 22
    • 0021265943 scopus 로고
    • The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes
    • YOUNG SP, BOMFORD A, WILLIAMS R: The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes. Biochem J 219:505-510, 1984
    • (1984) Biochem J , vol.219 , pp. 505-510
    • Young, S.P.1    Bomford, A.2    Williams, R.3
  • 23
    • 0030608152 scopus 로고    scopus 로고
    • Ferritin: Molecular properties, iron storage function and cellular regulation
    • HARRISON PM, AROSIO P: Ferritin: Molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275: 161-203, 1996
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 27
    • 0025924788 scopus 로고
    • A new role for the transferrin receptor in the release of iron from transferrin
    • BALI PK, ZAP O, AILEEN P: A new role for the transferrin receptor in the release of iron from transferrin. Biochemistry 30:324-328, 1991
    • (1991) Biochemistry , vol.30 , pp. 324-328
    • Bali, P.K.1    Zap, O.2    Aileen, P.3
  • 29
  • 31
    • 0029865751 scopus 로고    scopus 로고
    • Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: Examination of cytoplasmic and mitochondrial intermediates involved in iron metabolism
    • RICHARDSON DR, PONKA P, VYORAL D: Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: Examination of cytoplasmic and mitochondrial intermediates involved in iron metabolism. Blood 87:3477-3488, 1996
    • (1996) Blood , vol.87 , pp. 3477-3488
    • Richardson, D.R.1    Ponka, P.2    Vyoral, D.3
  • 32
    • 1642628290 scopus 로고    scopus 로고
    • Delivery of iron into erythroid cell mitochondria requires endosome mobility
    • ZHANG A-S, SHEFTEL AD, HAJEK J, PONKA P: Delivery of iron into erythroid cell mitochondria requires endosome mobility. (abstract) Blood 90(Suppl 1):6a, 1997
    • (1997) Blood , vol.90 , Issue.1 SUPPL.
    • Zhang, A.-S.1    Sheftel, A.D.2    Hajek, J.3    Ponka, P.4
  • 33
    • 0000622023 scopus 로고
    • Iron-transferrin requirements and transferrin receptor expression in proliferating cells
    • edited by PONKA P, SCHULMAN HM, WOODWORTH RD, Boca Raton, CRC Press
    • KUHN LC, SCHULMAN HM, PONKA P: Iron-transferrin requirements and transferrin receptor expression in proliferating cells, in Iron Transport and Storage, edited by PONKA P, SCHULMAN HM, WOODWORTH RD, Boca Raton, CRC Press, 1990, pp 149-191
    • (1990) Iron Transport and Storage , pp. 149-191
    • Kuhn, L.C.1    Schulman, H.M.2    Ponka, P.3
  • 34
    • 0026684574 scopus 로고
    • Iron-dependent regulation of ferritin and transferrin receptor expression by the iron-responsive element binding protein
    • LEIBOLD EA, Guo B: Iron-dependent regulation of ferritin and transferrin receptor expression by the iron-responsive element binding protein. Annu Rev Nutr 12:345-368, 1992
    • (1992) Annu Rev Nutr , vol.12 , pp. 345-368
    • Leibold, E.A.1    Guo, B.2
  • 35
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • KLAUSNER RD, ROUAULT TA, HARFORD JT: Regulating the fate of mRNA: The control of cellular iron metabolism. Cell 72:19-28, 1993
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.T.3
  • 36
    • 0028114730 scopus 로고
    • Iron regulatory elements (IREs): A family of mRNA non-coding sequences
    • THEIL EC: Iron regulatory elements (IREs): A family of mRNA non-coding sequences. Biochem J 304:1-11, 1994
    • (1994) Biochem J , vol.304 , pp. 1-11
    • Theil, E.C.1
  • 37
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress
    • HENTZE MW, KUHN LC: Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress. Proc Natl Acad Sci USA 93:8175-8182, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 38
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • STAMLER JS, SINGEL DJ, LOSCALZO J: Biochemistry of nitric oxide and its redox-activated forms. Science 258:1898-1902, 1992
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 39
    • 0028784211 scopus 로고
    • The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells
    • RICHARDSON DR, NEUMANNOVA V, NAGY E, PONKA P: The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells. Blood 86:3211-3219, 1995
    • (1995) Blood , vol.86 , pp. 3211-3219
    • Richardson, D.R.1    Neumannova, V.2    Nagy, E.3    Ponka, P.4
  • 41
    • 0025766759 scopus 로고
    • Differential regulation of iron regulatory element-binding protein(s) in cell extracts of activated lymphocytes versus monocytesmacrophages
    • TESTA U, KUHN L, PETRINI M, QUARANTA MT, PELOSI E, PESCHLE C: Differential regulation of iron regulatory element-binding protein(s) in cell extracts of activated lymphocytes versus monocytesmacrophages. J Biol Chem 266:13925-13930, 1991
    • (1991) J Biol Chem , vol.266 , pp. 13925-13930
    • Testa, U.1    Kuhn, L.2    Petrini, M.3    Quaranta, M.T.4    Pelosi, E.5    Peschle, C.6
  • 42
    • 0000474506 scopus 로고
    • Structural organization of the mammalian kidney
    • edited by SELDIN DW, GIEBISCH G, New York, Raven Press
    • KRIZ W, KAISSLING B: Structural organization of the mammalian kidney, in The Kidney: Physiology and Pathophysiology (2nd ed), edited by SELDIN DW, GIEBISCH G, New York, Raven Press, 1992, pp 707-777
    • (1992) The Kidney: Physiology and Pathophysiology (2nd Ed) , pp. 707-777
    • Kriz, W.1    Kaissling, B.2
  • 43
    • 0024273450 scopus 로고
    • Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein
    • GOLDBERG MA, DUNNING SP, BUNN HF: Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein. Science 242:1412-1415, 1988
    • (1988) Science , vol.242 , pp. 1412-1415
    • Goldberg, M.A.1    Dunning, S.P.2    Bunn, H.F.3
  • 44
    • 0031028158 scopus 로고    scopus 로고
    • Erythropoietin gene regulation depends on heme-dependent oxygen sending and assembly of interacting transcription factors
    • HUANG LE, HO V, ARANY Z, KRAINC D, GALSON D, TENDLER D. LIVINGSTON DM, BUNN HF: Erythropoietin gene regulation depends on heme-dependent oxygen sending and assembly of interacting transcription factors. Kidney Int 51:548-552, 1997
    • (1997) Kidney Int , vol.51 , pp. 548-552
    • Huang, L.E.1    Ho, V.2    Arany, Z.3    Krainc, D.4    Galson, D.5    Tendler, D.6    Livingston, D.M.7    Bunn, H.F.8
  • 45
    • 0030905888 scopus 로고    scopus 로고
    • Structure requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells
    • ODORIZZI G, TROWBRIDGE IS: Structure requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells. J Cell Biol 137:1255-1264, 1997
    • (1997) J Cell Biol , vol.137 , pp. 1255-1264
    • Odorizzi, G.1    Trowbridge, I.S.2
  • 46
    • 0028304457 scopus 로고
    • The calmodulin antagonist, W-13, alters transcytosis, recycling, and the morphology of the endocytic pathway in Madin-Darby canine kidney cells
    • APODACA G, ENRICH C, MOSTOV KA: The calmodulin antagonist, W-13, alters transcytosis, recycling, and the morphology of the endocytic pathway in Madin-Darby canine kidney cells. J Biol Chem 269:19005-19013, 1994
    • (1994) J Biol Chem , vol.269 , pp. 19005-19013
    • Apodaca, G.1    Enrich, C.2    Mostov, K.A.3
  • 48
    • 0027717217 scopus 로고
    • Characterization of a second RN A-binding protein in rodents with specificity for iron-responsive elements
    • HENDERSON BH, SEISER C, KUHN LC: Characterization of a second RN A-binding protein in rodents with specificity for iron-responsive elements. J Biol Chem 268:27327-27334, 1993
    • (1993) J Biol Chem , vol.268 , pp. 27327-27334
    • Henderson, B.H.1    Seiser, C.2    Kuhn, L.C.3
  • 49
    • 0030455852 scopus 로고    scopus 로고
    • Effects of iron deficiency and iron overload on manganese uptake and deposition in the brain and other organs of the rat
    • CHUA ACG, MORGAN EH: Effects of iron deficiency and iron overload on manganese uptake and deposition in the brain and other organs of the rat. Biol Trace Elem Res 5539-54, 1996
    • (1996) Biol Trace Elem Res , vol.55 , pp. 39-54
    • Chua, A.C.G.1    Morgan, E.H.2
  • 50
    • 0025055459 scopus 로고
    • Effect of thalassemia/hemoglobin e disease on macro, trace, and ultratrace element concentrations in human tissue
    • SHULER TR, POOTRAKUL P, YARNSUKON P, NIELSES FH: Effect of thalassemia/hemoglobin E disease on macro, trace, and ultratrace element concentrations in human tissue. J Trace Elem Exp Med 3:31-43, 1990
    • (1990) J Trace Elem Exp Med , vol.3 , pp. 31-43
    • Shuler, T.R.1    Pootrakul, P.2    Yarnsukon, P.3    Nielses, F.H.4
  • 55
    • 0028329767 scopus 로고
    • Role of iron and oxygen radicals in the progression of chronic renal failure
    • ALFREY AC: Role of iron and oxygen radicals in the progression of chronic renal failure. Am J Kidney Dis 23:183-187, 1994
    • (1994) Am J Kidney Dis , vol.23 , pp. 183-187
    • Alfrey, A.C.1
  • 57
    • 0024102731 scopus 로고
    • Regulation of porphyrin and heme metabolism in the kidney
    • WOODS JS: Regulation of porphyrin and heme metabolism in the kidney. Semin Hematol 25:336-348, 1988
    • (1988) Semin Hematol , vol.25 , pp. 336-348
    • Woods, J.S.1
  • 58
    • 0031936712 scopus 로고    scopus 로고
    • Expression and distribution of heme oxygenase-2 mRNA and protein in rat kidney
    • Hu Y, MA N, YANG M, SEMBA R: Expression and distribution of heme oxygenase-2 mRNA and protein in rat kidney. J Histochem Cytochem 46:249-256, 1998
    • (1998) J Histochem Cytochem , vol.46 , pp. 249-256
    • Hu, Y.1    Ma, N.2    Yang, M.3    Semba, R.4
  • 59
    • 0027485237 scopus 로고
    • Induction of kidney heme oxygenase-1 (HSP32) mRNA and protein by ischemia reperfusion: Possible role of heme as both promoter of tissue damage and regulator of HSP32
    • MAINES MD, MAYER RD, EWING JF, MCCONBREY WK JR: Induction of kidney heme oxygenase-1 (HSP32) mRNA and protein by ischemia reperfusion: Possible role of heme as both promoter of tissue damage and regulator of HSP32. J Pharmacol Exp Ther 264:457-462, 1993
    • (1993) J Pharmacol Exp Ther , vol.264 , pp. 457-462
    • Maines, M.D.1    Mayer, R.D.2    Ewing, J.F.3    Mcconbrey Jr., W.K.4
  • 60
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological significance
    • STOCKER R, YAMAMOTO Y, MCDONAGH AF, GLAZER AN, AMES BN: Bilirubin is an antioxidant of possible physiological significance. Science 235:1043-1046, 1987
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    Mcdonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 61
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • POSS KD, TONEGAWA S: Heme oxygenase 1 is required for mammalian iron reutilization. Proc Natl Acad Sci USA 94:10919-10924, 1997
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 62
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1-deficient cells
    • POSS KD, TONEGAWA S: Reduced stress defense in heme oxygenase 1-deficient cells. Proc Natl Acad Sci USA 94:10925-10930, 1997
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10925-10930
    • Poss, K.D.1    Tonegawa, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.