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Volumn 54, Issue 10, 1996, Pages 295-317

Iron metabolism: A comprehensive review

Author keywords

[No Author keywords available]

Indexed keywords

FERRITIN; HEMOGLOBIN; IRON; TRANSFERRIN; TRANSFERRIN RECEPTOR;

EID: 0030424010     PISSN: 00296643     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1753-4887.1996.tb03794.x     Document Type: Review
Times cited : (239)

References (277)
  • 1
    • 12644272769 scopus 로고
    • Prelude to a cell
    • de Duve C. Prelude to a cell. The Sciences 1990;30:22-8
    • (1990) The Sciences , vol.30 , pp. 22-28
    • De Duve, C.1
  • 2
    • 0021965878 scopus 로고
    • Paleolithic nutrition. A consideration of its nature and current implications
    • Eaton SB, Konner M. Paleolithic nutrition. A consideration of its nature and current implications. N Engl J Med 1985;312:283-9
    • (1985) N Engl J Med , vol.312 , pp. 283-289
    • Eaton, S.B.1    Konner, M.2
  • 7
    • 12644280807 scopus 로고
    • The iron mixture of Dr. Griffith
    • Cule J. The iron mixture of Dr. Griffith. Pharm J. 1967;CXCVIII:399-400
    • (1967) Pharm J. , vol.198 , pp. 399-400
    • Cule, J.1
  • 12
    • 0344126659 scopus 로고
    • Du fer contenu dans le sang et dans les aliments
    • Boussingault JB. Du fer contenu dans le sang et dans les aliments. CR Acad Sci Paris 1872;74: 1353-9
    • (1872) CR Acad Sci Paris , vol.74 , pp. 1353-1359
    • Boussingault, J.B.1
  • 14
    • 50349143880 scopus 로고
    • Absorption and excretion of iron
    • McCance RA, Widdowson EM. Absorption and excretion of iron. Lancet 1937;2:680-4
    • (1937) Lancet , vol.2 , pp. 680-684
    • McCance, R.A.1    Widdowson, E.M.2
  • 15
    • 12644270195 scopus 로고
    • Studies in iron transportation and metabolism. IV. Observations on the absorption of iron from the gastrointestinal tract
    • Moore CV, Arrowsmith WR, Welch J, Minnich V. Studies in iron transportation and metabolism. IV. Observations on the absorption of iron from the gastrointestinal tract. J Clin Invest. 1939;18:553-80
    • (1939) J Clin Invest. , vol.18 , pp. 553-580
    • Moore, C.V.1    Arrowsmith, W.R.2    Welch, J.3    Minnich, V.4
  • 16
    • 0011869104 scopus 로고
    • Protein apoferritin in iron feeding and absorption
    • Granick S. Protein apoferritin in iron feeding and absorption. Science 1946;103:107-13
    • (1946) Science , vol.103 , pp. 107-113
    • Granick, S.1
  • 17
    • 12644315027 scopus 로고
    • National Live Stock and Meat Board
    • Iron in Human Nutrition. National Live Stock and Meat Board, 1990
    • (1990) Iron in Human Nutrition
  • 18
    • 84940616830 scopus 로고
    • Mineral metabolism of healthy adults on white and brown bread dietaries
    • McCance RA, Widdowson EM. Mineral metabolism of healthy adults on white and brown bread dietaries. J Physiol 1942;101:44-85
    • (1942) J Physiol , vol.101 , pp. 44-85
    • McCance, R.A.1    Widdowson, E.M.2
  • 20
    • 0014572992 scopus 로고
    • Effect of histidine and certain other amino acids on the absorption of iron-59 by rats
    • Van Campen D, Gross C. Effect of histidine and certain other amino acids on the absorption of iron-59 by rats. J Nutr 1969;99:68-74
    • (1969) J Nutr , vol.99 , pp. 68-74
    • Van Campen, D.1    Gross, C.2
  • 22
    • 0017180237 scopus 로고
    • Food iron absorption in human subjects. IV. The effects of calcium and phosphate salts on the absorption of nonheme iron
    • Monsen ER, Cook JD. Food iron absorption in human subjects. IV. The effects of calcium and phosphate salts on the absorption of nonheme iron. Am J Clin Nutr 1976;29:1142-8
    • (1976) Am J Clin Nutr , vol.29 , pp. 1142-1148
    • Monsen, E.R.1    Cook, J.D.2
  • 23
    • 12644295034 scopus 로고
    • Potential role of in vitro iron bioavailability studies in combatting iron deficiency: A study of the effects of phosvitin on iron mobilization from pinto beans
    • Breddy M, Chidambaram MV, Fonseca J, Bates GW. Potential role of in vitro iron bioavailability studies in combatting iron deficiency: a study of the effects of phosvitin on iron mobilization from pinto beans. USAid Cooperative Agreement 1976;1:1-45
    • (1976) USAid Cooperative Agreement , vol.1 , pp. 1-45
    • Breddy, M.1    Chidambaram, M.V.2    Fonseca, J.3    Bates, G.W.4
  • 24
    • 12644287521 scopus 로고
    • Effect of histidine, cysteine, glutathione or beef on iron absorption in humans
    • Layrisse M, Martinez-Torres C, Leets I, Taylor P, Ramirez J. Effect of histidine, cysteine, glutathione or beef on iron absorption in humans. Br J Nutr 1984;52:37-46
    • (1984) Br J Nutr , vol.52 , pp. 37-46
    • Layrisse, M.1    Martinez-Torres, C.2    Leets, I.3    Taylor, P.4    Ramirez, J.5
  • 26
    • 0016711657 scopus 로고
    • Iron deficiency and dietary factors in Finland
    • Takkunen H, Seppänen R. Iron deficiency and dietary factors in Finland. Am J Clin Nutr 1975;28: 1141-7
    • (1975) Am J Clin Nutr , vol.28 , pp. 1141-1147
    • Takkunen, H.1    Seppänen, R.2
  • 27
    • 0015953290 scopus 로고
    • Food iron absorption in man. Application of the two-pool extrinsic tag method to measure heme and non-heme iron absorption
    • Bjorn-Rasmussen E, Hallberg L, Isaksson B, Arvidsson B. Food iron absorption in man. Application of the two-pool extrinsic tag method to measure heme and non-heme iron absorption. J Clin Invest. 1974;53: 247-56
    • (1974) J Clin Invest. , vol.53 , pp. 247-256
    • Bjorn-Rasmussen, E.1    Hallberg, L.2    Isaksson, B.3    Arvidsson, B.4
  • 28
    • 12644292887 scopus 로고
    • Iron fortification: An update
    • Cook JD, Reusser ME. Iron fortification: an update. J Food Sci 1983;48:1340-9
    • (1983) J Food Sci , vol.48 , pp. 1340-1349
    • Cook, J.D.1    Reusser, M.E.2
  • 29
    • 0025988250 scopus 로고
    • Assessment of dietary determinants of nonheme-iron absorption in humans and rats
    • Reddy MB, Cook JD. Assessment of dietary determinants of nonheme-iron absorption in humans and rats. Am J Clin Nutr 1991;54:723-8
    • (1991) Am J Clin Nutr , vol.54 , pp. 723-728
    • Reddy, M.B.1    Cook, J.D.2
  • 30
    • 0021001159 scopus 로고
    • The bioavailability of trace mineral elements
    • Forbes RM, Erdman JW. The bioavailability of trace mineral elements. Ann Rev Nutr 1983;3:213-31
    • (1983) Ann Rev Nutr , vol.3 , pp. 213-231
    • Forbes, R.M.1    Erdman, J.W.2
  • 31
    • 0026002694 scopus 로고
    • Asessment of the role of non-heme-iron availibility in iron balance
    • Cook JD, Dassenko SA, Lynch SR. Asessment of the role of non-heme-iron availibility in iron balance. Am J Clin Nutr 1991;54:717-22
    • (1991) Am J Clin Nutr , vol.54 , pp. 717-722
    • Cook, J.D.1    Dassenko, S.A.2    Lynch, S.R.3
  • 33
    • 12644275414 scopus 로고
    • Iron fortification - Rationale and effects
    • Beard J. Iron fortification - rationale and effects. Nutr Today 1986;21:17-20
    • (1986) Nutr Today , vol.21 , pp. 17-20
    • Beard, J.1
  • 34
    • 12644284488 scopus 로고
    • Yin, yang and iron
    • Crosby WH. Yin, yang and iron. Nutr Today 1986; 21:14-6
    • (1986) Nutr Today , vol.21 , pp. 14-16
    • Crosby, W.H.1
  • 35
    • 0026806469 scopus 로고
    • Stored iron and ischemic heart disease - Empirical support for a new paradigm
    • Sullivan JL. Stored iron and ischemic heart disease - empirical support for a new paradigm. Circulation 1992;86:1036-7
    • (1992) Circulation , vol.86 , pp. 1036-1037
    • Sullivan, J.L.1
  • 36
    • 85056951187 scopus 로고
    • Preventive measures for the maintenance of low but adequate iron stores
    • Lauffer R, ed. Boca Raton: CRC Press
    • Lauffer R. Preventive measures for the maintenance of low but adequate iron stores. In: Lauffer R, ed. Iron and Human Disease. Boca Raton: CRC Press, 1992
    • (1992) Iron and Human Disease
    • Lauffer, R.1
  • 38
    • 0027439562 scopus 로고
    • Effect of bovine-hemoglobin fortified cookies on iron status of schoolchildren - A nationwide program in Chile
    • Walter T, Hertrampf E, Pizarro F, et al. Effect of bovine-hemoglobin fortified cookies on iron status of schoolchildren - a nationwide program in Chile. Am J Clin Nutr 1993;57:190-4
    • (1993) Am J Clin Nutr , vol.57 , pp. 190-194
    • Walter, T.1    Hertrampf, E.2    Pizarro, F.3
  • 39
    • 0026751985 scopus 로고
    • Supplementation of an adapted formula with bovine lactoferrin. 2. Effects on serum iron, ferritin and zinc levels
    • Chierici R, Sawatzki G, Tamisari L, Volpato S, Vigi V. Supplementation of an adapted formula with bovine lactoferrin. 2. Effects on serum iron, ferritin and zinc levels. Acta Paediatr 1992;81:475-9
    • (1992) Acta Paediatr , vol.81 , pp. 475-479
    • Chierici, R.1    Sawatzki, G.2    Tamisari, L.3    Volpato, S.4    Vigi, V.5
  • 41
    • 0026470429 scopus 로고
    • Contributions of heme and nonheme iron to human nutrition
    • Carpenter CE, Mahoney AW. Contributions of heme and nonheme iron to human nutrition. Crit Rev Food Sci Nutr 1992;31:333-67
    • (1992) Crit Rev Food Sci Nutr , vol.31 , pp. 333-367
    • Carpenter, C.E.1    Mahoney, A.W.2
  • 42
    • 0023620331 scopus 로고
    • Dependence of intestinal iron absorption on the valency state of iron
    • Wollenberg P, Rummel W. Dependence of intestinal iron absorption on the valency state of iron. Naunyn Schmiedebegs Arch Pharmacol 1987;336:578-82
    • (1987) Naunyn Schmiedebegs Arch Pharmacol , vol.336 , pp. 578-582
    • Wollenberg, P.1    Rummel, W.2
  • 46
    • 0013968152 scopus 로고
    • Does the pancreas influence iron absorption?
    • Murry MJ, Stein N. Does the pancreas influence iron absorption? Gastroenterol 1966;51:694-700
    • (1966) Gastroenterol , vol.51 , pp. 694-700
    • Murry, M.J.1    Stein, N.2
  • 49
    • 0025120673 scopus 로고
    • Rat intestinal iron transfer capacity and the longitudinal distribution of its adaptation to iron deficiency
    • Schümann K, Elsenhans B, Ehtechami C, Forth W. Rat intestinal iron transfer capacity and the longitudinal distribution of its adaptation to iron deficiency. Digestion. 1990;46:35-45
    • (1990) Digestion , vol.46 , pp. 35-45
    • Schümann, K.1    Elsenhans, B.2    Ehtechami, C.3    Forth, W.4
  • 51
    • 0015322649 scopus 로고
    • Model for measuring dietary absorption of heme iron: Test with a complete meal
    • Layrisse M, Martinez-Torres C. Model for measuring dietary absorption of heme iron: test with a complete meal. Am J Clin Nutr 1972;25:401-11
    • (1972) Am J Clin Nutr , vol.25 , pp. 401-411
    • Layrisse, M.1    Martinez-Torres, C.2
  • 54
    • 0015580453 scopus 로고
    • The effects of ascorbic acid supplementation on the absorption of iron in maize, wheat and soy
    • Sayers MH, Lynch SR, Jacobs P, et al. The effects of ascorbic acid supplementation on the absorption of iron in maize, wheat and soy. Br J Haematol 1973;24:209-18
    • (1973) Br J Haematol , vol.24 , pp. 209-218
    • Sayers, M.H.1    Lynch, S.R.2    Jacobs, P.3
  • 55
    • 0017162417 scopus 로고
    • Food iron absorption in human subjects. III. comparison of the effect of animal proteins on non heme iron absorption
    • Cook JD, Monsen ER. Food iron absorption in human subjects. III. comparison of the effect of animal proteins on non heme iron absorption. Am J Clin Nutr 1976;29:859-67
    • (1976) Am J Clin Nutr , vol.29 , pp. 859-867
    • Cook, J.D.1    Monsen, E.R.2
  • 56
    • 0022574837 scopus 로고
    • The effect of cysteine-containing peptides released during meat digestion on iron absorption in humans
    • Taylor PG, Martinez-Torres C, Romano EL, Latrisse M. The effect of cysteine-containing peptides released during meat digestion on iron absorption in humans. Am J Clin Nutr 1986;43:68-71
    • (1986) Am J Clin Nutr , vol.43 , pp. 68-71
    • Taylor, P.G.1    Martinez-Torres, C.2    Romano, E.L.3    Latrisse, M.4
  • 57
    • 0019779269 scopus 로고
    • The inhibitory effect of bran on iron absorption in humans
    • Simpson KM, Morris ER, Cook JD. The inhibitory effect of bran on iron absorption in humans. Am J Clin Nutr 1981;34:1469-78
    • (1981) Am J Clin Nutr , vol.34 , pp. 1469-1478
    • Simpson, K.M.1    Morris, E.R.2    Cook, J.D.3
  • 58
    • 0021028975 scopus 로고
    • Effect of dietary pectin on iron absorption and turnover in the rat
    • Baig MM, Burgin CW, Cerda JJ. Effect of dietary pectin on iron absorption and turnover in the rat. J Nutr 1983;113:2615-22
    • (1983) J Nutr , vol.113 , pp. 2615-2622
    • Baig, M.M.1    Burgin, C.W.2    Cerda, J.J.3
  • 59
    • 0021327517 scopus 로고
    • The effect of soy protein isolate in the diet on retention by the rat of iron from radio-labeled test meals
    • Thompson DB, Erdman JEW. The effect of soy protein isolate in the diet on retention by the rat of iron from radio-labeled test meals. J Nutr 1984;114:307-11
    • (1984) J Nutr , vol.114 , pp. 307-311
    • Thompson, D.B.1    Erdman, J.E.W.2
  • 60
    • 0019848768 scopus 로고
    • The inhibitory effect of soy products on nonheme iron absorption in man
    • Cook JD, Morck TA, Lynch SR. The inhibitory effect of soy products on nonheme iron absorption in man. Am J Clin Nutr 1981;34:2180-4
    • (1981) Am J Clin Nutr , vol.34 , pp. 2180-2184
    • Cook, J.D.1    Morck, T.A.2    Lynch, S.R.3
  • 61
  • 62
    • 0020646325 scopus 로고
    • The influence of tin, nickel, and cadmium on the intestinal absorption of iron
    • Schäfer SG, Forth W. The influence of tin, nickel, and cadmium on the intestinal absorption of iron. Ecotoxicol Environ Safety 1982;7:87-95
    • (1982) Ecotoxicol Environ Safety , vol.7 , pp. 87-95
    • Schäfer, S.G.1    Forth, W.2
  • 63
    • 0021915014 scopus 로고
    • Manganese binding proteins in human and cow's milk
    • Lönnerdal B, Keen CL, Hurley LS. Manganese binding proteins in human and cow's milk. Am J Clin Nutr 1985;41:550-9
    • (1985) Am J Clin Nutr , vol.41 , pp. 550-559
    • Lönnerdal, B.1    Keen, C.L.2    Hurley, L.S.3
  • 64
    • 0019499345 scopus 로고
    • Studies on the bioavailibility of zinc in humans IV: Effects of heme and nonheme iron on the absorption of zinc
    • Solomons NW, Jacob RA. Studies on the bioavailibility of zinc in humans IV: effects of heme and nonheme iron on the absorption of zinc. Am J Clin Nutr 1981;34:475-82
    • (1981) Am J Clin Nutr , vol.34 , pp. 475-482
    • Solomons, N.W.1    Jacob, R.A.2
  • 65
    • 0021127927 scopus 로고
    • Plasma zinc and copper levels of infants fed different formulas
    • Craig WJ, Balbach L, Harris S, Vyhmeister N. Plasma zinc and copper levels of infants fed different formulas. J Am Coll Nutr 1984;3:183-6
    • (1984) J Am Coll Nutr , vol.3 , pp. 183-186
    • Craig, W.J.1    Balbach, L.2    Harris, S.3    Vyhmeister, N.4
  • 66
    • 12544260758 scopus 로고
    • Does iron supplementation compromise zinc nutrition in healthy infants
    • Yip R, Reeves JD, Lönnerdal B, Keen CL, Dallman PR. Does iron supplementation compromise zinc nutrition in healthy infants. J Nutr 1983;113:2159-70
    • (1983) J Nutr , vol.113 , pp. 2159-2170
    • Yip, R.1    Reeves, J.D.2    Lönnerdal, B.3    Keen, C.L.4    Dallman, P.R.5
  • 68
  • 69
    • 0026440714 scopus 로고
    • Interactions among dietary manganese, heme iron, and nonheme iron in women
    • Davis CD, Malecki EA, Greger JL. Interactions among dietary manganese, heme iron, and nonheme iron in women. Am J Clin Nutr 1992;56:926-32
    • (1992) Am J Clin Nutr , vol.56 , pp. 926-932
    • Davis, C.D.1    Malecki, E.A.2    Greger, J.L.3
  • 70
    • 0026483440 scopus 로고
    • Calcium supplementation and plasma ferritin concentrations in premenopausal women
    • Sokoll LJ, Dawson-Hughes B. Calcium supplementation and plasma ferritin concentrations in premenopausal women. Am J Clin Nutr 1992;56:1045-8
    • (1992) Am J Clin Nutr , vol.56 , pp. 1045-1048
    • Sokoll, L.J.1    Dawson-Hughes, B.2
  • 71
    • 0026586953 scopus 로고
    • Calcium and iron absorption: Mechanism of action and nutritional importance
    • Hallberg L, Rossander-Hulten L, Brune M, Gleerup A. Calcium and iron absorption: mechanism of action and nutritional importance. Eur J Clin Nutr 1992;46:317-27
    • (1992) Eur J Clin Nutr , vol.46 , pp. 317-327
    • Hallberg, L.1    Rossander-Hulten, L.2    Brune, M.3    Gleerup, A.4
  • 72
    • 0023265485 scopus 로고
    • Iron uptake by rat duodenal microvillous membrane vesicles: Evidence for a carrier mediated transport system
    • Stremmel W, Lotz G, Niederau C, Teschke R, Strohmeyer G. Iron uptake by rat duodenal microvillous membrane vesicles: evidence for a carrier mediated transport system. Eur J Clin Invest 1987;17:136-45
    • (1987) Eur J Clin Invest , vol.17 , pp. 136-145
    • Stremmel, W.1    Lotz, G.2    Niederau, C.3    Teschke, R.4    Strohmeyer, G.5
  • 74
    • 0020486094 scopus 로고
    • Spectral and other studies on the intestinal haem receptor of the pig
    • Grasbeck R, Majuri I, Kouvonen I, Tenhun R. Spectral and other studies on the intestinal haem receptor of the pig. Biochim Biophys Acta 1982;700:137-47
    • (1982) Biochim Biophys Acta , vol.700 , pp. 137-147
    • Grasbeck, R.1    Majuri, I.2    Kouvonen, I.3    Tenhun, R.4
  • 76
    • 0016326163 scopus 로고
    • Intestinal absorption of hemoglobin heme iron cleavage by mucosal heme oxygenase
    • Raffin SB, Woo CH, Roost KT, Price DC, Schmid R. Intestinal absorption of hemoglobin heme iron cleavage by mucosal heme oxygenase. J Clin Invest 1974;54:1344
    • (1974) J Clin Invest , vol.54 , pp. 1344
    • Raffin, S.B.1    Woo, C.H.2    Roost, K.T.3    Price, D.C.4    Schmid, R.5
  • 77
    • 0024437243 scopus 로고
    • Characterization of heme oxygenase in small intestinal epithelium
    • Rosenberg DW, Kappas A. Characterization of heme oxygenase in small intestinal epithelium. Arch Biochem Biophys 1989;274:471-80
    • (1989) Arch Biochem Biophys , vol.274 , pp. 471-480
    • Rosenberg, D.W.1    Kappas, A.2
  • 78
    • 0020700570 scopus 로고
    • The significance of transferrin for intestinal iron absorption
    • Huebers HA, Huebers E, Csiba E, Rummel W, Finch CA. The significance of transferrin for intestinal iron absorption. Blood 1983;61:283-90
    • (1983) Blood , vol.61 , pp. 283-290
    • Huebers, H.A.1    Huebers, E.2    Csiba, E.3    Rummel, W.4    Finch, C.A.5
  • 79
    • 0018250434 scopus 로고
    • Studies on iron transport in human intestine by immunoperoxidase technique. I. The localization of ferritin, lactoferritin and transferrin in human duodenal mucosa
    • Isobe K, Sakurami T, Ysobe Y. Studies on iron transport in human intestine by immunoperoxidase technique. I. The localization of ferritin, lactoferritin and transferrin in human duodenal mucosa. Acta Haematol Jpn 1978;41:294-99
    • (1978) Acta Haematol Jpn , vol.41 , pp. 294-299
    • Isobe, K.1    Sakurami, T.2    Ysobe, Y.3
  • 80
    • 0024521960 scopus 로고
    • Immunohistochemical evidence for a lack of ferritin in duodenal absorptive epithelial cells in idiopathic hemochromatosis
    • Fracanzani AL, Fargion S, Romano R, et al. Immunohistochemical evidence for a lack of ferritin in duodenal absorptive epithelial cells in idiopathic hemochromatosis. Gastroenterology 1989;96:1071-8
    • (1989) Gastroenterology , vol.96 , pp. 1071-1078
    • Fracanzani, A.L.1    Fargion, S.2    Romano, R.3
  • 81
    • 1642583058 scopus 로고
    • Rat transferrin gene expression: Tissue-specificity regulation by iron deficiency
    • Idzerda KL, Huebers H, Finch CA, McKnight GS. Rat transferrin gene expression: tissue-specificity regulation by iron deficiency. Proc Natl Acad Sci USA 1986;83:3723-7
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3723-3727
    • Idzerda, K.L.1    Huebers, H.2    Finch, C.A.3    McKnight, G.S.4
  • 82
    • 0026567061 scopus 로고
    • Regulation of transferrin, transferrin receptor, and ferritin genes in human duodenum
    • Pietrangelo A, Rocchi E, Casalgrandi G, et al. Regulation of transferrin, transferrin receptor, and ferritin genes in human duodenum. Gastroenterology 1992;102:802-9
    • (1992) Gastroenterology , vol.102 , pp. 802-809
    • Pietrangelo, A.1    Rocchi, E.2    Casalgrandi, G.3
  • 84
    • 0010497110 scopus 로고
    • The ultrastructural immunocytochemical localization of transferrin receptor (TFR) and transferrin (TF) in the gastrointestinal tract
    • Levine JS, Seligman PA. The ultrastructural immunocytochemical localization of transferrin receptor (TFR) and transferrin (TF) in the gastrointestinal tract. [Abstract] Gastroenterology 1984;86:1161
    • (1984) Gastroenterology , vol.86 , pp. 1161
    • Levine, J.S.1    Seligman, P.A.2
  • 85
    • 0021798633 scopus 로고
    • Ultrastructural localization of transferrin, transferrin receptor, and iron-binding sites on human placental and duodenal microvilli
    • Parmley RT, Barton JC, Conrad ME. Ultrastructural localization of transferrin, transferrin receptor, and iron-binding sites on human placental and duodenal microvilli. Br J Haematol 1985;60:81-9
    • (1985) Br J Haematol , vol.60 , pp. 81-89
    • Parmley, R.T.1    Barton, J.C.2    Conrad, M.E.3
  • 88
    • 0026098238 scopus 로고
    • A role for mucin in the absorption of inorganic iron and other metal cations. A study in rats
    • Conrad ME, Umbreit JN, Moore EG. A role for mucin in the absorption of inorganic iron and other metal cations. A study in rats. Gastroenterology 1991;100:129-36
    • (1991) Gastroenterology , vol.100 , pp. 129-136
    • Conrad, M.E.1    Umbreit, J.N.2    Moore, E.G.3
  • 89
    • 0025688902 scopus 로고
    • Iron uptake by human upper small intestine microvillous membrane vesicles: Indication for a facilitated transport mechanism mediated by a membrane iron-binding protein
    • Teichmann R, Stremmel W. Iron uptake by human upper small intestine microvillous membrane vesicles: indication for a facilitated transport mechanism mediated by a membrane iron-binding protein. J Clin Invest 1990;86:2145
    • (1990) J Clin Invest , vol.86 , pp. 2145
    • Teichmann, R.1    Stremmel, W.2
  • 90
    • 0026597163 scopus 로고
    • The mechanisms of nonheme iron uptake determined in IEC-6 rat intestinal cells
    • Nichols GM, Pearce AR, Alverez X, et al. The mechanisms of nonheme iron uptake determined in IEC-6 rat intestinal cells. J Nutr 1992;122:945-52
    • (1992) J Nutr , vol.122 , pp. 945-952
    • Nichols, G.M.1    Pearce, A.R.2    Alverez, X.3
  • 92
    • 0017250221 scopus 로고
    • A new iron-binding protein isolated from intestinal mucosa
    • Pollack S, Lasky FD. A new iron-binding protein isolated from intestinal mucosa. J Lab Clin Med 1976;87:670-9
    • (1976) J Lab Clin Med , vol.87 , pp. 670-679
    • Pollack, S.1    Lasky, F.D.2
  • 93
    • 0027181554 scopus 로고
    • Rat duodenal iron-binding protein mobilferrin is a homologue of calreticulin
    • Conrad ME, Umbreit JN, Moore EG. Rat duodenal iron-binding protein mobilferrin is a homologue of calreticulin. Gastroenterology 1993;104:1700-4
    • (1993) Gastroenterology , vol.104 , pp. 1700-1704
    • Conrad, M.E.1    Umbreit, J.N.2    Moore, E.G.3
  • 94
    • 0001537486 scopus 로고
    • Radioactive iron absorption by gastro-intestinal tract: Influence of anemia, anoxia and antecedent feeding distribution in growing dogs
    • Hahn PF, Bale WF, Ross JF, Balfour WM, Whipple GH. Radioactive iron absorption by gastro-intestinal tract: influence of anemia, anoxia and antecedent feeding distribution in growing dogs. J Exp Med 1943;78:169-88
    • (1943) J Exp Med , vol.78 , pp. 169-188
    • Hahn, P.F.1    Bale, W.F.2    Ross, J.F.3    Balfour, W.M.4    Whipple, G.H.5
  • 95
    • 0001751325 scopus 로고
    • Ferritin. IX. Increase of the protein apoferritin in the gastrointestinal mucosa as a direct response to iron feeding. The function of ferritin in the regulation of iron absorption
    • Granick S. Ferritin. IX. Increase of the protein apoferritin in the gastrointestinal mucosa as a direct response to iron feeding. The function of ferritin in the regulation of iron absorption. J Biol Chem 1946;164: 737-46
    • (1946) J Biol Chem , vol.164 , pp. 737-746
    • Granick, S.1
  • 97
    • 0014027719 scopus 로고
    • The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum
    • Osaki S, Johnson DA, Freiden E. The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum. J Biol Chem 1966;241:2746
    • (1966) J Biol Chem , vol.241 , pp. 2746
    • Osaki, S.1    Johnson, D.A.2    Freiden, E.3
  • 98
    • 0025069640 scopus 로고
    • The valency state of absorbed iron appearing in the portal blood and ceruloplasmin substitution
    • Wollenberg P, Malberg R, Rummel W. The valency state of absorbed iron appearing in the portal blood and ceruloplasmin substitution. Biometals 1990;336:1
    • (1990) Biometals , vol.336 , pp. 1
    • Wollenberg, P.1    Malberg, R.2    Rummel, W.3
  • 99
    • 0342415175 scopus 로고
    • Copper
    • Brown ML, ed. Washington, DC: International Life Sciences Institute Nutrition Foundation
    • O'Dell BL. Copper. In: Brown ML, ed. Present Knowledge in Nutrition, 6th ed. Washington, DC: International Life Sciences Institute Nutrition Foundation, 1990, p 261-267
    • (1990) Present Knowledge in Nutrition, 6th Ed. , pp. 261-267
    • O'Dell, B.L.1
  • 101
    • 0014555521 scopus 로고
    • Normal iron absorption in hypertransferremic mice
    • Scade SG, Bernier GM, Conrad ME. Normal iron absorption in hypertransferremic mice. Br J Haematol 1969;17:187-90
    • (1969) Br J Haematol , vol.17 , pp. 187-190
    • Scade, S.G.1    Bernier, G.M.2    Conrad, M.E.3
  • 102
    • 0025042548 scopus 로고
    • Serum transferrin receptor as an index of iron absorbtion
    • Cook JD, Dassenko S, Skikne BS. Serum transferrin receptor as an index of iron absorbtion. Br J Haematol 1990;75:603-9
    • (1990) Br J Haematol , vol.75 , pp. 603-609
    • Cook, J.D.1    Dassenko, S.2    Skikne, B.S.3
  • 103
    • 0022545796 scopus 로고
    • Transferrin receptors in the human gastrointestinal tract. Relationship to body iron stores
    • Banerjee D, Flanagan PR, Cluett J, Valberg LS. Transferrin receptors in the human gastrointestinal tract. Relationship to body iron stores. Gastroenterology 1986;91:861-9
    • (1986) Gastroenterology , vol.91 , pp. 861-869
    • Banerjee, D.1    Flanagan, P.R.2    Cluett, J.3    Valberg, L.S.4
  • 104
    • 0025233620 scopus 로고
    • Differential expression of transferrin receptor in duodenal mucosa in iron overload. Evidence for a site-specific defect in genetic hemochromatosis
    • Lombard M, Bomford AB, Poison RJ, Bellingham AJ, Williams R. Differential expression of transferrin receptor in duodenal mucosa in iron overload. Evidence for a site-specific defect in genetic hemochromatosis. Gastroenterology 1990;98:976-84
    • (1990) Gastroenterology , vol.98 , pp. 976-984
    • Lombard, M.1    Bomford, A.B.2    Poison, R.J.3    Bellingham, A.J.4    Williams, R.5
  • 105
    • 0025098220 scopus 로고
    • Transferrin receptor distribution and regulation in the small intestine. Effect of iron stores and erythropoiesis
    • Anderson GJ, Powell LW, Halliday JW. Transferrin receptor distribution and regulation in the small intestine. Effect of iron stores and erythropoiesis. Gastroenterology 1990;98:576-84
    • (1990) Gastroenterology , vol.98 , pp. 576-584
    • Anderson, G.J.1    Powell, L.W.2    Halliday, J.W.3
  • 107
    • 0025986817 scopus 로고
    • The effect of human recombinant erythropoietin on iron absorption and hepatic iron in a rat model
    • Adams PC, Chau LA, Lin E, Muirhead N. The effect of human recombinant erythropoietin on iron absorption and hepatic iron in a rat model. Clin Invest Med 1991;14:432-6
    • (1991) Clin Invest Med , vol.14 , pp. 432-436
    • Adams, P.C.1    Chau, L.A.2    Lin, E.3    Muirhead, N.4
  • 108
    • 0020074170 scopus 로고
    • Effect of transfused reticulocytes on iron exchange
    • Finch CA, Heuber H, Eng M, Miller L. Effect of transfused reticulocytes on iron exchange. Blood 1982;59:364-9
    • (1982) Blood , vol.59 , pp. 364-369
    • Finch, C.A.1    Heuber, H.2    Eng, M.3    Miller, L.4
  • 109
    • 84937095109 scopus 로고
    • Effect of hypoxia on iron absorption in rats
    • Vassar PS, Taylor DM. Effect of hypoxia on iron absorption in rats. Proc Soc Exp Biol Med 1956;93: 504-6
    • (1956) Proc Soc Exp Biol Med , vol.93 , pp. 504-506
    • Vassar, P.S.1    Taylor, D.M.2
  • 111
    • 0000723465 scopus 로고
    • Studies on iron absorption. I. The relationship between the rate of erythropoiesis, hypoxia and iron absorption
    • Mendel GA. Studies on iron absorption. I. The relationship between the rate of erythropoiesis, hypoxia and iron absorption. Blood 1961;18:727
    • (1961) Blood , vol.18 , pp. 727
    • Mendel, G.A.1
  • 112
    • 0002973627 scopus 로고
    • The significance of iron turnover in the control of iron absorption
    • Weintraub LR, Conrad ME, Crosby WH. The significance of iron turnover in the control of iron absorption. Blood 1964;24:19-24
    • (1964) Blood , vol.24 , pp. 19-24
    • Weintraub, L.R.1    Conrad, M.E.2    Crosby, W.H.3
  • 113
    • 12644257564 scopus 로고
    • Storage iron kinetics. VI. The effects of inflammation on iron exchange in the rat
    • Hershko C. Storage iron kinetics. VI. The effects of inflammation on iron exchange in the rat. Br J Haematol 1977;26:67-75
    • (1977) Br J Haematol , vol.26 , pp. 67-75
    • Hershko, C.1
  • 114
    • 0025349053 scopus 로고
    • Manganese transport across the blood brain barrier: Relationship to iron homeostasis
    • Aschner M, Aschner JL. Manganese transport across the blood brain barrier: Relationship to iron homeostasis. Brain Res Bull 1990;24:857-60
    • (1990) Brain Res Bull , vol.24 , pp. 857-860
    • Aschner, M.1    Aschner, J.L.2
  • 115
    • 0017184117 scopus 로고
    • Functional heterogeneity and pH dependent dissociation properties of human transferrin
    • Princiotto JV, Zapolski FJ. Functional heterogeneity and pH dependent dissociation properties of human transferrin. Biochim Biophys Acta 1976;428:766-71
    • (1976) Biochim Biophys Acta , vol.428 , pp. 766-771
    • Princiotto, J.V.1    Zapolski, F.J.2
  • 116
    • 12644295031 scopus 로고
    • No functional difference of the two iron-binding sites of human transferrin in vitro
    • van Der Heul C, Roos MJK, van Noort WL, van Eijk HG. No functional difference of the two iron-binding sites of human transferrin in vitro. Br J Haematol 1980;46:417-26
    • (1980) Br J Haematol , vol.46 , pp. 417-426
    • Van Der Heul, C.1    Roos, M.J.K.2    Van Noort, W.L.3    Van Eijk, H.G.4
  • 118
    • 0026031099 scopus 로고
    • A transferrin (hemiferrin) mRNA is expressed in the germ cells of rat testis
    • Stallard BJ, Collard MW, Griswold MD. A transferrin (hemiferrin) mRNA is expressed in the germ cells of rat testis. Mol Cell Biol 1991;11:1448-53
    • (1991) Mol Cell Biol , vol.11 , pp. 1448-1453
    • Stallard, B.J.1    Collard, M.W.2    Griswold, M.D.3
  • 119
    • 0022885445 scopus 로고
    • The human transferrin gene: 5′ region contains conserved sequences which match the control elements regulated by heavy metals, glucocorticoids and acute phase reaction
    • Adrian GS, Korinek BW, Bowman BH, Yang F. The human transferrin gene: 5′ region contains conserved sequences which match the control elements regulated by heavy metals, glucocorticoids and acute phase reaction. Gene 1986;49:167-75
    • (1986) Gene , vol.49 , pp. 167-175
    • Adrian, G.S.1    Korinek, B.W.2    Bowman, B.H.3    Yang, F.4
  • 120
    • 0022707291 scopus 로고
    • Regulation of transferrin receptor expression at the cell surface by insulin-like growth factors, epidermal growth factor and platelet-derived growth factor
    • Davis RJ, Czech MP. Regulation of transferrin receptor expression at the cell surface by insulin-like growth factors, epidermal growth factor and platelet-derived growth factor. EMBO J 1986;5:653-8
    • (1986) EMBO J , vol.5 , pp. 653-658
    • Davis, R.J.1    Czech, M.P.2
  • 121
    • 0026545292 scopus 로고
    • Transcriptional regulation of transferrin and albumin genes by retinoic acid in human hepatoma cell line Hep3B
    • Hsu SL, Lin YF, Chou CK. Transcriptional regulation of transferrin and albumin genes by retinoic acid in human hepatoma cell line Hep3B. Biochem J 1992;283:611-5
    • (1992) Biochem J , vol.283 , pp. 611-615
    • Hsu, S.L.1    Lin, Y.F.2    Chou, C.K.3
  • 123
    • 0027180801 scopus 로고
    • Posttranscriptional regulation of chimeric human transferrin genes by iron
    • Cox LA, Adrian GS. Posttranscriptional regulation of chimeric human transferrin genes by iron. Biochemistry 1993;32:4738-45
    • (1993) Biochemistry , vol.32 , pp. 4738-4745
    • Cox, L.A.1    Adrian, G.S.2
  • 124
  • 125
    • 0021677758 scopus 로고
    • Human lactoferrin: Amino acid sequence and structural comparison with other transferrins
    • Metz-Boutique M-H, Jollés J, Marzurier J, et al. Human lactoferrin: amino acid sequence and structural comparison with other transferrins. Eur J Biochem 1984;145:659-76
    • (1984) Eur J Biochem , vol.145 , pp. 659-676
    • Metz-Boutique, M.-H.1    Jollés, J.2    Marzurier, J.3
  • 126
    • 0026648532 scopus 로고
    • Lactoferrin uptake by the rat liver. Characterization of the recognition site and effect of selective modification of arginine residues
    • Ziere GJ, Van Dijk MC, Bijsterbosch MK, Van Berkel TJ. Lactoferrin uptake by the rat liver. Characterization of the recognition site and effect of selective modification of arginine residues. J Biol Chem 1992;267:11229-35
    • (1992) J Biol Chem , vol.267 , pp. 11229-11235
    • Ziere, G.J.1    Van Dijk, M.C.2    Bijsterbosch, M.K.3    Van Berkel, T.J.4
  • 127
    • 0022981174 scopus 로고
    • The non-immune inflammatory response: Serial changes in plasma iron, TIBC, lactoferrin, ferritin, and C-reactive protein
    • Baynes R, Bezwoda W, Bothwell T, Khan Q, Mansoor N. The non-immune inflammatory response: serial changes in plasma iron, TIBC, lactoferrin, ferritin, and C-reactive protein. Scand J Clin Lab Invest 1986;46:695-704
    • (1986) Scand J Clin Lab Invest , vol.46 , pp. 695-704
    • Baynes, R.1    Bezwoda, W.2    Bothwell, T.3    Khan, Q.4    Mansoor, N.5
  • 128
    • 0020558254 scopus 로고
    • Detection and isolation of a hepatic membrane receptor for ferritin
    • Mack U, Powell LW, Halliday JW. Detection and isolation of a hepatic membrane receptor for ferritin. J Biol Chem 1983;258:4672-5
    • (1983) J Biol Chem , vol.258 , pp. 4672-4675
    • Mack, U.1    Powell, L.W.2    Halliday, J.W.3
  • 130
    • 0023813241 scopus 로고
    • Isolation of a human hepatic ferritin receptor
    • Adams PC, Powell LW, Halliday JW. Isolation of a human hepatic ferritin receptor. Hepatology 1988;8: 719-21
    • (1988) Hepatology , vol.8 , pp. 719-721
    • Adams, P.C.1    Powell, L.W.2    Halliday, J.W.3
  • 131
    • 0026705752 scopus 로고
    • Functional roles of the ferritin receptors of human liver, hepatoma, lymphoid and erythroid cells
    • Moss D, Fargion S, Fracanzani AL, et al. Functional roles of the ferritin receptors of human liver, hepatoma, lymphoid and erythroid cells. J Inorg Biochem 1992;47:219-27
    • (1992) J Inorg Biochem , vol.47 , pp. 219-227
    • Moss, D.1    Fargion, S.2    Fracanzani, A.L.3
  • 133
    • 0018860041 scopus 로고
    • Studies on the concentration and intracellular localization of iron proteins in liver biopsy specimens from patients with iron overload with special reference to their role in lysosomal disruption
    • Selden C, Owen JMP, Hopkins JMP, Peters TJ. Studies on the concentration and intracellular localization of iron proteins in liver biopsy specimens from patients with iron overload with special reference to their role in lysosomal disruption. Br J Haematol 1980;44:593
    • (1980) Br J Haematol , vol.44 , pp. 593
    • Selden, C.1    Owen, J.M.P.2    Hopkins, J.M.P.3    Peters, T.J.4
  • 134
    • 0023067301 scopus 로고
    • Ferritin: Structure, gene regulation, and cellular function in animals, plants and microorganisms
    • Thiel EC. Ferritin: structure, gene regulation, and cellular function in animals, plants and microorganisms. Ann Rev Biochem 1987;56:289-315
    • (1987) Ann Rev Biochem , vol.56 , pp. 289-315
    • Thiel, E.C.1
  • 135
    • 0022403395 scopus 로고
    • Genes for the 'H' subunit of human ferritin are present on a number of human chromosomes
    • Cragg SJ, Drysdale J, Worwood M. Genes for the 'H' subunit of human ferritin are present on a number of human chromosomes. Hum Genet 1985;71: 108-12
    • (1985) Hum Genet , vol.71 , pp. 108-112
    • Cragg, S.J.1    Drysdale, J.2    Worwood, M.3
  • 136
    • 0022350427 scopus 로고
    • Human ferritin light chain gene sequences mapped to several assorted chromosomes
    • Lebo RV, Kan YW, Cheung MC, Jain SK, Drysdale J. Human ferritin light chain gene sequences mapped to several assorted chromosomes. Human Genet 1985;71:325-8
    • (1985) Human Genet , vol.71 , pp. 325-328
    • Lebo, R.V.1    Kan, Y.W.2    Cheung, M.C.3    Jain, S.K.4    Drysdale, J.5
  • 137
    • 0023216280 scopus 로고
    • Human ferritin H and L sequences lie on ten different chromosomes
    • McGill, JR, Naylor SL, Sakaguchi AY, et al. Human ferritin H and L sequences lie on ten different chromosomes. Human Genet 1987;76:66-70
    • (1987) Human Genet , vol.76 , pp. 66-70
    • McGill, J.R.1    Naylor, S.L.2    Sakaguchi, A.Y.3
  • 138
    • 0011239569 scopus 로고
    • Novel mechanism for translational control in regulation of ferritin synthesis by iron
    • Zahringer J, Baliga BS, Munro HN. Novel mechanism for translational control in regulation of ferritin synthesis by iron. Proc Natl Acad Sci USA 1976;73: 857-61
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 857-861
    • Zahringer, J.1    Baliga, B.S.2    Munro, H.N.3
  • 139
    • 0022646809 scopus 로고
    • Both subunits of rat liver ferritin are regulated at translational level by iron induction
    • Aziz N, Munro HN. Both subunits of rat liver ferritin are regulated at translational level by iron induction. Nucleic Acids Res 1986;14:915-27
    • (1986) Nucleic Acids Res , vol.14 , pp. 915-927
    • Aziz, N.1    Munro, H.N.2
  • 140
    • 0023884191 scopus 로고
    • Induction of ferritin subunit synthesis by iron is regulated at both the transcriptional and translational level
    • White K, Munro HN. Induction of ferritin subunit synthesis by iron is regulated at both the transcriptional and translational level. J Biol Chem 1988;263: 8938-42
    • (1988) J Biol Chem , vol.263 , pp. 8938-8942
    • White, K.1    Munro, H.N.2
  • 142
    • 0027237515 scopus 로고
    • Ferritin synthesis is controlled by iron-dependent translational derepression and by changes in synthesis/transport of nuclear ferritin RNAs
    • Coulson RMR, Cleveland DW. Ferritin synthesis is controlled by iron-dependent translational derepression and by changes in synthesis/transport of nuclear ferritin RNAs. Proc Natl Acad Sci USA 1993;90:7613-7
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7613-7617
    • Coulson, R.M.R.1    Cleveland, D.W.2
  • 143
    • 0025589263 scopus 로고
    • Ferritin mRNA translation, structure, and gene transcription during development of animals and plants
    • Thiel EC. Ferritin mRNA translation, structure, and gene transcription during development of animals and plants. Enzyme 1990;44:68-82
    • (1990) Enzyme , vol.44 , pp. 68-82
    • Thiel, E.C.1
  • 144
    • 0013834428 scopus 로고
    • An x-ray scattering study of ferritin and apoferritin
    • Fishbach FA, Andreregg JW. An x-ray scattering study of ferritin and apoferritin. J Mol Biol 1965;14: 458-73
    • (1965) J Mol Biol , vol.14 , pp. 458-473
    • Fishbach, F.A.1    Andreregg, J.W.2
  • 145
    • 0019939073 scopus 로고
    • Serum ferritin: A possible model for the assessment of nutrient stores
    • Cook JD, Skikne BS. Serum ferritin: a possible model for the assessment of nutrient stores. Am J Clin Nutr 1982;35:1180-5
    • (1982) Am J Clin Nutr , vol.35 , pp. 1180-1185
    • Cook, J.D.1    Skikne, B.S.2
  • 146
    • 0026472376 scopus 로고
    • Iron metabolism - New perspectives in view
    • Crichton R, Ward RJ. Iron metabolism - new perspectives in view. Biochemistry 1992;31:11255-64
    • (1992) Biochemistry , vol.31 , pp. 11255-11264
    • Crichton, R.1    Ward, R.J.2
  • 147
    • 0024245282 scopus 로고
    • Mechanism of ferritin iron uptake: Activity of the H-chain and deletion mapping of the ferro-oxidase site
    • Levi S, Luzzago A, Cesareni G, et al. Mechanism of ferritin iron uptake: activity of the H-chain and deletion mapping of the ferro-oxidase site. J Biol Chem 1988;263:18086-92
    • (1988) J Biol Chem , vol.263 , pp. 18086-18092
    • Levi, S.1    Luzzago, A.2    Cesareni, G.3
  • 148
    • 0024384482 scopus 로고
    • Expression and structure and functional properties of human ferritin L-chain from Escherichia coli
    • Levi S, Franceschinelli F, Cozzi A, Doerner MH, Arosio P. Expression and structure and functional properties of human ferritin L-chain from Escherichia coli. Biochemistry 1989;28:5179-85
    • (1989) Biochemistry , vol.28 , pp. 5179-5185
    • Levi, S.1    Franceschinelli, F.2    Cozzi, A.3    Doerner, M.H.4    Arosio, P.5
  • 149
    • 0026475825 scopus 로고
    • Evidence that H- and L-chains have cooperative roles in the iron-uptake mechanism of human ferritin
    • Levi S, Yewdall SJ, Harrison PM, et al. Evidence that H- and L-chains have cooperative roles in the iron-uptake mechanism of human ferritin. Biochem J 1992;288:591-6
    • (1992) Biochem J , vol.288 , pp. 591-596
    • Levi, S.1    Yewdall, S.J.2    Harrison, P.M.3
  • 150
    • 0026730687 scopus 로고
    • Stoichiometry of Fe(II) oxidation during ceruloplasmin-catalyzed loading of ferritin
    • De Silva D, Aust SD. Stoichiometry of Fe(II) oxidation during ceruloplasmin-catalyzed loading of ferritin. Arch Biochem Biophys 1992;298:259-64
    • (1992) Arch Biochem Biophys , vol.298 , pp. 259-264
    • De Silva, D.1    Aust, S.D.2
  • 151
    • 0029868538 scopus 로고    scopus 로고
    • Vitamin C driven free radical generation from iron
    • Herbert V, Shaw S, Jayatilleke E. Vitamin C driven free radical generation from iron. J Nutr 1996;126: 1213S-1220S
    • (1996) J Nutr , vol.126
    • Herbert, V.1    Shaw, S.2    Jayatilleke, E.3
  • 152
    • 0020740951 scopus 로고
    • The role of ascorbic acid in the turnover of storage iron
    • Roeser HP. The role of ascorbic acid in the turnover of storage iron. Sem Hematol 1983;20:91-100
    • (1983) Sem Hematol , vol.20 , pp. 91-100
    • Roeser, H.P.1
  • 153
    • 0021270247 scopus 로고
    • Non-random distribution of iron entering rat liver ferritin in vivo
    • Treffry A, Harrison PM. Non-random distribution of iron entering rat liver ferritin in vivo. Biochem J 1984;220:857-9
    • (1984) Biochem J , vol.220 , pp. 857-859
    • Treffry, A.1    Harrison, P.M.2
  • 154
    • 0026713685 scopus 로고
    • Haem binding to ferritin and possible mechanisms of physiological iron uptake and release by ferritin
    • Kuhn LC, Hentze MW. Haem binding to ferritin and possible mechanisms of physiological iron uptake and release by ferritin. J Inorg Biochem 1992;47: 175-81
    • (1992) J Inorg Biochem , vol.47 , pp. 175-181
    • Kuhn, L.C.1    Hentze, M.W.2
  • 155
    • 0026519144 scopus 로고
    • Haem binding to horse spleen ferritin and its effect on the rate of iron release
    • Kadir FH, al Massad F, Moore GR. Haem binding to horse spleen ferritin and its effect on the rate of iron release. Biochem J 1992;282:867-70
    • (1992) Biochem J , vol.282 , pp. 867-870
    • Kadir, F.H.1    Al Massad, F.2    Moore, G.R.3
  • 156
    • 0014691028 scopus 로고
    • Mobilization of liver iron by ferroxidase (ceruloplasmin)
    • Osaki S, Johnson DA, Freiden E. Mobilization of liver iron by ferroxidase (ceruloplasmin). J Biol Chem 1969;244:5757-65
    • (1969) J Biol Chem , vol.244 , pp. 5757-5765
    • Osaki, S.1    Johnson, D.A.2    Freiden, E.3
  • 158
    • 0021711350 scopus 로고
    • Biochemical studies on the isolation and characterisation of human spleen haemosiderin
    • Weir MP, Gibson JF, Peters TJ. Biochemical studies on the isolation and characterisation of human spleen haemosiderin. Biochem J 1984;223:31-8
    • (1984) Biochem J , vol.223 , pp. 31-38
    • Weir, M.P.1    Gibson, J.F.2    Peters, T.J.3
  • 163
    • 0018328652 scopus 로고
    • Plasma ferritin levels as an index of iron deficiency in women using intrauterine devices
    • Guillebaud J, Barnett MD, Gordon YB. Plasma ferritin levels as an index of iron deficiency in women using intrauterine devices. Br J Obstet Gynaecol 1979;86:51-5
    • (1979) Br J Obstet Gynaecol , vol.86 , pp. 51-55
    • Guillebaud, J.1    Barnett, M.D.2    Gordon, Y.B.3
  • 164
    • 0022657895 scopus 로고
    • Iron deficiency in women using modern copper intrauterine devices
    • Kivijarvi A, Timonen H, Rajamaki A, Gronroos M. Iron deficiency in women using modern copper intrauterine devices. Obstet Gynecol 1986;67:95-8
    • (1986) Obstet Gynecol , vol.67 , pp. 95-98
    • Kivijarvi, A.1    Timonen, H.2    Rajamaki, A.3    Gronroos, M.4
  • 165
    • 50549165951 scopus 로고
    • Aspirin and gastrointestinal bleeding chromate blood loss studies
    • Pierson RNJ, Holt PR, Watson RM, Keating RP. Aspirin and gastrointestinal bleeding chromate blood loss studies. Am J Med 1961;31:259-65
    • (1961) Am J Med , vol.31 , pp. 259-265
    • Pierson, R.N.J.1    Holt, P.R.2    Watson, R.M.3    Keating, R.P.4
  • 166
    • 0000826969 scopus 로고
    • The relationship between anemia and hookworm infection. Results of a survey of a rural Venezuelan population
    • Layrisse M, Roche M. The relationship between anemia and hookworm infection. Results of a survey of a rural Venezuelan population. Am J Hyg 1964;79:279-301
    • (1964) Am J Hyg , vol.79 , pp. 279-301
    • Layrisse, M.1    Roche, M.2
  • 167
    • 0019834156 scopus 로고
    • Cow milk feeding in infancy: Gastrointestinal blood loss and iron nutritional status
    • Fomon SJ, Ziegler EE, Nelson SE, Edwards BB. Cow milk feeding in infancy: gastrointestinal blood loss and iron nutritional status. J Pediatr 1981;98: 540-5
    • (1981) J Pediatr , vol.98 , pp. 540-545
    • Fomon, S.J.1    Ziegler, E.E.2    Nelson, S.E.3    Edwards, B.B.4
  • 168
    • 0002634779 scopus 로고
    • Analgesic-anti-pyretics and anti-inflammatory agents; drugs employed in the treatment of gout
    • Gilman AG, Goodman LS, Rall TW, Murad F, eds. New York: Macmillan
    • Flower RJ, Moncada S, Vane JR. Analgesic-anti-pyretics and anti-inflammatory agents; drugs employed in the treatment of gout. In: Gilman AG, Goodman LS, Rall TW, Murad F, eds. The Pharmacological Basis of Therapeutics, 7th ed. New York: Macmillan, 1985:682-728
    • (1985) The Pharmacological Basis of Therapeutics, 7th Ed. , pp. 682-728
    • Flower, R.J.1    Moncada, S.2    Vane, J.R.3
  • 169
    • 0000375207 scopus 로고
    • Adrenocorticotropic hormone; adrenocortical steroids and their synthetic analogs; inhibitors of adrenocortical steroid biosynthesis
    • Gilman AG, Goodman LS, Rall TW, Murad F, eds. New York: Macmillan
    • Haynes RC Jr, Murad F. Adrenocorticotropic hormone; adrenocortical steroids and their synthetic analogs; inhibitors of adrenocortical steroid biosynthesis. In: Gilman AG, Goodman LS, Rall TW, Murad F, eds. The Pharmacological Basis of Therapeutics, 7th ed. New York: Macmillan, 1985:1466-96
    • (1985) The Pharmacological Basis of Therapeutics, 7th Ed. , pp. 1466-1496
    • Haynes Jr., R.C.1    Murad, F.2
  • 170
    • 0023634584 scopus 로고
    • Clinical spectrum of hereditary hemorrhagic telangiectasia (Osler-Weber-Rendu disease)
    • Peery WH. Clinical spectrum of hereditary hemorrhagic telangiectasia (Osler-Weber-Rendu disease). Am J Med 1987;82:989-97
    • (1987) Am J Med , vol.82 , pp. 989-997
    • Peery, W.H.1
  • 171
    • 0017626225 scopus 로고
    • Effect of blood donation of iron stores as evaluated by serum ferritin
    • Finch CA, Cook JD, Labbe RF, Culala M. Effect of blood donation of iron stores as evaluated by serum ferritin. Blood 1977;50:441-7
    • (1977) Blood , vol.50 , pp. 441-447
    • Finch, C.A.1    Cook, J.D.2    Labbe, R.F.3    Culala, M.4
  • 172
    • 0023282177 scopus 로고
    • Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid attachment site
    • Jing S, Trowbridge IS. Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid attachment site. EMBO J 1987;6:327-31
    • (1987) EMBO J , vol.6 , pp. 327-331
    • Jing, S.1    Trowbridge, I.S.2
  • 174
    • 0022372141 scopus 로고
    • Regional localization of human transferrin receptor gene to 3q26.2 - Qter
    • Rabin M, McClelland A, Kuhn L, Ruddle FH. Regional localization of human transferrin receptor gene to 3q26.2 - qter. Am J Human Genet 1985;37:1112-6
    • (1985) Am J Human Genet , vol.37 , pp. 1112-1116
    • Rabin, M.1    McClelland, A.2    Kuhn, L.3    Ruddle, F.H.4
  • 176
    • 0023882711 scopus 로고
    • Iron-responsive elements: Regulatory RNA sequences that control mRNA levels and translation
    • Casey JL, Hentze MW, Koeller DM, et al. Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation. Science 1988;240:924-28
    • (1988) Science , vol.240 , pp. 924-928
    • Casey, J.L.1    Hentze, M.W.2    Koeller, D.M.3
  • 177
    • 0026513802 scopus 로고
    • Effect of iron and retinoic acid on the control of transferrin receptor and ferritin in the human promonocytic cell line U937
    • Iturralde M, Vass JK, Oria R, Brock JH. Effect of iron and retinoic acid on the control of transferrin receptor and ferritin in the human promonocytic cell line U937. Biochim Biophys Acta 1992;1133:241-6
    • (1992) Biochim Biophys Acta , vol.1133 , pp. 241-246
    • Iturralde, M.1    Vass, J.K.2    Oria, R.3    Brock, J.H.4
  • 178
    • 0021685289 scopus 로고
    • The human transferrin receptor gene: Genomic organisation and the complete primary structure of the receptor deduced from a cDNA sequence
    • McClelland A, Kuhn LC, Ruddle FH. The human transferrin receptor gene: genomic organisation and the complete primary structure of the receptor deduced from a cDNA sequence. Cell 1984;39:267-74
    • (1984) Cell , vol.39 , pp. 267-274
    • McClelland, A.1    Kuhn, L.C.2    Ruddle, F.H.3
  • 179
    • 0025635559 scopus 로고
    • Transferrin internalization sequence YXRF implicates a tight turn as the structural recognition motif for internalization
    • Collawa JF, Stangel M, Kuhn LA, et al. Transferrin internalization sequence YXRF implicates a tight turn as the structural recognition motif for internalization. Cell 1990;63:1061-72
    • (1990) Cell , vol.63 , pp. 1061-1072
    • Collawa, J.F.1    Stangel, M.2    Kuhn, L.A.3
  • 180
    • 0022974705 scopus 로고
    • Identification of serine 24 as the unique site on the transferrin receptor phosphorylated by protein kinase C
    • Davis RJ, Johnson GL, Kelleher DJ, Anderson JK, Mole JE, Czech MP. Identification of serine 24 as the unique site on the transferrin receptor phosphorylated by protein kinase C. J Biol Chem 1986;261:9034-41
    • (1986) J Biol Chem , vol.261 , pp. 9034-9041
    • Davis, R.J.1    Johnson, G.L.2    Kelleher, D.J.3    Anderson, J.K.4    Mole, J.E.5    Czech, M.P.6
  • 181
    • 1842341609 scopus 로고
    • Phosphorylation of the human transferrin receptor by protein kinase C is not required for endocytosis and recycling in mouse 3T3 cells
    • Zerial M, Suomalainen M, Zanetti-Schneider M, Schneider C, Garoff H. Phosphorylation of the human transferrin receptor by protein kinase C is not required for endocytosis and recycling in mouse 3T3 cells. EMBO J 1987;6:2661-7
    • (1987) EMBO J , vol.6 , pp. 2661-2667
    • Zerial, M.1    Suomalainen, M.2    Zanetti-Schneider, M.3    Schneider, C.4    Garoff, H.5
  • 182
    • 0022749229 scopus 로고
    • The transmembrane segment of the human transferrin receptor functions as a signal peptide
    • Zerial M, Melancon P, Schneider C, Garoff H. The transmembrane segment of the human transferrin receptor functions as a signal peptide. EMBO J 1986;5:1543-50
    • (1986) EMBO J , vol.5 , pp. 1543-1550
    • Zerial, M.1    Melancon, P.2    Schneider, C.3    Garoff, H.4
  • 183
    • 0018592009 scopus 로고
    • Transferrin in human placental brush border membranes
    • Wada HD, Mass PE, Sussman HH. Transferrin in human placental brush border membranes. J Biol Chem 1979;254:12629-35
    • (1979) J Biol Chem , vol.254 , pp. 12629-12635
    • Wada, H.D.1    Mass, P.E.2    Sussman, H.H.3
  • 184
    • 0021265943 scopus 로고
    • The effect of iron saturation of transferrin on its binding and uptake by rabbit reticulocytes
    • Young SP, Bomford A, Williams R. The effect of iron saturation of transferrin on its binding and uptake by rabbit reticulocytes. Biochem J 1984;219:505-10
    • (1984) Biochem J , vol.219 , pp. 505-510
    • Young, S.P.1    Bomford, A.2    Williams, R.3
  • 185
    • 0020354532 scopus 로고
    • Transferrin receptors and iron uptake during erythroid cell development
    • Iacopetta BJ, Morgan EH, Yeoh GCT. Transferrin receptors and iron uptake during erythroid cell development. Biochim Biophys Acta 1982;687:204-10
    • (1982) Biochim Biophys Acta , vol.687 , pp. 204-210
    • Iacopetta, B.J.1    Morgan, E.H.2    Yeoh, G.C.T.3
  • 186
    • 0021933559 scopus 로고
    • Rapid endocytosis of the transferrin receptor in the absence of bound transferrin
    • Watts CA. Rapid endocytosis of the transferrin receptor in the absence of bound transferrin. J Cell Biol 1985;100:633-7
    • (1985) J Cell Biol , vol.100 , pp. 633-637
    • Watts, C.A.1
  • 187
    • 0342291152 scopus 로고
    • Rapid internalization of the transferrin receptor in K562 cells is triggered by ligand binding or treatment with a phorbol ester
    • Klausner RD, Hartford J, van Renswoude J. Rapid internalization of the transferrin receptor in K562 cells is triggered by ligand binding or treatment with a phorbol ester. Proc Natl Acad Sci USA 1984;81: 3005-9
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3005-3009
    • Klausner, R.D.1    Hartford, J.2    Van Renswoude, J.3
  • 188
    • 0027181635 scopus 로고
    • The anion requirement for iron release from transferrin is preserved in the receptor transferrin complex
    • Egan TJ, Zak O, Aisen P. The anion requirement for iron release from transferrin is preserved in the receptor transferrin complex. Biochemistry 1993;32: 8162-7
    • (1993) Biochemistry , vol.32 , pp. 8162-8167
    • Egan, T.J.1    Zak, O.2    Aisen, P.3
  • 189
    • 0025924788 scopus 로고
    • A new role for the transferrin receptor in the release of iron from transferrin
    • Bali PK, Zak O, Aisen P. A new role for the transferrin receptor in the release of iron from transferrin. Biochemistry 1991;30:324-9
    • (1991) Biochemistry , vol.30 , pp. 324-329
    • Bali, P.K.1    Zak, O.2    Aisen, P.3
  • 191
    • 0027222141 scopus 로고
    • NAD(P)H:ferric iron reductase in endosomal membranes from rat liver
    • Scheiber B, Goldenberg H. NAD(P)H:ferric iron reductase in endosomal membranes from rat liver. Arch Biochem Biophys 1993;305:225-30
    • (1993) Arch Biochem Biophys , vol.305 , pp. 225-230
    • Scheiber, B.1    Goldenberg, H.2
  • 192
    • 0026623265 scopus 로고
    • Effect of ascorbate in the reduction of transferrin-associated iron in endocytic vesicles
    • Escobar A, Gaete V, Núñez MT. Effect of ascorbate in the reduction of transferrin-associated iron in endocytic vesicles. J Bioenerg Biomembrane 1992;24: 227-33
    • (1992) J Bioenerg Biomembrane , vol.24 , pp. 227-233
    • Escobar, A.1    Gaete, V.2    Núñez, M.T.3
  • 193
    • 0026787076 scopus 로고
    • Intermediate steps in cellular iron uptake from transferrin. Detection of a cytoplasmic pool of iron, free of transferrin
    • Richardson DR, Baker E. Intermediate steps in cellular iron uptake from transferrin. Detection of a cytoplasmic pool of iron, free of transferrin. J Biol Chem 1992;267:21384-9
    • (1992) J Biol Chem , vol.267 , pp. 21384-21389
    • Richardson, D.R.1    Baker, E.2
  • 194
    • 0028283493 scopus 로고
    • +-ATPase from reticulocyte endosomes reconstituted into liposomes acts as an iron transporter
    • +-ATPase from reticulocyte endosomes reconstituted into liposomes acts as an iron transporter. J Biol Chem 1994;269:10242-6
    • (1994) J Biol Chem , vol.269 , pp. 10242-10246
    • Li, C.Y.1    Watkins, J.A.2    Glass, J.3
  • 195
    • 0021137528 scopus 로고
    • Selective externalization of the transferrin receptor by sheep reticulocytes in vitro. Response to ligands and inhibitors of endocytosis
    • Pan BT, Johnstone R. Selective externalization of the transferrin receptor by sheep reticulocytes in vitro. Response to ligands and inhibitors of endocytosis. J Biol Chem 1984;259:9776-82
    • (1984) J Biol Chem , vol.259 , pp. 9776-9782
    • Pan, B.T.1    Johnstone, R.2
  • 196
    • 0026038910 scopus 로고
    • Shedding of transferrin receptor from rat reticulocytes during maturation in vitro: Soluble transferrin receptor is derived from receptor shed in vesicles
    • Chitambar CR, Loebel AL, Noble NA. Shedding of transferrin receptor from rat reticulocytes during maturation in vitro: soluble transferrin receptor is derived from receptor shed in vesicles. Blood 1991;78: 2444-2450
    • (1991) Blood , vol.78 , pp. 2444-2450
    • Chitambar, C.R.1    Loebel, A.L.2    Noble, N.A.3
  • 197
    • 0022547495 scopus 로고
    • Circulating transferrin receptor in human serum
    • Kongo Y, Nishisato T, Kondo H, et al. Circulating transferrin receptor in human serum. Br J Haematol 1986;64:277-81
    • (1986) Br J Haematol , vol.64 , pp. 277-281
    • Kongo, Y.1    Nishisato, T.2    Kondo, H.3
  • 199
    • 33645370514 scopus 로고
    • The size of small molecular weight iron pools in rat tissues
    • Saltman P, Hagenaue J, eds. New York: Elsevier
    • Mulligan M, Linder M. The size of small molecular weight iron pools in rat tissues. In: Saltman P, Hagenaue J, eds. The Biochemistry and Physiology of Iron. New York: Elsevier, 1982 p 313-314
    • (1982) The Biochemistry and Physiology of Iron , pp. 313-314
    • Mulligan, M.1    Linder, M.2
  • 200
    • 0022437471 scopus 로고
    • Non-ferritin, non-heme iron pools in rat tissues
    • Mulligan M, Althaus B, Linder MC. Non-ferritin, non-heme iron pools in rat tissues. Int J Biochem 1986;18:791-801
    • (1986) Int J Biochem , vol.18 , pp. 791-801
    • Mulligan, M.1    Althaus, B.2    Linder, M.C.3
  • 201
    • 0024473778 scopus 로고
    • Low molecular weight isolated from guinea pig reticulocytes as AMP-iron and ATP-iron complexes
    • Weaver J, Pollack S. Low molecular weight isolated from guinea pig reticulocytes as AMP-iron and ATP-iron complexes. Biochem J 1989;261:787-93
    • (1989) Biochem J , vol.261 , pp. 787-793
    • Weaver, J.1    Pollack, S.2
  • 202
    • 0025822118 scopus 로고
    • Identification of a novel iron-responsive element in murine and human erythroid d-aminolevulinic acid synthase mRNA
    • Dandekar T, Stripecke R, Gray NK, et al. Identification of a novel iron-responsive element in murine and human erythroid d-aminolevulinic acid synthase mRNA. EMBO J 1991;10:1903-9
    • (1991) EMBO J , vol.10 , pp. 1903-1909
    • Dandekar, T.1    Stripecke, R.2    Gray, N.K.3
  • 203
    • 0345246445 scopus 로고
    • Regulation of cytochrome P-450 b/e gene expression by a heme- and phenobarbitone-modulated transcription factor
    • Rangarajan PN, Padmanaban G. Regulation of cytochrome P-450 b/e gene expression by a heme- and phenobarbitone-modulated transcription factor. Proc Natl Acad Sci USA 1989;86:3963-7
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3963-3967
    • Rangarajan, P.N.1    Padmanaban, G.2
  • 204
    • 0024427488 scopus 로고
    • Receptor-mediated transport of heme by hemopexin regulates gene expression in mammalian cells
    • Alam J, Smith A. Receptor-mediated transport of heme by hemopexin regulates gene expression in mammalian cells. J Biol Chem 1989;264:17637-40
    • (1989) J Biol Chem , vol.264 , pp. 17637-17640
    • Alam, J.1    Smith, A.2
  • 205
    • 0026665256 scopus 로고
    • Heme-hemopexin-mediated induction of metallothionein gene expression
    • Alam J, Smith A. Heme-hemopexin-mediated induction of metallothionein gene expression. J Biol Chem 1992;267:16379-84
    • (1992) J Biol Chem , vol.267 , pp. 16379-16384
    • Alam, J.1    Smith, A.2
  • 206
    • 0026782841 scopus 로고
    • Mutagenesis of the iron-regulatory element further defines a role for rna secondary structure in the regulation of ferritin and transferrin receptor expression
    • Bettany A, Eisenstein RS, Munro HN. Mutagenesis of the iron-regulatory element further defines a role for rna secondary structure in the regulation of ferritin and transferrin receptor expression. J Biol Chem 1992;267:16531-7
    • (1992) J Biol Chem , vol.267 , pp. 16531-16537
    • Bettany, A.1    Eisenstein, R.S.2    Munro, H.N.3
  • 207
    • 0012198506 scopus 로고
    • Iron-dependent regulation of ferritin synthesis
    • Berdanier C, Hargrove JL, eds. Boca Raton: CRC Press
    • Munro HN, Kikinis Z, Eisenstein RS. Iron-dependent regulation of ferritin synthesis. In: Berdanier C, Hargrove JL, eds. Nutrition and Gene Expression. Boca Raton: CRC Press, 1993:525-45
    • (1993) Nutrition and Gene Expression , pp. 525-545
    • Munro, H.N.1    Kikinis, Z.2    Eisenstein, R.S.3
  • 208
    • 0024276911 scopus 로고
    • A stem-loop in the 3′ untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm
    • Müllner EW, Kühn LC. A stem-loop in the 3′ untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm. Cell 1988;53:815-25
    • (1988) Cell , vol.53 , pp. 815-825
    • Müllner, E.W.1    Kühn, L.C.2
  • 209
    • 0023336087 scopus 로고
    • Noncoding 3′ sequences of the transferrin receptor gene are required for mRNA regulation by iron
    • Owen D, Kuhn LC. Noncoding 3′ sequences of the transferrin receptor gene are required for mRNA regulation by iron. EMBO J 1987;6:1287-95
    • (1987) EMBO J , vol.6 , pp. 1287-1295
    • Owen, D.1    Kuhn, L.C.2
  • 210
    • 0024819020 scopus 로고
    • Iron regulation of transferrin receptor mRNA requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA
    • Casey JL, Koeller DM, Ramin VC, Klausner RD, Harford JB. Iron regulation of transferrin receptor mRNA requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA. EMBO J 1989;8:3693-9
    • (1989) EMBO J , vol.8 , pp. 3693-3699
    • Casey, J.L.1    Koeller, D.M.2    Ramin, V.C.3    Klausner, R.D.4    Harford, J.B.5
  • 211
    • 0027048349 scopus 로고
    • Binding of cytosolic aconitase to the iron responsive element of porcine mitochondrial aconitase mRNA
    • Zheng L, Kennedy MC, Blondin GA, Beinert H, Zalkin H. Binding of cytosolic aconitase to the iron responsive element of porcine mitochondrial aconitase mRNA. Arch Biochem Biophys 1992;299:356-60
    • (1992) Arch Biochem Biophys , vol.299 , pp. 356-360
    • Zheng, L.1    Kennedy, M.C.2    Blondin, G.A.3    Beinert, H.4    Zalkin, H.5
  • 212
    • 0023476064 scopus 로고
    • Iron regulates ferritin mRNA translation through a segment of its 5′ untranslated region
    • Aziz N, Munro HN. Iron regulates ferritin mRNA translation through a segment of its 5′ untranslated region. Proc Natl Acad Sci USA 1987;84:8478-82
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8478-8482
    • Aziz, N.1    Munro, H.N.2
  • 213
    • 0024121621 scopus 로고
    • Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs
    • Leibold EA, Munro HN. Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs. Proc Natl Acad Sci USA 1988;85: 2171-5
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 214
    • 0027503294 scopus 로고
    • Translational control of 5-aminolevulinate synthase mRNA by iron-responsive elements in erythroid cells
    • Melefors Ö, Goossen B, Johansson HE, Stripecke R, Gray NK, Hentze MW. Translational control of 5-aminolevulinate synthase mRNA by iron-responsive elements in erythroid cells. J Biol Chem 1993;268:5974-8
    • (1993) J Biol Chem , vol.268 , pp. 5974-5978
    • Melefors, Ö.1    Goossen, B.2    Johansson, H.E.3    Stripecke, R.4    Gray, N.K.5    Hentze, M.W.6
  • 215
    • 0026716016 scopus 로고
    • Clinically-silent mutation in the putative iron-responsive element in exon-17 of the beta-amyloid precursor protein gene
    • Panter SS, Braughler JM, Hall ED. Clinically-silent mutation in the putative iron-responsive element in exon-17 of the beta-amyloid precursor protein gene. J Neuropathol Exp Neurol 1992;51:459-63
    • (1992) J Neuropathol Exp Neurol , vol.51 , pp. 459-463
    • Panter, S.S.1    Braughler, J.M.2    Hall, E.D.3
  • 216
    • 0026716016 scopus 로고
    • Clinically silent mutation in the putative iron-response element in exon 17 of the β-amyloid precursor protein gene
    • Zubenko GS, Farr J, Stiffer JS, Hughes HB, Kaplan BB. Clinically silent mutation in the putative iron-response element in exon 17 of the β-amyloid precursor protein gene. J Neuropathol Exp Neurol 1992;51:459-66
    • (1992) J Neuropathol Exp Neurol , vol.51 , pp. 459-466
    • Zubenko, G.S.1    Farr, J.2    Stiffer, J.S.3    Hughes, H.B.4    Kaplan, B.B.5
  • 217
    • 0011938466 scopus 로고
    • Translational repression in eukaryotes: Partial purification and characterization of a repressor of ferritin mRNA translation
    • Walden WE, Daniels-McQueen S, Brown PH, et al. Translational repression in eukaryotes: partial purification and characterization of a repressor of ferritin mRNA translation. Proc Natl Acad Sci USA 1988;85:9503-7
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 9503-9507
    • Walden, W.E.1    Daniels-McQueen, S.2    Brown, P.H.3
  • 218
    • 0024365045 scopus 로고
    • A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA
    • Müllner EW, Neupert B, Kühn LC. A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA. Cell 1989;58:373-82
    • (1989) Cell , vol.58 , pp. 373-382
    • Müllner, E.W.1    Neupert, B.2    Kühn, L.C.3
  • 219
    • 0025882090 scopus 로고
    • Ferritin mRNA: Interactions of iron regulatory elements with translational regulator protein P-90 and the effect on base-paired flanking regions
    • Harrell CM, McKenzie AR, Patino MM, Walden WE, Thiel EC. Ferritin mRNA: interactions of iron regulatory elements with translational regulator protein P-90 and the effect on base-paired flanking regions. Proc Natl Acad Sci USA 1991;88:4166-70
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4166-4170
    • Harrell, C.M.1    McKenzie, A.R.2    Patino, M.M.3    Walden, W.E.4    Thiel, E.C.5
  • 220
    • 0026658472 scopus 로고
    • In vivo and in vitro modulation of the mRNA-binding activity of iron-regulatory factor. Tissue distribution and effects of cell proliferation, iron levels and redox state
    • Müllner EW, Rothenberger S, Müller AM, Kühn LC. In vivo and in vitro modulation of the mRNA-binding activity of iron-regulatory factor. Tissue distribution and effects of cell proliferation, iron levels and redox state. Eur J Biochem 1992;208:597-605
    • (1992) Eur J Biochem , vol.208 , pp. 597-605
    • Müllner, E.W.1    Rothenberger, S.2    Müller, A.M.3    Kühn, L.C.4
  • 221
    • 0024360593 scopus 로고
    • Chromosomal localization of nucleic acid-binding proteins by affinity mapping: Assignment of the IRE-binding protein gene to human chromosome 9
    • Hentz MW, Senanez HN, O'Brien SJ, Hartford JB, Klausner RD. Chromosomal localization of nucleic acid-binding proteins by affinity mapping: assignment of the IRE-binding protein gene to human chromosome 9. Nucleic Acids Res 1989;17:6103-8
    • (1989) Nucleic Acids Res , vol.17 , pp. 6103-6108
    • Hentz, M.W.1    Senanez, H.N.2    O'Brien, S.J.3    Hartford, J.B.4    Klausner, R.D.5
  • 222
    • 0026736834 scopus 로고
    • The iron-responsive element binding protein - Purification, cloning, and regulation in rat liver
    • Yu Y, Radisky E, Leibold EA. The iron-responsive element binding protein - purification, cloning, and regulation in rat liver. J Biol Chem 1992;267:19005-10
    • (1992) J Biol Chem , vol.267 , pp. 19005-19010
    • Yu, Y.1    Radisky, E.2    Leibold, E.A.3
  • 223
    • 0025865421 scopus 로고
    • Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase
    • Hentz MW, Argos P. Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase. Nucleic Acids Res 1991;19:1739-40
    • (1991) Nucleic Acids Res , vol.19 , pp. 1739-1740
    • Hentz, M.W.1    Argos, P.2
  • 224
    • 0027081042 scopus 로고
    • Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein
    • Kennedy MC, Mende-Mueller L, Blondin GA, Beinert H. Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc Natl Acad Sci USA 1992;89:11730-4
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 225
    • 0026483360 scopus 로고
    • Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation
    • Tang CK, Chin J, Harford JB, Klausner RD, Rouault TA. Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation. J Biol Chem 1992;267: 24466-70
    • (1992) J Biol Chem , vol.267 , pp. 24466-24470
    • Tang, C.K.1    Chin, J.2    Harford, J.B.3    Klausner, R.D.4    Rouault, T.A.5
  • 226
    • 0026756095 scopus 로고
    • Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein - Role of the iron-sulfur cluster
    • Haile DJ, Rouault TA, Tang CK, Chin J, Hartford JB, Klausner RD. Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein - role of the iron-sulfur cluster. Proc Natl Acad Sci USA 1992;89: 7536-40
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7536-7540
    • Haile, D.J.1    Rouault, T.A.2    Tang, C.K.3    Chin, J.4    Hartford, J.B.5    Klausner, R.D.6
  • 227
    • 0027050315 scopus 로고
    • Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron-sulfur cluster results in high affinity RNA binding
    • Haile DJ, Rouault TA, Hartford JB, Kennedy MC, Blondin GA, Beinert H, Klausner RD. Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high affinity RNA binding. Proc Natl Acad Sci USA 1992;89:11735-9
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11735-11739
    • Haile, D.J.1    Rouault, T.A.2    Hartford, J.B.3    Kennedy, M.C.4    Blondin, G.A.5    Beinert, H.6    Klausner, R.D.7
  • 228
    • 0027297916 scopus 로고
    • Iron regulatory factor expressed from recombinant baculovirus - Conversion between the RNA-binding apoprotein and Fe-S cluster containing aconitase
    • Emery-Goodman A, Hirling H, Scarpellino L, Henderson B, Kühn LC. Iron regulatory factor expressed from recombinant baculovirus - conversion between the RNA-binding apoprotein and Fe-S cluster containing aconitase. Nucleic Acids Res 1993;21:1457-61
    • (1993) Nucleic Acids Res , vol.21 , pp. 1457-1461
    • Emery-Goodman, A.1    Hirling, H.2    Scarpellino, L.3    Henderson, B.4    Kühn, L.C.5
  • 229
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier JC, Hirling H, Wietzerbin J, Kaldy P, Kühn LC. Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J 1993;12: 3643-9
    • (1993) EMBO J , vol.12 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kühn, L.C.5
  • 230
    • 0027184412 scopus 로고
    • Translational regulation via iron-responsive elements by the nitric oxide/NO-synthase pathway
    • Weiss G, Goossen B, Doppler W, et al. Translational regulation via iron-responsive elements by the nitric oxide/NO-synthase pathway. EMBO J 1993;12: 3651-7
    • (1993) EMBO J , vol.12 , pp. 3651-3657
    • Weiss, G.1    Goossen, B.2    Doppler, W.3
  • 232
    • 0027717217 scopus 로고
    • Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements
    • Henderson BR, Seiser C, Kühn LC. Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements. J Biol Chem 1993;268:27327-34
    • (1993) J Biol Chem , vol.268 , pp. 27327-27334
    • Henderson, B.R.1    Seiser, C.2    Kühn, L.C.3
  • 234
    • 0242303463 scopus 로고
    • Iron-dependent enzymes in mammalian systems
    • Ponka P, ed. Boca Raton: CRC Press
    • Cammack R, Wriggleworth JM, Baum H. Iron-dependent enzymes in mammalian systems. In: Ponka P, ed. Iron Transport and Storage. Boca Raton: CRC Press, 1990:17-39
    • (1990) Iron Transport and Storage , pp. 17-39
    • Cammack, R.1    Wriggleworth, J.M.2    Baum, H.3
  • 235
    • 0022464750 scopus 로고
    • Biochemical basis for the manifestations of iron deficiency
    • Dallman PR. Biochemical basis for the manifestations of iron deficiency. Ann Rev Nutr 1986;6:13-40
    • (1986) Ann Rev Nutr , vol.6 , pp. 13-40
    • Dallman, P.R.1
  • 236
    • 0025765126 scopus 로고
    • The P450 superfamily: Update on new sequences, gene mapping, and recommended nomenclature
    • Nebert DW, Nelson DR, Coon MJ, et al. The P450 superfamily: update on new sequences, gene mapping, and recommended nomenclature. DNA Cell Biol 1991;10:1-33
    • (1991) DNA Cell Biol , vol.10 , pp. 1-33
    • Nebert, D.W.1    Nelson, D.R.2    Coon, M.J.3
  • 237
    • 0026660191 scopus 로고
    • Spectral characterization of brain and macrophage nitric oxide synthases. Cytochrome P-450-like hemeproteins that contain a flavin semiquinone radical
    • Stuehr DJ, Ikeda SM. Spectral characterization of brain and macrophage nitric oxide synthases. Cytochrome P-450-like hemeproteins that contain a flavin semiquinone radical. J Biol Chem 1992;267: 20547-50
    • (1992) J Biol Chem , vol.267 , pp. 20547-20550
    • Stuehr, D.J.1    Ikeda, S.M.2
  • 238
    • 0026735580 scopus 로고
    • Nitric oxide synthase is a cytochrome P450 type hemoprotein
    • White KA, Marietta MA. Nitric oxide synthase is a cytochrome P450 type hemoprotein. Biochemistry 1992;31:6627-31
    • (1992) Biochemistry , vol.31 , pp. 6627-6631
    • White, K.A.1    Marietta, M.A.2
  • 239
    • 0025848403 scopus 로고
    • Brain nitric oxide synthase is a biopterin- and flavin-containing multi-functional oxido-reductase
    • Mayer B, John M, Heinzel B, Werner ER, et al. Brain nitric oxide synthase is a biopterin- and flavin-containing multi-functional oxido-reductase. Febs Lett 1991;288:187-91
    • (1991) Febs Lett , vol.288 , pp. 187-191
    • Mayer, B.1    John, M.2    Heinzel, B.3    Werner, E.R.4
  • 240
    • 0025160342 scopus 로고
    • Neuroendocrine alterations in iron deficiency
    • Beard JL. Neuroendocrine alterations in iron deficiency. Prog Food Nutr Sci 1990;14:45-82
    • (1990) Prog Food Nutr Sci , vol.14 , pp. 45-82
    • Beard, J.L.1
  • 241
    • 0019508918 scopus 로고
    • Spectral electroencephalographic correlates of iron status: Tired blood revisited
    • Tucker DM, Sandstead HH. Spectral electroencephalographic correlates of iron status: tired blood revisited. Physiol Behav 1981;26:439-49
    • (1981) Physiol Behav , vol.26 , pp. 439-449
    • Tucker, D.M.1    Sandstead, H.H.2
  • 242
  • 246
    • 0023229229 scopus 로고
    • Recommended dietary intakes (RDI) of iron in humans
    • Herbert V. Recommended dietary intakes (RDI) of iron in humans. Am J Clin Nutr 1987;45:679-86
    • (1987) Am J Clin Nutr , vol.45 , pp. 679-686
    • Herbert, V.1
  • 247
    • 0026633933 scopus 로고
    • Serum transferrin receptor distinguishes the anemia of chronic disease from iron deficiency anemia
    • Ferguson BJ, Skikne BS, Simpson KM, Baynes RD, Cook JD. Serum transferrin receptor distinguishes the anemia of chronic disease from iron deficiency anemia. J Lab Clin Med 1992;119:385-90
    • (1992) J Lab Clin Med , vol.119 , pp. 385-390
    • Ferguson, B.J.1    Skikne, B.S.2    Simpson, K.M.3    Baynes, R.D.4    Cook, J.D.5
  • 248
    • 0003094261 scopus 로고
    • Iron deficiency
    • Clydesdale F, Weimer KL, eds. New York: Academic Press
    • Beard JL, Finch CA. Iron deficiency. In: Clydesdale F, Weimer KL, eds. Iron Fortification of Foods. New York: Academic Press, 1985 p 3-16
    • (1985) Iron Fortification of Foods , pp. 3-16
    • Beard, J.L.1    Finch, C.A.2
  • 249
    • 0020035215 scopus 로고
    • Perspectives in iron metabolism
    • Finch CA, Heubers H. Perspectives in iron metabolism. N Engl J Med 1982;306:1520-8
    • (1982) N Engl J Med , vol.306 , pp. 1520-1528
    • Finch, C.A.1    Heubers, H.2
  • 250
    • 0025996715 scopus 로고
    • Day-to-day variation in iron-status indices in healthy men and women
    • Borel MJ, Smith SM, Derr J, Beard JL. Day-to-day variation in iron-status indices in healthy men and women. Am J Clin Nutr 1991;54:729-35
    • (1991) Am J Clin Nutr , vol.54 , pp. 729-735
    • Borel, M.J.1    Smith, S.M.2    Derr, J.3    Beard, J.L.4
  • 252
    • 12644255679 scopus 로고
    • Washington, DC: International Life Science Institute
    • Measurement of Iron Status. Washington, DC: International Life Science Institute, 1984
    • (1984) Measurement of Iron Status
  • 253
    • 0016667173 scopus 로고
    • A clinical evaluation of serum ferritin as an index of iron stores
    • Lipschitz DA, Cook JD, Finch CA. A clinical evaluation of serum ferritin as an index of iron stores. Proc Soc Exp Biol Med 1975;148:358-64
    • (1975) Proc Soc Exp Biol Med , vol.148 , pp. 358-364
    • Lipschitz, D.A.1    Cook, J.D.2    Finch, C.A.3
  • 254
    • 12644284487 scopus 로고
    • Increased serum ferritin levels in hyperthyroidism
    • Macaron CI, Macaron ZG. Increased serum ferritin levels in hyperthyroidism. J Clin Endocrinol Metab 1985;61:672-6
    • (1985) J Clin Endocrinol Metab , vol.61 , pp. 672-676
    • Macaron, C.I.1    Macaron, Z.G.2
  • 255
  • 256
    • 0012485318 scopus 로고
    • Tissue effects of iron deficiency
    • Jacobs A, Worwood M, eds. London: Academic Press
    • Dallman PR. Tissue effects of iron deficiency. In: Jacobs A, Worwood M, eds. Iron in Biochemistry and Medicine. London: Academic Press, 1974 p 437-476
    • (1974) Iron in Biochemistry and Medicine , pp. 437-476
    • Dallman, P.R.1
  • 257
    • 0021193844 scopus 로고
    • Transferrin: Physiologic behavior and clinical implications
    • Huebers HA, Finch CA. Transferrin: physiologic behavior and clinical implications. Blood 1984;64:763-7
    • (1984) Blood , vol.64 , pp. 763-767
    • Huebers, H.A.1    Finch, C.A.2
  • 258
    • 0020005494 scopus 로고
    • Manifestations of iron deficiency
    • Dallman PR. Manifestations of iron deficiency. Semin Hematol 1982;19:19-30
    • (1982) Semin Hematol , vol.19 , pp. 19-30
    • Dallman, P.R.1
  • 259
    • 0018849687 scopus 로고
    • Manifestations of iron deficiency at various levels of dietary iron intake
    • Siimes MA, Refino C, Dallman PR. Manifestations of iron deficiency at various levels of dietary iron intake. Am J Clin Nutr 1980;33:570-4
    • (1980) Am J Clin Nutr , vol.33 , pp. 570-574
    • Siimes, M.A.1    Refino, C.2    Dallman, P.R.3
  • 260
    • 0026546708 scopus 로고
    • The soluble transferrin receptor: Biological aspects and clinical usefulness as quantitative measure of erythropoiesis
    • Beguin Y. The soluble transferrin receptor: biological aspects and clinical usefulness as quantitative measure of erythropoiesis [editorial]. Haematologica 1992;77:1-10
    • (1992) Haematologica , vol.77 , pp. 1-10
    • Beguin, Y.1
  • 262
    • 0027160748 scopus 로고
    • The transferrin receptor: Its diagnostic value and its potential as therapeutic target
    • Thorsterisen K, Romslo I. The transferrin receptor: its diagnostic value and its potential as therapeutic target. Scan J Clin Lab Invest 1993;53(Suppl 215): 113-20
    • (1993) Scan J Clin Lab Invest , vol.53 , Issue.215 SUPPL. , pp. 113-120
    • Thorsterisen, K.1    Romslo, I.2
  • 263
    • 0025840286 scopus 로고
    • Serum transferrin receptor for the detection of iron deficiency in pregnancy
    • Carriaga MT, Skikne BS, Finley B, Cutler B, Cook JD. Serum transferrin receptor for the detection of iron deficiency in pregnancy. Am J Clin Nutr 1991;54:1077-81
    • (1991) Am J Clin Nutr , vol.54 , pp. 1077-1081
    • Carriaga, M.T.1    Skikne, B.S.2    Finley, B.3    Cutler, B.4    Cook, J.D.5
  • 264
    • 0025271562 scopus 로고
    • Serum transferrin receptor: A quantitative measure of tissue iron deficiency
    • Skikne BS, Flowers CH, Cook JD. Serum transferrin receptor: a quantitative measure of tissue iron deficiency. Blood 1990;75:1870-6
    • (1990) Blood , vol.75 , pp. 1870-1876
    • Skikne, B.S.1    Flowers, C.H.2    Cook, J.D.3
  • 266
  • 267
    • 0022396603 scopus 로고
    • Summary of a report on assessment of the iron nutritional status of the United States population
    • Group ESW. Summary of a report on assessment of the iron nutritional status of the United States population. Am J Clin Nutr 1985;42:1318-30
    • (1985) Am J Clin Nutr , vol.42 , pp. 1318-1330
  • 271
    • 0003673876 scopus 로고
    • Washington, DC: The National Academy of Sciences
    • National Research Council, Food and Nutrition Board. Recommended Dietary Allowances, 10th ed. Washington, DC: The National Academy of Sciences, 1989
    • (1989) Recommended Dietary Allowances, 10th Ed.
  • 272
    • 0001920592 scopus 로고
    • Changing iron needs from birth to adolescence
    • Fomon SJ, Zlotkin S, eds. New York: Vervey/Raven Press
    • Dallman PR. Changing iron needs from birth to adolescence. In: Fomon SJ, Zlotkin S, eds. Nutritional Anemias. New York: Vervey/Raven Press, 1992 p 29-38
    • (1992) Nutritional Anemias , pp. 29-38
    • Dallman, P.R.1
  • 273
    • 0002188256 scopus 로고
    • Iron balance in pregnancy and lactation
    • Fomon SJ, Zlotkin S, eds. New York: Vervey/Raven Press
    • Hallberg L. Iron balance in pregnancy and lactation. In: Fomon SJ, Zlotkin S, eds. Nutritional Anemias. New York: Vervey/Raven Press, 1992 p 13-28
    • (1992) Nutritional Anemias , pp. 13-28
    • Hallberg, L.1
  • 274
    • 0020684273 scopus 로고
    • Iron requirements in normal pregnancy as assessed by serum ferritin, serum transferrin saturation and erythrocyte protoporphyrin determinations
    • Romslo I, Haram K, Sagen N, Augensen K. Iron requirements in normal pregnancy as assessed by serum ferritin, serum transferrin saturation and erythrocyte protoporphyrin determinations. Br J Obstet Gynaecol 1983;90:101-7
    • (1983) Br J Obstet Gynaecol , vol.90 , pp. 101-107
    • Romslo, I.1    Haram, K.2    Sagen, N.3    Augensen, K.4
  • 276
    • 0026512123 scopus 로고
    • Detection of functional iron deficiency during erythropoietin treatment - A new approach
    • Macdougall IC, Cavill I, Hulme B, et al. Detection of functional iron deficiency during erythropoietin treatment - a new approach. Br Med J 1992;304:225-6
    • (1992) Br Med J , vol.304 , pp. 225-226
    • Macdougall, I.C.1    Cavill, I.2    Hulme, B.3
  • 277
    • 0026767089 scopus 로고
    • Anemia of renal failure. Use of erythropoietin
    • Humphries JE. Anemia of renal failure. Use of erythropoietin. Med Clin North Am 1992;76:711-25
    • (1992) Med Clin North Am , vol.76 , pp. 711-725
    • Humphries, J.E.1


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