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Volumn 67, Issue 1, 1997, Pages 1-15

Iron crosses the endosomal membrane by a carrier-mediated process

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM); CARRIER PROTEIN; FERRIC ION; FERROUS ION; INTEGRIN; IRON; IRON BINDING PROTEIN; MOBILFERRIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TRANSFERRIN; TRANSFERRIN RECEPTOR;

EID: 0030728731     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6107(97)00009-6     Document Type: Review
Times cited : (46)

References (107)
  • 1
    • 0029096535 scopus 로고
    • Phorbol esters stimulate non-transferrin iron uptake by K562 cells
    • Akompong, T., Inman, R. S. and Wessling-Resnick, M. (1995) Phorbol esters stimulate non-transferrin iron uptake by K562 cells. J. biol. Chem. 270, 20937-20941.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20937-20941
    • Akompong, T.1    Inman, R.S.2    Wessling-Resnick, M.3
  • 2
    • 0027312095 scopus 로고
    • Glycosyl, phosphatidylinositol membrane anchoring of melanotransferrin (p97): Apical compartmentalization in intestinal epithelial cells
    • Alemany, R., Rosa, V. M., Franci, C., Egea, G., Real, F. X. and Thompson, J. M. (1993) Glycosyl, phosphatidylinositol membrane anchoring of melanotransferrin (p97): apical compartmentalization in intestinal epithelial cells. J. Cell Sci. 104, 1155-1162.
    • (1993) J. Cell Sci. , vol.104 , pp. 1155-1162
    • Alemany, R.1    Rosa, V.M.2    Franci, C.3    Egea, G.4    Real, F.X.5    Thompson, J.M.6
  • 3
    • 0028058038 scopus 로고
    • The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
    • Askwith, C., Eide, D., Ho, A. V., Bernard, P. S., Li, L. L., Davis-Kaplan, S., Sipe, D. M. and Kaplan, J. (1994) The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76, 403-410.
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.1    Eide, D.2    Ho, A.V.3    Bernard, P.S.4    Li, L.L.5    Davis-Kaplan, S.6    Sipe, D.M.7    Kaplan, J.8
  • 6
    • 0025924788 scopus 로고
    • A new role for the transferrin receptor in the release of iron from transferrin
    • Bali, P. K., Zak, O. and Aisen, P. (1991) A new role for the transferrin receptor in the release of iron from transferrin. Biochemistry 30, 324-328.
    • (1991) Biochemistry , vol.30 , pp. 324-328
    • Bali, P.K.1    Zak, O.2    Aisen, P.3
  • 7
    • 0028832455 scopus 로고
    • Evidence for a low Km transporter for non-transferrin-bound iron in isolated rat hepatocytes
    • Barisani, D., Berg, C. L., Wessling-Resnick, M. and Gollan, J. L. (1995) Evidence for a low Km transporter for non-transferrin-bound iron in isolated rat hepatocytes. Am. J. Physiol. 269, G570-G576.
    • (1995) Am. J. Physiol. , vol.269
    • Barisani, D.1    Berg, C.L.2    Wessling-Resnick, M.3    Gollan, J.L.4
  • 8
    • 0022600935 scopus 로고
    • Iron-induced L1210 cell growth: Evidence of a transferrin-independent iron transport
    • Basset, P., Quesneau, Y. and Zwiller, J. (1986) Iron-induced L1210 cell growth: Evidence of a transferrin-independent iron transport. Cancer Res. 46, 1644-1647.
    • (1986) Cancer Res. , vol.46 , pp. 1644-1647
    • Basset, P.1    Quesneau, Y.2    Zwiller, J.3
  • 9
    • 0023188747 scopus 로고
    • Receptor-mediated endocytosis of transferrin and ferritin by guinea-pig reticulocytes. Uptake by a common endocytic pathway
    • Blight, G. D. and Morgan, E. H. (1987) Receptor-mediated endocytosis of transferrin and ferritin by guinea-pig reticulocytes. Uptake by a common endocytic pathway. Eur. J. Cell Biol. 43, 260-265.
    • (1987) Eur. J. Cell Biol. , vol.43 , pp. 260-265
    • Blight, G.D.1    Morgan, E.H.2
  • 10
    • 0028834446 scopus 로고
    • Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II)
    • Breuer, W., Epsztejn, S. and Cabantchik, Z. I. (1995) Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II). J. biol. Chem. 270, 24209-24215.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24209-24215
    • Breuer, W.1    Epsztejn, S.2    Cabantchik, Z.I.3
  • 11
    • 0022345593 scopus 로고
    • Efficient cleanse of non-transferrin-bound iron by rat liver
    • Brissot, P., Wright, T. L., Ma, W. L. and Weisiger, R. A. (1985) Efficient cleanse of non-transferrin-bound iron by rat liver. J. clin. Invest. 76, 1463-1470.
    • (1985) J. Clin. Invest. , vol.76 , pp. 1463-1470
    • Brissot, P.1    Wright, T.L.2    Ma, W.L.3    Weisiger, R.A.4
  • 12
    • 0020029134 scopus 로고
    • Human melanoma-associated antigen p97 is structurally and functionally related to transferrin
    • Brown, J. P., Hewick, R. M., Hellstrom, I., Hellstrom, K. E., Doolittle, R. F. and Dreyer, W. J. (1982) Human melanoma-associated antigen p97 is structurally and functionally related to transferrin. Nature 296, 171-173.
    • (1982) Nature , vol.296 , pp. 171-173
    • Brown, J.P.1    Hewick, R.M.2    Hellstrom, I.3    Hellstrom, K.E.4    Doolittle, R.F.5    Dreyer, W.J.6
  • 13
    • 0026770143 scopus 로고
    • Transferrin-receptor-independent but iron-dependent proliferation of variant Chinese hamster ovary cells
    • Chan, R. Y. Y., Ponka, P. and Schulman, H. M. (1992) Transferrin-receptor-independent but iron-dependent proliferation of variant Chinese hamster ovary cells. Exp. cell. Res. 202, 326-336.
    • (1992) Exp. Cell. Res. , vol.202 , pp. 326-336
    • Chan, R.Y.Y.1    Ponka, P.2    Schulman, H.M.3
  • 14
    • 0023611360 scopus 로고
    • Rabbit reticulocyte coated vesicles carrying the transferrin-transferrin receptor complex: I. Purification and partial characterization
    • Choe, H. R., Moseley, S. T., Glass, J. and Nunez, M. T. (1987) Rabbit reticulocyte coated vesicles carrying the transferrin-transferrin receptor complex: I. Purification and partial characterization. Blood 70, 1035-1039.
    • (1987) Blood , vol.70 , pp. 1035-1039
    • Choe, H.R.1    Moseley, S.T.2    Glass, J.3    Nunez, M.T.4
  • 15
    • 0025228853 scopus 로고
    • A newly identified iron binding protein in duodenal mucosa of rats, purification and characterization of mobilferrin
    • Conrad, M. E., Umbreit, J. N., Moore, E. G., Peterson, R. D. A. and Jones, M. B. (1990) A newly identified iron binding protein in duodenal mucosa of rats, purification and characterization of mobilferrin. J. biol. Chem. 265, 5273-5279.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5273-5279
    • Conrad, M.E.1    Umbreit, J.N.2    Moore, E.G.3    Peterson, R.D.A.4    Jones, M.B.5
  • 16
    • 0026098238 scopus 로고
    • A role of mucin in the absorption of inorganic iron and other metal cations
    • Conrad, M. E., Umbreit, J. N. and Moore, E. G. (1991) A role of mucin in the absorption of inorganic iron and other metal cations. Gastroenterology 100, 129-136.
    • (1991) Gastroenterology , vol.100 , pp. 129-136
    • Conrad, M.E.1    Umbreit, J.N.2    Moore, E.G.3
  • 17
    • 0026586391 scopus 로고
    • Newly identified iron binding protein in human duodenal mucosa
    • Conrad, M. E., Umbreit, J. N., Moore, E. G. and Rodning, C. R. (1992) Newly identified iron binding protein in human duodenal mucosa. Blood 79, 244-247.
    • (1992) Blood , vol.79 , pp. 244-247
    • Conrad, M.E.1    Umbreit, J.N.2    Moore, E.G.3    Rodning, C.R.4
  • 19
    • 0027396615 scopus 로고
    • A concise review: Iron absorption - The mucin-mobilferrin-integrin pathways. A competitive pathway for metal absorption
    • Conrad, M. E. and Umbreit, J. N. (1993) A concise review: Iron absorption - the mucin-mobilferrin-integrin pathways. A competitive pathway for metal absorption. Am. J. Hematol. 42, 67-73.
    • (1993) Am. J. Hematol. , vol.42 , pp. 67-73
    • Conrad, M.E.1    Umbreit, J.N.2
  • 20
    • 0027496419 scopus 로고
    • Regulation of iron transport: Proteins involved in duodenal mucosal uptake and transport
    • Conrad, M. E., Umbreit, J. N. and Moore, E. G. (1993a) Regulation of iron transport: Proteins involved in duodenal mucosal uptake and transport. J. Am. Coll. Nutr. 12, 720-728.
    • (1993) J. Am. Coll. Nutr. , vol.12 , pp. 720-728
    • Conrad, M.E.1    Umbreit, J.N.2    Moore, E.G.3
  • 21
    • 0027181554 scopus 로고
    • Rat duodenal iron-binding protein mobilferrin is a homologue of calreticulin
    • Conrad, M. E., Umbreit, J. N. and Moore, E. G. (1993b) Rat duodenal iron-binding protein mobilferrin is a homologue of calreticulin. Gastroenterology 104, 1700-1704.
    • (1993) Gastroenterology , vol.104 , pp. 1700-1704
    • Conrad, M.E.1    Umbreit, J.N.2    Moore, E.G.3
  • 25
    • 0026506018 scopus 로고
    • Ferric reductase of Saccharomyces cerevisiae: Molecular characterization, role in iron uptake, and transcriptional control by iron
    • Dancis, A., Roman, D. G., Anderson, G. J., Hinnebusch, A. G. and Klausner, R. D. (1992) Ferric reductase of Saccharomyces cerevisiae: Molecular characterization, role in iron uptake, and transcriptional control by iron. Proc. natn. Acad. Sci. U.S.A. 89, 3869-3871.
    • (1992) Proc. Natn. Acad. Sci. U.S.A. , vol.89 , pp. 3869-3871
    • Dancis, A.1    Roman, D.G.2    Anderson, G.J.3    Hinnebusch, A.G.4    Klausner, R.D.5
  • 26
    • 0021056428 scopus 로고
    • Identification and molecular cloning of human Blym transforming gene activities in Burkitts's lymphomas
    • Diamond, A., Cooper, G. M., Ritz, J. and Lane, M. A. (1983) Identification and molecular cloning of human Blym transforming gene activities in Burkitts's lymphomas. Nature 305, 112-115.
    • (1983) Nature , vol.305 , pp. 112-115
    • Diamond, A.1    Cooper, G.M.2    Ritz, J.3    Lane, M.A.4
  • 27
    • 0343208990 scopus 로고
    • Cell surface antigens of human melanoma: Definition of six antigenic systems with monoclonal antibodies
    • Dippold, W. G., Lloyd, K. O., Li, T. C., Ikeda, H., Oettgen, H. F. and Old, L. J. (1980) Cell surface antigens of human melanoma: Definition of six antigenic systems with monoclonal antibodies. Proc. natn. Acad. Sci. U.S.A. 77, 6114-6118.
    • (1980) Proc. Natn. Acad. Sci. U.S.A. , vol.77 , pp. 6114-6118
    • Dippold, W.G.1    Lloyd, K.O.2    Li, T.C.3    Ikeda, H.4    Oettgen, H.F.5    Old, L.J.6
  • 28
    • 0023938640 scopus 로고
    • Carrier mediated iron transport through erythroid cell membrane
    • Egyed, A. (1988) Carrier mediated iron transport through erythroid cell membrane. Br. J. Haematol. 68, 483-486.
    • (1988) Br. J. Haematol. , vol.68 , pp. 483-486
    • Egyed, A.1
  • 29
    • 0025872370 scopus 로고
    • 2+ transport through the erythroid cell membrane
    • 2+ transport through the erythroid cell membrane. Biochem. J. 275, 635-638.
    • (1991) Biochem. J. , vol.275 , pp. 635-638
    • Egyed, A.1
  • 30
    • 0026758238 scopus 로고
    • Regulation of iron uptake in Saccharomyces cerevisiae. The ferrireductase and Fe(II) transporter are regulated independently
    • Eide, D., Davis-Kaplan, S., Jordan, I., Sipe, D. and Kaplan, J. (1992) Regulation of iron uptake in Saccharomyces cerevisiae. The ferrireductase and Fe(II) transporter are regulated independently. J. biol. Chem. 267, 20774-20781.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20774-20781
    • Eide, D.1    Davis-Kaplan, S.2    Jordan, I.3    Sipe, D.4    Kaplan, J.5
  • 31
    • 0026623265 scopus 로고
    • Effect of ascorbate in the reduction of transferrin-associated iron in endocytic vesicles
    • Escobar, A., Gaete, V. and Nunez, M. T. (1992) Effect of ascorbate in the reduction of transferrin-associated iron in endocytic vesicles. J. Bioenerg. Biomembr. 24, 227-233.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 227-233
    • Escobar, A.1    Gaete, V.2    Nunez, M.T.3
  • 32
    • 0028111120 scopus 로고
    • Transport and expression in human melanomas of a transferrin-like glycosylphosphatidylinositol-anchored protein
    • Food, M. R., Rothenberger, S., Gabathuler, R., Haidl, I. D., Reid, G. and Jefferies, W. A. (1994) Transport and expression in human melanomas of a transferrin-like glycosylphosphatidylinositol-anchored protein. J. biol. Chem. 269, 3034-3040.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3034-3040
    • Food, M.R.1    Rothenberger, S.2    Gabathuler, R.3    Haidl, I.D.4    Reid, G.5    Jefferies, W.A.6
  • 34
    • 0016342687 scopus 로고
    • Endocytosis and exocytosis in membrane remodelling during reticulocyte maturation
    • Gasko, O. and Danon, D. (1974) Endocytosis and exocytosis in membrane remodelling during reticulocyte maturation. Br. J. Haematol. 28, 463-470.
    • (1974) Br. J. Haematol. , vol.28 , pp. 463-470
    • Gasko, O.1    Danon, D.2
  • 35
    • 0025766932 scopus 로고
    • Uptake and endocytic pathway of transferrin and iron in perfused rat liver
    • Goldenberg, H., Seelos, C., Chatwani, S., Chegini, S. and Pumm, R. (1991) Uptake and endocytic pathway of transferrin and iron in perfused rat liver. Biochim. biophys. Acta 1067, 145-152.
    • (1991) Biochim. Biophys. Acta , vol.1067 , pp. 145-152
    • Goldenberg, H.1    Seelos, C.2    Chatwani, S.3    Chegini, S.4    Pumm, R.5
  • 36
    • 0028789141 scopus 로고
    • Biochemical aspects of iron metabolism, transport and regulation
    • Goldenberg, H. and Scheiber, B (1995) Biochemical aspects of iron metabolism, transport and regulation. Wien. Klin. Wochenschr. 107, 669-676.
    • (1995) Wien. Klin. Wochenschr. , vol.107 , pp. 669-676
    • Goldenberg, H.1    Scheiber, B.2
  • 37
    • 0020693711 scopus 로고
    • Molecular cloning and nucleotide sequence of a transforming gene detected by transfection of a chicken B-cell lymphoma DNA
    • Goubin, G., Goldman, D. S., Luce, J., Neiman, P. E. and Cooper, G. M. (1983) Molecular cloning and nucleotide sequence of a transforming gene detected by transfection of a chicken B-cell lymphoma DNA. Nature 302, 114-119.
    • (1983) Nature , vol.302 , pp. 114-119
    • Goubin, G.1    Goldman, D.S.2    Luce, J.3    Neiman, P.E.4    Cooper, G.M.5
  • 38
    • 0024564712 scopus 로고
    • Non-transferrin bound iron in plasma or serum from patients with idiopathic hemochromatosis
    • Grootveld, M., Bell, J. D., Halliwell, B., Arvoma, O. I., Bomford, A. and Sadler, P. J. (1989) Non-transferrin bound iron in plasma or serum from patients with idiopathic hemochromatosis. J. biol. Chem. 264, 4417-4422.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4417-4422
    • Grootveld, M.1    Bell, J.D.2    Halliwell, B.3    Arvoma, O.I.4    Bomford, A.5    Sadler, P.J.6
  • 39
    • 0021719707 scopus 로고
    • Endocytosis and intracellular processing of transferrin and colloidal gold-transferrin in rat reticulocytes: Demonstration of a pathway for receptor shedding
    • Harding, C., Heuser, J. and Stahl, P. (1984) Endocytosis and intracellular processing of transferrin and colloidal gold-transferrin in rat reticulocytes: Demonstration of a pathway for receptor shedding. Eur. J. Cell Biol. 35, 256-263.
    • (1984) Eur. J. Cell Biol. , vol.35 , pp. 256-263
    • Harding, C.1    Heuser, J.2    Stahl, P.3
  • 40
    • 0028337112 scopus 로고
    • Receptor-independent uptake of transferrin-bound iron by reticulocytes
    • Hodgson, L. L., Quail, E. A. and Morgan, E. H. (1994) Receptor-independent uptake of transferrin-bound iron by reticulocytes. Arch. Biochem. Biophys. 308, 318-326.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 318-326
    • Hodgson, L.L.1    Quail, E.A.2    Morgan, E.H.3
  • 41
    • 0028966457 scopus 로고
    • Iron transport mechanisms in reticulocytes and mature erythrocytes
    • Hodgson, L. L., Quail, E. A. and Morgan, E. H. (1995) Iron transport mechanisms in reticulocytes and mature erythrocytes. J. cell. Physiol. 162, 181-190.
    • (1995) J. Cell. Physiol. , vol.162 , pp. 181-190
    • Hodgson, L.L.1    Quail, E.A.2    Morgan, E.H.3
  • 42
    • 0023666065 scopus 로고
    • Integrin: A family of cell surface receptors
    • Hynes, R. O. (1987) Integrin: A family of cell surface receptors. Cell 48, 549-554.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 43
    • 0027512915 scopus 로고
    • Characterization of transferrin-independent iron transport in K562 cells
    • Inman, R. S. and Wessling-Resnick, M. (1993) Characterization of transferrin-independent iron transport in K562 cells. J. biol. Chem. 268, 8521-8528.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8521-8528
    • Inman, R.S.1    Wessling-Resnick, M.2
  • 44
    • 0028109907 scopus 로고
    • Extracellular ferrireductase activity of K562 cells is coupled to transferrin-independent iron uptake
    • Inman, R. S., Coughlan, M. M. and Wessling-Resnick, M. (1994) Extracellular ferrireductase activity of K562 cells is coupled to transferrin-independent iron uptake. Biochemistry 33, 11850-11857.
    • (1994) Biochemistry , vol.33 , pp. 11850-11857
    • Inman, R.S.1    Coughlan, M.M.2    Wessling-Resnick, M.3
  • 45
    • 73649205621 scopus 로고
    • The plasma-to-cell cycle of transferrin
    • Jandl, J. and Katz, J. (1963) The plasma-to-cell cycle of transferrin. J. clin. Invest. 42, 314-326.
    • (1963) J. Clin. Invest. , vol.42 , pp. 314-326
    • Jandl, J.1    Katz, J.2
  • 46
    • 0023645106 scopus 로고
    • Vesicle formation during reticulocyte maturation. Association of plasma membrane activities with released vesicles (exosomes)
    • Johnstone, R. M., Adam, M., Hammond, J. R., Orr, L. and Turbide, C. (1987) Vesicle formation during reticulocyte maturation. Association of plasma membrane activities with released vesicles (exosomes). J. biol. Chem. 262, 9412-9420.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9412-9420
    • Johnstone, R.M.1    Adam, M.2    Hammond, J.R.3    Orr, L.4    Turbide, C.5
  • 47
    • 0028170059 scopus 로고
    • The mammalian transferrin-independent iron transport system may involve surface ferrireductase activity
    • Jordan, I. and Kaplan, J. (1994) The mammalian transferrin-independent iron transport system may involve surface ferrireductase activity. Biochem. J. 302, 875-879.
    • (1994) Biochem. J. , vol.302 , pp. 875-879
    • Jordan, I.1    Kaplan, J.2
  • 48
    • 0025774978 scopus 로고
    • Regulation of the transferrin-independent iron transport system in cultured cells
    • Kaplan, J., Jordan, I. and Sturrock, A. (1991) Regulation of the transferrin-independent iron transport system in cultured cells. J. biol. Chem. 266, 2997-3004.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2997-3004
    • Kaplan, J.1    Jordan, I.2    Sturrock, A.3
  • 49
    • 0026587547 scopus 로고
    • Endocytosis of glycophospholipid-anchored and transmembrane forms of CD4 by different endocytic pathways
    • Keller, G. A., Siegel, M. W. and Caras, I. W. (1992) Endocytosis of glycophospholipid-anchored and transmembrane forms of CD4 by different endocytic pathways. Eur. molec. Biol. Org. J. 11, 863-874.
    • (1992) Eur. Molec. Biol. Org. J. , vol.11 , pp. 863-874
    • Keller, G.A.1    Siegel, M.W.2    Caras, I.W.3
  • 51
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klausner, R. D., Rouault, T. A. and Harford, J. B. (1993) Regulating the fate of mRNA: The control of cellular iron metabolism. Cell 72, 19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 53
    • 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. 269, 10242-10246.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10242-10246
    • Li, C.Y.1    Watkins, J.A.2    Glass, J.3
  • 55
    • 0021710575 scopus 로고
    • A mono-sited transferrin from a representative deuterostome: The ascidian Pyura stolonifera (subphylum urochordata)
    • Martin, A. W., Huebers, E., Huebers, H., Webb, J. and Finch, C. A. (1984) A mono-sited transferrin from a representative deuterostome: The ascidian Pyura stolonifera (subphylum urochordata). Blood 64, 1047-1052.
    • (1984) Blood , vol.64 , pp. 1047-1052
    • Martin, A.W.1    Huebers, E.2    Huebers, H.3    Webb, J.4    Finch, C.A.5
  • 56
    • 0002668643 scopus 로고
    • Biological significance of low molecular weight iron (III) complexes
    • (ed. H Sigel). Marcel Dekker Inc., NY
    • May, P. M., Williams, D. R. and Linder, P. W. (1980) Biological significance of low molecular weight iron (III) complexes. In Metal Ions in Biological Systems, pp. 29-76 (ed. H Sigel). Marcel Dekker Inc., NY.
    • (1980) Metal Ions in Biological Systems , pp. 29-76
    • May, P.M.1    Williams, D.R.2    Linder, P.W.3
  • 57
    • 0015233788 scopus 로고
    • A study of iron transfer from rabbit transferrin to reticulocytes using synthetic chelating agents
    • Morgan, E. H. (1971) A study of iron transfer from rabbit transferrin to reticulocytes using synthetic chelating agents. Biochim. biophys. Acta 244, 103-116.
    • (1971) Biochim. Biophys. Acta , vol.244 , pp. 103-116
    • Morgan, E.H.1
  • 58
    • 0019860059 scopus 로고
    • Transferrin, biochemistry, physiology and clinical significance
    • Morgan, E. H. (1981) Transferrin, biochemistry, physiology and clinical significance. Molec. Aspects Med. 4, 1-123.
    • (1981) Molec. Aspects Med. , vol.4 , pp. 1-123
    • Morgan, E.H.1
  • 59
    • 0023694365 scopus 로고
    • Membrane transport of non-transferrin iron by reticulocytes
    • Morgan, E. H. (1988) Membrane transport of non-transferrin iron by reticulocytes. Biochim. biophys. Acta 943, 428-439.
    • (1988) Biochim. Biophys. Acta , vol.943 , pp. 428-439
    • Morgan, E.H.1
  • 60
    • 0023714954 scopus 로고
    • Role of transferrin receptors and endocytosis in iron uptake by hepatic and erythroid cells
    • Morgan, E. H. and Baker, E. (1988) Role of transferrin receptors and endocytosis in iron uptake by hepatic and erythroid cells. Ann. N. Y. Acad. Sci. 256, 65-82.
    • (1988) Ann. N. Y. Acad. Sci. , vol.256 , pp. 65-82
    • Morgan, E.H.1    Baker, E.2
  • 62
    • 0020691273 scopus 로고
    • The reticulocyte plasma membrane pathway of iron uptake as determined by the addition of a-a′ dipyridyl inhibition
    • Nunez, M. T., Cole, E. S. and Glass, J. (1983) The reticulocyte plasma membrane pathway of iron uptake as determined by the addition of a-a′ dipyridyl inhibition. J. biol. Chem. 258, 1146-1151.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1146-1151
    • Nunez, M.T.1    Cole, E.S.2    Glass, J.3
  • 63
    • 0024549396 scopus 로고
    • Assay and characteristics of the iron binding moiety of reticulocyte endocytic vesicles
    • Nunez, M. T., Pinto, I. and Glass, J. (1989) Assay and characteristics of the iron binding moiety of reticulocyte endocytic vesicles. J. Membr. Biol. 107, 129-135.
    • (1989) J. Membr. Biol. , vol.107 , pp. 129-135
    • Nunez, M.T.1    Pinto, I.2    Glass, J.3
  • 64
    • 0025211404 scopus 로고
    • Mobilization of iron from endocytic vesicles. The effects of acidification and reduction
    • Nunez, M. T., Gaete, V., Watkins, J. A. and Glass, J. (1990) Mobilization of iron from endocytic vesicles. The effects of acidification and reduction. J. biol. Chem. 265, 6688-6692.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6688-6692
    • Nunez, M.T.1    Gaete, V.2    Watkins, J.A.3    Glass, J.4
  • 66
    • 0028191543 scopus 로고
    • The role of membrane-associated iron-binding complex in intestinal absorption in the rat
    • Orimo, H., Hisayasu, S., Hirai, Y. and Yoshino, Y. (1994) The role of membrane-associated iron-binding complex in intestinal absorption in the rat. J. Nutr. Sci. Vitaminol. 40, 511-522.
    • (1994) J. Nutr. Sci. Vitaminol. , vol.40 , pp. 511-522
    • Orimo, H.1    Hisayasu, S.2    Hirai, Y.3    Yoshino, Y.4
  • 67
    • 0023495548 scopus 로고
    • Externalization of membrane-bound activities during sheep reticulocyte maturation is temperature and ATP dependent
    • Orr, L., Adam, M. and Johnstone, R. M. (1987) Externalization of membrane-bound activities during sheep reticulocyte maturation is temperature and ATP dependent. Biochem. Cell Biol. 65, 1080-1090.
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 1080-1090
    • Orr, L.1    Adam, M.2    Johnstone, R.M.3
  • 68
    • 0027378891 scopus 로고
    • Redox, transferrin-independent, and receptor-mediated endocytosis iron uptake system in cultured human fibroblasts
    • Oshiro, S., Nakajima, H., Markello, T., Krasnewich, D., Bernardini, I. and Gahl, W. A. (1993) Redox, transferrin-independent, and receptor-mediated endocytosis iron uptake system in cultured human fibroblasts. J. biol. Chem. 268, 21586-26591.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21586-26591
    • Oshiro, S.1    Nakajima, H.2    Markello, T.3    Krasnewich, D.4    Bernardini, I.5    Gahl, W.A.6
  • 69
    • 0022201056 scopus 로고
    • Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes
    • Pan, B. T., Teng, K., Wu, C., Adam, M. and Johnstone, R. M. (1985) Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes. J. cell. Biol. 101, 942-948.
    • (1985) J. Cell. Biol. , vol.101 , pp. 942-948
    • Pan, B.T.1    Teng, K.2    Wu, C.3    Adam, M.4    Johnstone, R.M.5
  • 70
    • 0021993655 scopus 로고
    • Regulation of heme synthesis in erythroid cells: Hemin inhibits transferrin iron utilization but not protoporphyrin synthesis
    • Ponka, P. and Schulman, M. (1985) Regulation of heme synthesis in erythroid cells: Hemin inhibits transferrin iron utilization but not protoporphyrin synthesis. Blood 65, 850-857.
    • (1985) Blood , vol.65 , pp. 850-857
    • Ponka, P.1    Schulman, M.2
  • 71
    • 0025004447 scopus 로고
    • Effect of lead on the transport of transferrin-free and transferrin-bound iron into rabbit reticulocytes
    • Qian, Z. M. and Morgan, E. H. (1990) Effect of lead on the transport of transferrin-free and transferrin-bound iron into rabbit reticulocytes. Biochem. Pharmacol. 40, 1049-1054.
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 1049-1054
    • Qian, Z.M.1    Morgan, E.H.2
  • 72
    • 0025863099 scopus 로고
    • Effect of metabolic inhibitors on uptake of non-transferrin-bound iron by reticulocytes
    • Qian, Z. M. and Morgan, E. H. (1991) Effect of metabolic inhibitors on uptake of non-transferrin-bound iron by reticulocytes. Biochim. biophys. Acta 1073, 456-462.
    • (1991) Biochim. Biophys. Acta , vol.1073 , pp. 456-462
    • Qian, Z.M.1    Morgan, E.H.2
  • 73
    • 0026516293 scopus 로고
    • Changes in the uptake of transferrin-free and transferrin-bound iron during reticulocyte maturation in vivo and in vitro
    • Qian, Z. M. and Morgan, E. H. (1992) Changes in the uptake of transferrin-free and transferrin-bound iron during reticulocyte maturation in vivo and in vitro. Biochim. biophys. Acta 1135, 35-43.
    • (1992) Biochim. Biophys. Acta , vol.1135 , pp. 35-43
    • Qian, Z.M.1    Morgan, E.H.2
  • 74
    • 0028832288 scopus 로고
    • Mechanisms of iron uptake by mammalian cells
    • Qian, Z. M. and Tang, P. L. (1995) Mechanisms of iron uptake by mammalian cells. Biochim. biophys. Acta 1269, 205-214.
    • (1995) Biochim. Biophys. Acta , vol.1269 , pp. 205-214
    • Qian, Z.M.1    Tang, P.L.2
  • 75
    • 0029875023 scopus 로고    scopus 로고
    • Effect of lipid peroxidation on transferrin-free iron uptake by rabbit reticulocytes
    • Qian, Z. M., Tang, P. L. and Morgan, E. H. (1996) Effect of lipid peroxidation on transferrin-free iron uptake by rabbit reticulocytes. Biochim. biophys. Acta 1310, 293-302.
    • (1996) Biochim. Biophys. Acta , vol.1310 , pp. 293-302
    • Qian, Z.M.1    Tang, P.L.2    Morgan, E.H.3
  • 76
    • 0028209786 scopus 로고
    • Role of membrane surface potential and other factors in the uptake of non-transferrin-bound iron by reticulocytes
    • Quail, E. A. and Morgan, E. H. (1994) Role of membrane surface potential and other factors in the uptake of non-transferrin-bound iron by reticulocytes. J. cell. Physiol. 159, 238-244.
    • (1994) J. Cell. Physiol. , vol.159 , pp. 238-244
    • Quail, E.A.1    Morgan, E.H.2
  • 77
    • 0026630201 scopus 로고
    • Transferrin uptake by bone marrow macrophages is independent of the degree of iron saturation
    • Rama, R. and Sanchez, J. (1992) Transferrin uptake by bone marrow macrophages is independent of the degree of iron saturation. Br. J. Haematol. 82, 455-459.
    • (1992) Br. J. Haematol. , vol.82 , pp. 455-459
    • Rama, R.1    Sanchez, J.2
  • 79
    • 0026690909 scopus 로고
    • Two mechanisms of iron uptake from transferrin by melanoma cells. The effect of desferrioxamine and ferric ammonium citrate
    • Richardson, D. and Baker, E. (1992) Two mechanisms of iron uptake from transferrin by melanoma cells. The effect of desferrioxamine and ferric ammonium citrate. J. biol. Chem. 267, 13972-13979.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13972-13979
    • Richardson, D.1    Baker, E.2
  • 80
    • 0008144817 scopus 로고
    • Primary structure of human melanoma-associated antigen p97 (melanotransferrin) deduced from the mRNA sequence
    • Rose, I. M., Plowman, G. D., Teplow, D. B., Dreyer, W. J., Hellstrom, K. E. and Brown, J. P. (1986) Primary structure of human melanoma-associated antigen p97 (melanotransferrin) deduced from the mRNA sequence. Proc. natn. Acad. Sci. U.S.A. 83, 1261-1265.
    • (1986) Proc. Natn. Acad. Sci. U.S.A. , vol.83 , pp. 1261-1265
    • Rose, I.M.1    Plowman, G.D.2    Teplow, D.B.3    Dreyer, W.J.4    Hellstrom, K.E.5    Brown, J.P.6
  • 82
    • 0027222141 scopus 로고
    • NAD(P)H: Ferric iron reductase in endosomal membranes from rat liver
    • Scheiber, B. and Goldenberg, H. (1993) NAD(P)H: Ferric iron reductase in endosomal membranes from rat liver. Arch. Biochem. Biophys. 305, 225-230.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 225-230
    • Scheiber, B.1    Goldenberg, H.2
  • 83
    • 0024539607 scopus 로고
    • In situ localization of melanotransferrin (melanoma-associated antigen p97) in human liver. A light- and electronmicroscopic immunohistochemical study
    • Sciot, R., De Vos, R., van Eyken, P., van der Steen, K., Moermen, P. and Desmet, V. J. (1989) In situ localization of melanotransferrin (melanoma-associated antigen p97) in human liver. A light- and electronmicroscopic immunohistochemical study. Liver 9, 110-119.
    • (1989) Liver , vol.9 , pp. 110-119
    • Sciot, R.1    De Vos, R.2    Van Eyken, P.3    Van Der Steen, K.4    Moermen, P.5    Desmet, V.J.6
  • 84
    • 0023912979 scopus 로고
    • Interactions between isolated hepatocytes and Kupfer cells in iron metabolism: A possible role for ferritin as an iron carrier protein
    • Sibille, J. C., Kondo, H. and Aisen, P. (1988) Interactions between isolated hepatocytes and Kupfer cells in iron metabolism: A possible role for ferritin as an iron carrier protein. Hepatology 8, 296-301.
    • (1988) Hepatology , vol.8 , pp. 296-301
    • Sibille, J.C.1    Kondo, H.2    Aisen, P.3
  • 85
    • 0030058299 scopus 로고    scopus 로고
    • Molecular mechanisms of iron uptake in eukaryotes
    • Silva, D. M. D., Askwith, C. and Kaplan, J. (1996) Molecular mechanisms of iron uptake in eukaryotes. Physiol. Rev. 76, 31-47.
    • (1996) Physiol. Rev. , vol.76 , pp. 31-47
    • Silva, D.M.D.1    Askwith, C.2    Kaplan, J.3
  • 86
    • 0022423308 scopus 로고
    • 2+ uptake by intestinal brush-border membrane vesicles from normal and hypoxic mice
    • 2+ uptake by intestinal brush-border membrane vesicles from normal and hypoxic mice. Biochim. biophys. Acta 814, 381-388.
    • (1985) Biochim. Biophys. Acta , vol.814 , pp. 381-388
    • Simpson, R.J.1    Peters, T.J.2
  • 88
    • 0024516905 scopus 로고
    • On the structure and function of endocytic transport systems
    • Singer, S. J. (1989) On the structure and function of endocytic transport systems. Biol. Cell 65, 1-5.
    • (1989) Biol. Cell , vol.65 , pp. 1-5
    • Singer, S.J.1
  • 89
    • 0025727891 scopus 로고
    • +-ATPase regulation of endosomal acidification in K562 erythroleukemia cells. Analysis via inhibition of transferrin recycling by low temperature
    • +-ATPase regulation of endosomal acidification in K562 erythroleukemia cells. Analysis via inhibition of transferrin recycling by low temperature. J. biol. Chem. 266, 3469-3474.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3469-3474
    • Sipe, D.M.1    Jesurum, A.2    Murphy, R.F.3
  • 90
    • 0025744263 scopus 로고
    • Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH
    • Sipe, D. M. and Murphy, R. F. (1991) Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH. J. biol. Chem. 266, 8002-8007.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8002-8007
    • Sipe, D.M.1    Murphy, R.F.2
  • 91
    • 0025188620 scopus 로고
    • Overview of hemochromatosis
    • Smith, L. (1990) Overview of hemochromatosis. West. J. Med. 153, 296-308.
    • (1990) West. J. Med. , vol.153 , pp. 296-308
    • Smith, L.1
  • 92
    • 0023265485 scopus 로고
    • Iron uptake by rat duodenal microvillus membrane vesicles: Evidence for a carrier transport system
    • Stremmel, W., Lotz, G., Niederau, C., Teschke, R. and Strohmeyer, G. (1987) Iron uptake by rat duodenal microvillus membrane vesicles: Evidence for a carrier transport system. Eur. J. clin. Invest. 17, 136-145.
    • (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
  • 93
    • 0025231790 scopus 로고
    • Characterization of a transferrin-independent uptake system for iron in HeLa cells
    • Sturrock, A., Alexander, J., Lamb, J., Craven, C. M. and Kaplan, J. (1990) Characterization of a transferrin-independent uptake system for iron in HeLa cells. J. biol. Chem. 265, 3139-3145.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3139-3145
    • Sturrock, A.1    Alexander, J.2    Lamb, J.3    Craven, C.M.4    Kaplan, J.5
  • 94
    • 0023665279 scopus 로고
    • NADH diferric transferrin reductase in liver plasma membrane
    • Sun, I. L., Navas, P., Crane, F. L., Morre, D. J. and Low, H. (1987) NADH diferric transferrin reductase in liver plasma membrane. J. biol. Chem. 262, 15915-15921.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15915-15921
    • Sun, I.L.1    Navas, P.2    Crane, F.L.3    Morre, D.J.4    Low, H.5
  • 95
    • 0025688902 scopus 로고
    • Iron uptake by human upper small intestine microvillus membrane vesicles
    • Teichmann, R. and Stremmel, W. (1990) Iron uptake by human upper small intestine microvillus membrane vesicles. J. clin. Invest. 86, 2145-2153.
    • (1990) J. Clin. Invest. , vol.86 , pp. 2145-2153
    • Teichmann, R.1    Stremmel, W.2
  • 96
    • 0023796128 scopus 로고
    • Hepatocytes and reticulocytes have different mechanisms for uptake of iron from transferrin
    • Thorstensen, K. (1988) Hepatocytes and reticulocytes have different mechanisms for uptake of iron from transferrin. J. biol. Chem. 263, 16837-16841.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16837-16841
    • Thorstensen, K.1
  • 97
    • 0023949731 scopus 로고
    • Uptake of iron from transferrin by isolated rat hepatocytes: A redox-mediated plasma membrane process
    • Thorstensen, K. and Romslo, I. (1988) Uptake of iron from transferrin by isolated rat hepatocytes: A redox-mediated plasma membrane process. J. biol. Chem. 263, 8844-8850.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8844-8850
    • Thorstensen, K.1    Romslo, I.2
  • 98
    • 0025306383 scopus 로고
    • Release of iron from diferric transferrin in the presence of rat liver plasma membranes: No evidence of a plasma membrane diferric transferrin reductase
    • Thorstensen, K. and Aisen, P. (1990) Release of iron from diferric transferrin in the presence of rat liver plasma membranes: No evidence of a plasma membrane diferric transferrin reductase. Biochim. biophys. Acta 1052, 29-35.
    • (1990) Biochim. Biophys. Acta , vol.1052 , pp. 29-35
    • Thorstensen, K.1    Aisen, P.2
  • 99
    • 0029152149 scopus 로고
    • Uptake of iron from N-terminal half-transferrin by isolated rat hepatocytes. Evidence of transferrin-receptor-independent iron uptake
    • Thorstensen, K., Trinder, D., Zak, O. and Aisen, P. (1995) Uptake of iron from N-terminal half-transferrin by isolated rat hepatocytes. Evidence of transferrin-receptor-independent iron uptake. Eur. J. Biochem. 232, 129-133.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 129-133
    • Thorstensen, K.1    Trinder, D.2    Zak, O.3    Aisen, P.4
  • 100
    • 0028798960 scopus 로고
    • + exchange modulates acidification of early rat endocytic vesicles
    • + exchange modulates acidification of early rat endocytic vesicles. Cell Physiol. 269, C943-C954.
    • (1995) Cell Physiol. , vol.269
    • Van Dake, R.W.1
  • 101
    • 0025959172 scopus 로고
    • Kinetics of iron passage through subcellular compartments of rabbit reticulocytes
    • Watkins, J. A., Nunez, M. T., Gaete, V., Alvarez, O. and Glass, J. (1991) Kinetics of iron passage through subcellular compartments of rabbit reticulocytes. J. Membr. Biol. 119, 141-149.
    • (1991) J. Membr. Biol. , vol.119 , pp. 141-149
    • Watkins, J.A.1    Nunez, M.T.2    Gaete, V.3    Alvarez, O.4    Glass, J.5
  • 102
    • 0026773665 scopus 로고
    • Kinetic characterization of reluctant dependent process of iron mobilization from endocytic vesicles
    • Watkins, J. A., Altazan, J. D., Elder, P., Li, C. Y., Nunez, M. T., Cui, X. X. and Glass, J. (1992) Kinetic characterization of reluctant dependent process of iron mobilization from endocytic vesicles. Biochemistry 31, 5820-5830.
    • (1992) Biochemistry , vol.31 , pp. 5820-5830
    • Watkins, J.A.1    Altazan, J.D.2    Elder, P.3    Li, C.Y.4    Nunez, M.T.5    Cui, X.X.6    Glass, J.7
  • 103
    • 0000398767 scopus 로고
    • The gastrointestinal tract and iron absorption
    • Wheby, M. S. and Crosby, W. H. (1963) The gastrointestinal tract and iron absorption. Blood 22, 416-428.
    • (1963) Blood , vol.22 , pp. 416-428
    • Wheby, M.S.1    Crosby, W.H.2
  • 104
    • 0001189076 scopus 로고
    • Effect of transferrin saturation on iron absorption in man
    • Wheby, M. S. and Umpierre, G. (1964) Effect of transferrin saturation on iron absorption in man. N. Engl. J. Med. 271, 1391-1395.
    • (1964) N. Engl. J. Med. , vol.271 , pp. 1391-1395
    • Wheby, M.S.1    Umpierre, G.2
  • 105
    • 0028587794 scopus 로고
    • An integrin-mobilferrin iron transport pathway in intestine and hematopoietic cell
    • Wolf, G. and Wessling-Resnick, M. (1994) An integrin-mobilferrin iron transport pathway in intestine and hematopoietic cell. Nutr. Rev. 22, 387-389.
    • (1994) Nutr. Rev. , vol.22 , pp. 387-389
    • Wolf, G.1    Wessling-Resnick, M.2
  • 106
    • 0023007268 scopus 로고
    • Characterization of non-transferrin-bound iron clearance by rat liver
    • Wright, T. L., Brissot, P., Ma, W. L. and Weisiger, R. A. (1986) Characterization of non-transferrin-bound iron clearance by rat liver. J. biol. Chem. 261, 10909-10914.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10909-10914
    • Wright, T.L.1    Brissot, P.2    Ma, W.L.3    Weisiger, R.A.4
  • 107
    • 0023931434 scopus 로고
    • Non-transferrin-bound iron uptake by rat liver. Role of membrane potential difference
    • Wright, T. L., Fitz, J. G. and Weisiger, R. A. (1988) Non-transferrin-bound iron uptake by rat liver. Role of membrane potential difference. J. biol. Chem. 263, 1842-1847.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1842-1847
    • Wright, T.L.1    Fitz, J.G.2    Weisiger, R.A.3


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