메뉴 건너뛰기




Volumn 24, Issue 4 I, 1996, Pages 934-938

Fe-nitrilotriacetic acid-binding proteins associated with rat liver plasma membranes

Author keywords

[No Author keywords available]

Indexed keywords

IRON BINDING PROTEIN; NITRILOTRIACETATE IRON;

EID: 0029832659     PISSN: 02709139     EISSN: None     Source Type: Journal    
DOI: 10.1053/jhep.1996.v24.pm0008855201     Document Type: Article
Times cited : (9)

References (40)
  • 1
    • 0026569505 scopus 로고
    • Receptor-mediated iron uptake and intracellular iron transport
    • Pollack S. Receptor-mediated iron uptake and intracellular iron transport. Am J Hematol 1992;39:113-118.
    • (1992) Am J Hematol , vol.39 , pp. 113-118
    • Pollack, S.1
  • 2
    • 0023280593 scopus 로고
    • Lack of hepatic transferrin receptor expression in hemochromatosis
    • Sciot R, Paterson AC, van den Oord JJ, Desmet VJ. Lack of hepatic transferrin receptor expression in hemochromatosis. HEPATOLOGY 1987;7:831-837.
    • (1987) Hepatology , vol.7 , pp. 831-837
    • Sciot, R.1    Paterson, A.C.2    Van Den Oord, J.J.3    Desmet, V.J.4
  • 3
    • 0025151812 scopus 로고
    • Effect of cellular iron concentration on iron uptake by hepatocytes
    • Trinder D, Batey RG, Morgan EH, Baker E. Effect of cellular iron concentration on iron uptake by hepatocytes. Am J Physiol 1990;259:G611-617.
    • (1990) Am J Physiol , vol.259
    • Trinder, D.1    Batey, R.G.2    Morgan, E.H.3    Baker, E.4
  • 4
    • 0026321461 scopus 로고
    • Regulation of hepatic transferrin, transferrin receptor and ferritin genes in human siderosis
    • Pietrangelo A, Rocchi E, Ferrari A, Ventura E, Cairo G. Regulation of hepatic transferrin, transferrin receptor and ferritin genes in human siderosis. HEPATOLOGY 1991;14:1083-1091.
    • (1991) Hepatology , vol.14 , pp. 1083-1091
    • Pietrangelo, A.1    Rocchi, E.2    Ferrari, A.3    Ventura, E.4    Cairo, G.5
  • 5
    • 0027296586 scopus 로고
    • Regulation of ferritin and transferrin receptor expression by iron in human hepatocyte cultures
    • Hubert N, Lescoat G, Sciot R, Moirand R, Jego P, Leroyer P, Brissot P. Regulation of ferritin and transferrin receptor expression by iron in human hepatocyte cultures. HEPATOLOGY 1993;18:301-312.
    • (1993) Hepatology , vol.18 , pp. 301-312
    • Hubert, N.1    Lescoat, G.2    Sciot, R.3    Moirand, R.4    Jego, P.5    Leroyer, P.6    Brissot, P.7
  • 6
    • 0025157647 scopus 로고
    • The pathology of hepatic iron overload: A free-radical mediated process?
    • Bacon BR, Britton RS. The pathology of hepatic iron overload: a free-radical mediated process? HEPATOLOGY 1990;11:127-137.
    • (1990) Hepatology , vol.11 , pp. 127-137
    • Bacon, B.R.1    Britton, R.S.2
  • 7
    • 0022345593 scopus 로고
    • Efficient clearance of non-transferrin-bound iron by rat liver. Implications for hepatic iron loading in iron overload states
    • Brissot P, Wright TL, Ma WL, Weisiger RA. Efficient clearance of non-transferrin-bound iron by rat liver. Implications for hepatic iron loading in iron overload states. J Clin Invest 1985;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
  • 8
    • 0023007268 scopus 로고
    • Characterization of non-transferrin-bound iron clearance by rat liver
    • Wright TL, Brissot P, Ma WL, Weisiger RA. Characterization of non-transferrin-bound iron clearance by rat liver. J Biol Chem 1986;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
  • 9
    • 0023931434 scopus 로고
    • Non-transferrin-bound iron uptake by rat liver. Role of membrane potential difference
    • Wright TL, Fitz JG, Weisiger RA. Non-transferrin-bound iron uptake by rat liver. Role of membrane potential difference. J Biol Chem 1988;263: 1842-1847.
    • (1988) J Biol Chem , vol.263 , pp. 1842-1847
    • Wright, T.L.1    Fitz, J.G.2    Weisiger, R.A.3
  • 11
    • 0018603774 scopus 로고
    • Some aspects of iron uptake by rat hepatocytes in suspension
    • Grohlich D, Morley CGD, Bezkorovainy A. Some aspects of iron uptake by rat hepatocytes in suspension. Int J Biochem 1979;10:797-802.
    • (1979) Int J Biochem , vol.10 , pp. 797-802
    • Grohlich, D.1    Morley, C.G.D.2    Bezkorovainy, A.3
  • 12
    • 0026007152 scopus 로고
    • Effects of calcium on hepatocyte iron uptake from transferrin, iron-pyrophosphate and iron-ascorbate
    • Nielsen T. Effects of calcium on hepatocyte iron uptake from transferrin, iron-pyrophosphate and iron-ascorbate. Biochim Biophys Acta 1991;1095: 39-45.
    • (1991) Biochim Biophys Acta , vol.1095 , pp. 39-45
    • Nielsen, T.1
  • 13
    • 0028832455 scopus 로고
    • Evidence for a low Km transporter for non-transferrin-bound iron in isolated rat hepatocytes
    • Barisani D, Berg CL, Wessling-Resnick M, Gollan JL. Evidence for a low Km transporter for non-transferrin-bound iron in isolated rat hepatocytes. Am J Physiol 1995;269:G570-G576.
    • (1995) Am J Physiol , vol.269
    • Barisani, D.1    Berg, C.L.2    Wessling-Resnick, M.3    Gollan, J.L.4
  • 14
    • 0028244452 scopus 로고
    • Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron
    • Randell EW, Parkes JG, Olivieri NF, Templeton DM. Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron. J Biol Chem 1994;269:16046-16053.
    • (1994) J Biol Chem , vol.269 , pp. 16046-16053
    • Randell, E.W.1    Parkes, J.G.2    Olivieri, N.F.3    Templeton, D.M.4
  • 15
    • 0028933888 scopus 로고
    • Modulation by iron-loading and chelation of the uptake of non-transferrin-bound iron by human liver cells
    • Parkes JG, Randell EW, Olivieri NF, Templeton DM. Modulation by iron-loading and chelation of the uptake of non-transferrin-bound iron by human liver cells. Biochim Biophys Acta 1995;1243:373-380.
    • (1995) Biochim Biophys Acta , vol.1243 , pp. 373-380
    • Parkes, J.G.1    Randell, E.W.2    Olivieri, N.F.3    Templeton, D.M.4
  • 16
    • 0028966457 scopus 로고
    • Iron transport mechanisms in reticulocytes and mature erythrocytes
    • Hodgson LL, Quail EA, Morgan EH. Iron transport mechanisms in reticulocytes and mature erythrocytes. J Cell Physiol 1995;162:181-190.
    • (1995) J Cell Physiol , vol.162 , pp. 181-190
    • Hodgson, L.L.1    Quail, E.A.2    Morgan, E.H.3
  • 17
    • 0023938640 scopus 로고
    • Carrier-mediated iron transport through erythroid cell membrane
    • Egyed A. Carrier-mediated iron transport through erythroid cell membrane. Br J Haematol 1988;68:483-486.
    • (1988) Br J Haematol , vol.68 , pp. 483-486
    • Egyed, A.1
  • 18
    • 0025793961 scopus 로고
    • The uptake of inorganic iron complexes by human melanoma cells
    • Richardson D, Baker E. The uptake of inorganic iron complexes by human melanoma cells. Biochim Biophys Acta 1991;1093:20-28.
    • (1991) Biochim Biophys Acta , vol.1093 , pp. 20-28
    • Richardson, D.1    Baker, E.2
  • 19
    • 0025774978 scopus 로고
    • Regulation of the transferrin-independent iron transport system in cultured cells
    • Kaplan J, Jordan I, Sturrock A. Regulation of the transferrin-independent iron transport system in cultured cells. J Biol Chem 1991;266:2997-3004.
    • (1991) J Biol Chem , vol.266 , pp. 2997-3004
    • Kaplan, J.1    Jordan, I.2    Sturrock, A.3
  • 20
    • 0027378891 scopus 로고
    • Redox, transferrin-independent, and receptor-mediated endocytosis iron uptake systems in cultured human fibroblasts
    • Oshiro S, Nakajima H, Markello T, Krasnewick D, Bernardini I, Gahl WA. Redox, transferrin-independent, and receptor-mediated endocytosis iron uptake systems in cultured human fibroblasts. J Biol Chem 1993;268: 21586-21591.
    • (1993) J Biol Chem , vol.268 , pp. 21586-21591
    • Oshiro, S.1    Nakajima, H.2    Markello, T.3    Krasnewick, D.4    Bernardini, I.5    Gahl, W.A.6
  • 21
    • 0027512915 scopus 로고
    • Characterization of transferrin-independent iron transport in K562 cells. Unique properties provide evidence for multiple pathways of iron uptake
    • Inman RS, Wessling-Resnick M. Characterization of transferrin-independent iron transport in K562 cells. Unique properties provide evidence for multiple pathways of iron uptake. J Biol Chem 1993;268:8521-8528.
    • (1993) J Biol Chem , vol.268 , pp. 8521-8528
    • Inman, R.S.1    Wessling-Resnick, M.2
  • 24
    • 0028109907 scopus 로고
    • Extracellular ferrireductase activity of K562 cells is coupled to transferrin-independent iron transport
    • Inman RS, Coughlan MM, Wessling-Resnick M. Extracellular ferrireductase activity of K562 cells is coupled to transferrin-independent iron transport. Biochemistry 1994;33:11850-11857.
    • (1994) Biochemistry , vol.33 , pp. 11850-11857
    • Inman, R.S.1    Coughlan, M.M.2    Wessling-Resnick, M.3
  • 25
    • 0028170059 scopus 로고
    • The mammalian transferrin-independent iron transport system may involve a surface ferrireductase activity
    • Jordan I, Kaplan J. The mammalian transferrin-independent iron transport system may involve a surface ferrireductase activity. Biochem J 1994; 302:875-879.
    • (1994) Biochem J , vol.302 , pp. 875-879
    • Jordan, I.1    Kaplan, J.2
  • 26
    • 0028114922 scopus 로고
    • A genetic approach to elucidating eukaryotic iron metabolism
    • Klausner RD, Dancis A. A genetic approach to elucidating eukaryotic iron metabolism. FEBS Lett. 1994;355:109-113.
    • (1994) FEBS Lett. , vol.355 , pp. 109-113
    • Klausner, R.D.1    Dancis, A.2
  • 27
    • 0025688902 scopus 로고
    • Iron uptake by human upper small intestine microvillous membrane vesicles. Indication for a facilitated transport mechanism 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 by a membrane iron-binding protein. J Clin Invest 1990;86: 2145-2153.
    • (1990) J Clin Invest , vol.86 , pp. 2145-2153
    • Teichmann, R.1    Stremmel, W.2
  • 30
    • 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; 269:10242-10246.
    • (1994) J Biol Chem , vol.269 , pp. 10242-10246
    • Li, C.Y.1    Watkins, J.A.2    Glass, J.3
  • 31
    • 0028930195 scopus 로고
    • Iron binding, a new function for the reticulocyte endosome H+-ATPase
    • Li CY, Watkins JA, Hamazaki S, Altazan JD, Glass J. Iron binding, a new function for the reticulocyte endosome H+-ATPase. Biochemistry 1995; 34:5130-5136.
    • (1995) Biochemistry , vol.34 , pp. 5130-5136
    • Li, C.Y.1    Watkins, J.A.2    Hamazaki, S.3    Altazan, J.D.4    Glass, J.5
  • 32
    • 0014492985 scopus 로고
    • Plasma membranes of the rat liver. Isolation and enzymatic characterization of a fraction rich in bile canaliculi
    • Song CS, Rubin W, Bifkind AB, Kappas A. Plasma membranes of the rat liver. Isolation and enzymatic characterization of a fraction rich in bile canaliculi. J Cell Biol 1969;41:124-132.
    • (1969) J Cell Biol , vol.41 , pp. 124-132
    • Song, C.S.1    Rubin, W.2    Bifkind, A.B.3    Kappas, A.4
  • 33
    • 0018568509 scopus 로고
    • Validation of a recording spectrophotometric method for measurement of membrane-associated Mg and Na-K ATPase activity
    • Scharschmidt BF, Keeffe EB, Blankenship NM, Ockner RK. Validation of a recording spectrophotometric method for measurement of membrane-associated Mg and Na-K ATPase activity. J Lab Clin Med 1979;93:790-799.
    • (1979) J Lab Clin Med , vol.93 , pp. 790-799
    • Scharschmidt, B.F.1    Keeffe, E.B.2    Blankenship, N.M.3    Ockner, R.K.4
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey JH. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal Biochem 1981;117: 307-310.
    • (1981) Anal Biochem , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 37
    • 0021114727 scopus 로고
    • Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions
    • Porath J, Olin B. Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions. Biochemistry 1983;22: 1621-1630.
    • (1983) Biochemistry , vol.22 , pp. 1621-1630
    • Porath, J.1    Olin, B.2
  • 38
    • 0018894715 scopus 로고
    • A non-transferrin-bound serum iron in idiopathic hemochromatosis
    • Batey RG, Fong PLC, Shamir S, Sherlock S. A non-transferrin-bound serum iron in idiopathic hemochromatosis. Dig Dis Sci 1980;25:340-346.
    • (1980) Dig Dis Sci , vol.25 , pp. 340-346
    • Batey, R.G.1    Fong, P.L.C.2    Shamir, S.3    Sherlock, S.4
  • 39
    • 0024564712 scopus 로고
    • Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis. Characterization by high performance liquid chromatography and nuclear magnetic resonance spectroscopy
    • Grootveld M, Bell JD, Halliwell B, Aruoma OI, Bomford A, Sadler PJ. Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis. Characterization by high performance liquid chromatography and nuclear magnetic resonance spectroscopy. J Biol Chem 1989; 264:4417-4422.
    • (1989) J Biol Chem , vol.264 , pp. 4417-4422
    • Grootveld, M.1    Bell, J.D.2    Halliwell, B.3    Aruoma, O.I.4    Bomford, A.5    Sadler, P.J.6
  • 40
    • 18244413271 scopus 로고
    • Iron chelate affinity chromatography of brush border membrane proteins
    • Simpson RJ, Raja KB, Shah T. Iron chelate affinity chromatography of brush border membrane proteins. Biochem Soc Trans 1992;20:194.
    • (1992) Biochem Soc Trans , vol.20 , pp. 194
    • Simpson, R.J.1    Raja, K.B.2    Shah, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.