메뉴 건너뛰기




Volumn 166, Issue 4, 2005, Pages 973-983

Plasma protein haptoglobin modulates renal iron loading

Author keywords

[No Author keywords available]

Indexed keywords

HAPTOGLOBIN; HEMOGLOBIN; PLASMA PROTEIN;

EID: 20244371687     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)62319-X     Document Type: Article
Times cited : (91)

References (41)
  • 1
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze MW, Muckenthaler MU, Andrews NC: Balancing acts: molecular control of mammalian iron metabolism. Cell 2004, 117:285-297
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 2
    • 0035474950 scopus 로고    scopus 로고
    • Recent advances in disorders of iron metabolism: Mutations, mechanisms and modifiers
    • Roy CN, Andrews NC: Recent advances in disorders of iron metabolism: mutations, mechanisms and modifiers. Hum Mol Genet 2001, 10:2181-2186
    • (2001) Hum Mol Genet , vol.10 , pp. 2181-2186
    • Roy, C.N.1    Andrews, N.C.2
  • 8
    • 17144363497 scopus 로고    scopus 로고
    • Congenital Haptoglobin Deficiency
    • Manoharan A: Congenital Haptoglobin Deficiency. Blood 1997, 90:17093-1709
    • (1997) Blood , vol.90 , pp. 17093-11709
    • Manoharan, A.1
  • 9
    • 0036893006 scopus 로고    scopus 로고
    • Haptoglobin polymorphism and iron homeostasis
    • Beutler E, Gelbart T, Lee P: Haptoglobin polymorphism and iron homeostasis. Clin Chem 2002, 48:2232-2235
    • (2002) Clin Chem , vol.48 , pp. 2232-2235
    • Beutler, E.1    Gelbart, T.2    Lee, P.3
  • 12
    • 0022456054 scopus 로고
    • A rapid method for the preparation of 1251-labelled human growth hormone for receptor studies, using reverse-phase high performance liquid chromatography
    • Hondo MM, Dehart I, De Meyts P: A rapid method for the preparation of 1251-labelled human growth hormone for receptor studies, using reverse-phase high performance liquid chromatography. Biochem Biophys Res Commun 1986, 134:671-677
    • (1986) Biochem Biophys Res Commun , vol.134 , pp. 671-677
    • Hondo, M.M.1    Dehart, I.2    De Meyts, P.3
  • 13
    • 0036893587 scopus 로고    scopus 로고
    • Enhanced splenomegaly and severe liver inflammation in haptoglobin/hemopexin double-null mice after acute hemolysis
    • Tolosano E, Fagoonee S, Hirsch E, Berger FG, Baumann H, Silengo L, Altruda F: Enhanced splenomegaly and severe liver inflammation in haptoglobin/hemopexin double-null mice after acute hemolysis. Blood 2002, 100:4201-4208
    • (2002) Blood , vol.100 , pp. 4201-4208
    • Tolosano, E.1    Fagoonee, S.2    Hirsch, E.3    Berger, F.G.4    Baumann, H.5    Silengo, L.6    Altruda, F.7
  • 15
    • 0034777015 scopus 로고    scopus 로고
    • Comparison of bathophenanthroline sulfonate and ferene as chromogens in colorimetric measurement of low hepatic iron concentration
    • Pieroni L, Khalil L, Charlotte F, Poynard T, Piton A, Hainque B, Imbert-Bismut F: Comparison of bathophenanthroline sulfonate and ferene as chromogens in colorimetric measurement of low hepatic iron concentration. Clin Chem 2001, 47:2059-2061
    • (2001) Clin Chem , vol.47 , pp. 2059-2061
    • Pieroni, L.1    Khalil, L.2    Charlotte, F.3    Poynard, T.4    Piton, A.5    Hainque, B.6    Imbert-Bismut, F.7
  • 16
    • 0037148525 scopus 로고    scopus 로고
    • The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading
    • Degani S, Balzac F, Brancaccio M, Guazzone S, Retta SF, Silengo L, Eva A, Tarone G: The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading. J Cell Biol 2002, 156:377-387
    • (2002) J Cell Biol , vol.156 , pp. 377-387
    • Degani, S.1    Balzac, F.2    Brancaccio, M.3    Guazzone, S.4    Retta, S.F.5    Silengo, L.6    Eva, A.7    Tarone, G.8
  • 17
    • 0028321518 scopus 로고
    • Cytochrome P-450 mediates tissue-damaging hydroxyl radical formation during reoxygenation of the kidney
    • Paller MS, Jacob HS: Cytochrome P-450 mediates tissue-damaging hydroxyl radical formation during reoxygenation of the kidney. Proc Natl Acad Sci USA 1994, 91:7002-7006
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7002-7006
    • Paller, M.S.1    Jacob, H.S.2
  • 18
    • 0023755521 scopus 로고
    • Hemoglobin- and myoglobin-induced acute renal failure in rats: Role of iron in nephrotoxicity
    • Paller MS: Hemoglobin- and myoglobin-induced acute renal failure in rats: role of iron in nephrotoxicity. Am J Physiol 1988, 255:F539-F544
    • (1988) Am J Physiol , vol.255
    • Paller, M.S.1
  • 19
    • 0023774805 scopus 로고
    • Role of iron in postischemic renal injury in the rat
    • Paller MS, Hedlund BE: Role of iron in postischemic renal injury in the rat. Kidney Int 1988, 34:474-480
    • (1988) Kidney Int , vol.34 , pp. 474-480
    • Paller, M.S.1    Hedlund, B.E.2
  • 22
    • 0030070639 scopus 로고    scopus 로고
    • Rhabdomyolysis and myohemoglobinuric acute renal failure
    • Zager RA: Rhabdomyolysis and myohemoglobinuric acute renal failure. Kidney Int 1996, 49:314-326
    • (1996) Kidney Int , vol.49 , pp. 314-326
    • Zager, R.A.1
  • 23
    • 0028810954 scopus 로고
    • Iron, heme oxygenase, and glutathione: Effects on myohemoglobinuric proximal tubular injury
    • Zager RA, Burkhart KM, Conrad DS, Gmur DJ: Iron, heme oxygenase, and glutathione: effects on myohemoglobinuric proximal tubular injury. Kidney Int 1995, 48:1624-1634
    • (1995) Kidney Int , vol.48 , pp. 1624-1634
    • Zager, R.A.1    Burkhart, K.M.2    Conrad, D.S.3    Gmur, D.J.4
  • 24
    • 84984766757 scopus 로고    scopus 로고
    • Megalin and cubilin: Multifunctional endocytic receptors
    • Christensen EI, Birn H: Megalin and cubilin: multifunctional endocytic receptors. Nat Rev Mol Cell Biol 2002, 3:256-266
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 256-266
    • Christensen, E.I.1    Birn, H.2
  • 26
    • 0020320825 scopus 로고
    • Kinetic aspects of hemoglobin.haptoglobin-receptor interaction in rat liver plasma membranes, isolated liver cells, and liver cells in primary culture
    • Kino K, Tsunoo H, Higa Y, Takami M, Nakajima H: Kinetic aspects of hemoglobin.haptoglobin-receptor interaction in rat liver plasma membranes, isolated liver cells, and liver cells in primary culture. J Biol Chem 1982, 257:4828-4833
    • (1982) J Biol Chem , vol.257 , pp. 4828-4833
    • Kino, K.1    Tsunoo, H.2    Higa, Y.3    Takami, M.4    Nakajima, H.5
  • 27
    • 0023689975 scopus 로고
    • Intrahepatocellular site of the catabolism of heme and globin moiety of hemoglobin-haptoglobin after intravenous administration to rats
    • Oshiro S, Nakajima H: Intrahepatocellular site of the catabolism of heme and globin moiety of hemoglobin-haptoglobin after intravenous administration to rats. J Biol Chem 1988, 263:16032-16038
    • (1988) J Biol Chem , vol.263 , pp. 16032-16038
    • Oshiro, S.1    Nakajima, H.2
  • 29
    • 0036174088 scopus 로고    scopus 로고
    • CD163: A signal receptor scavenging haptoglobin-hemoglobin complexes from plasma
    • Graversen JH, Madsen M, Moestrup SK: CD163: a signal receptor scavenging haptoglobin-hemoglobin complexes from plasma. Int J Biochem Cell Biol 2002, 34:309-314
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 309-314
    • Graversen, J.H.1    Madsen, M.2    Moestrup, S.K.3
  • 30
    • 0032145516 scopus 로고    scopus 로고
    • Internalization study using EDTA-prepared hepatocytes for receptor-mediated endocytosis of haemoglobin-haptoglobin complex
    • Zuwala-Jagiello J, Osada J: Internalization study using EDTA-prepared hepatocytes for receptor-mediated endocytosis of haemoglobin-haptoglobin complex. Int J Biochem Cell Biol 1998, 30:923-931
    • (1998) Int J Biochem Cell Biol , vol.30 , pp. 923-931
    • Zuwala-Jagiello, J.1    Osada, J.2
  • 31
    • 0026731506 scopus 로고
    • Expression of haptoglobin receptors in human hepatoma cells
    • Okuda M, Tokunaga R, Taketani S: Expression of haptoglobin receptors in human hepatoma cells. Biochim Biophys Acta 1992, 1136:143-149
    • (1992) Biochim Biophys Acta , vol.1136 , pp. 143-149
    • Okuda, M.1    Tokunaga, R.2    Taketani, S.3
  • 32
    • 0041672570 scopus 로고    scopus 로고
    • Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation
    • Ganz T: Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation. Blood 2003, 102:783-788
    • (2003) Blood , vol.102 , pp. 783-788
    • Ganz, T.1
  • 33
    • 85047693999 scopus 로고    scopus 로고
    • Anemia of inflammation: The cytokine-hepcidin link
    • Andrews NC: Anemia of inflammation: the cytokine-hepcidin link. J Clin Invest 2004, 113:1251-1253
    • (2004) J Clin Invest , vol.113 , pp. 1251-1253
    • Andrews, N.C.1
  • 35
    • 0032079491 scopus 로고    scopus 로고
    • Congenital anhaptoglobinemia versus acquired hypohaptoglobinemia
    • Delanghe J, Langlois M, De Buyzere M: Congenital anhaptoglobinemia versus acquired hypohaptoglobinemia. Blood 1998, 91:3524
    • (1998) Blood , vol.91 , pp. 3524
    • Delanghe, J.1    Langlois, M.2    De Buyzere, M.3
  • 36
    • 1542286876 scopus 로고    scopus 로고
    • Ferroportin-1 is not upregulated in copper-deficient mice
    • Chung J, Prohaska JR, Wessling-Resnick M: Ferroportin-1 is not upregulated in copper-deficient mice. J Nutr 2004, 134:517-521
    • (2004) J Nutr , vol.134 , pp. 517-521
    • Chung, J.1    Prohaska, J.R.2    Wessling-Resnick, M.3
  • 37
    • 0023707789 scopus 로고
    • Evidence suggesting a role for hydroxyl radical in glycerol-induced acute renal failure
    • Shah SV, Walker PD: Evidence suggesting a role for hydroxyl radical in glycerol-induced acute renal failure. Am J Physiol 1988, 255:F438-F443
    • (1988) Am J Physiol , vol.255
    • Shah, S.V.1    Walker, P.D.2
  • 38
    • 0036259938 scopus 로고    scopus 로고
    • Hemopexin: Structure, function, and regulation
    • Tolosano E, Altruda F: Hemopexin: structure, function, and regulation. DNA Cell BiOl 2002, 21:297-306
    • (2002) DNA Cell BiOl , vol.21 , pp. 297-306
    • Tolosano, E.1    Altruda, F.2
  • 39
    • 0037085766 scopus 로고    scopus 로고
    • Processing of the lipocalin alpha(1)-microglobulin by hemoglobin induces heme-binding and heme-degradation properties
    • Allhorn M, Berggard T, Nordberg J, Olsson ML, Akerstrom B: Processing of the lipocalin alpha(1)-microglobulin by hemoglobin induces heme-binding and heme-degradation properties. Blood 2002, 99:1894-1901
    • (2002) Blood , vol.99 , pp. 1894-1901
    • Allhorn, M.1    Berggard, T.2    Nordberg, J.3    Olsson, M.L.4    Akerstrom, B.5
  • 40
    • 0030875594 scopus 로고    scopus 로고
    • Tissue, temporal and inducible expression pattern of haptoglobin in mice
    • D'Armiento J, Dalal SS, Chada K: Tissue, temporal and inducible expression pattern of haptoglobin in mice. Gene 1997, 195:19-27
    • (1997) Gene , vol.195 , pp. 19-27
    • D'Armiento, J.1    Dalal, S.S.2    Chada, K.3
  • 41
    • 0037560989 scopus 로고    scopus 로고
    • The acute phase protein haptoglobin is locally expressed in arthritic and oncological tissues
    • Smeets MB, Fontijn J, Kavelaars A, Pasterkamp G, De Kleijn DP: The acute phase protein haptoglobin is locally expressed in arthritic and oncological tissues. Int J Exp Pathol 2003, 84:69-74
    • (2003) Int J Exp Pathol , vol.84 , pp. 69-74
    • Smeets, M.B.1    Fontijn, J.2    Kavelaars, A.3    Pasterkamp, G.4    De Kleijn, D.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.