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Volumn 49, Issue 3, 2009, Pages 1012-1016

Is the iron donor lipocalin 2 implicated in the pathophysiology of hereditary hemochromatosis?

Author keywords

[No Author keywords available]

Indexed keywords

HFE PROTEIN; IRON; NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN; TRANSFERRIN; ACUTE PHASE PROTEIN; HFE PROTEIN, MOUSE; HLA ANTIGEN CLASS 1; LCN2 PROTEIN, MOUSE; LIPOCALIN; MEMBRANE PROTEIN; ONCOPROTEIN;

EID: 63349099823     PISSN: 02709139     EISSN: None     Source Type: Journal    
DOI: 10.1002/hep.22699     Document Type: Article
Times cited : (8)

References (43)
  • 1
    • 0032830130 scopus 로고    scopus 로고
    • The transferrin receptor: Role in health and disease
    • Ponka P, Lok CN. The transferrin receptor: Role in health and disease. Int J Biochem Cell Biol 1999;31:1111-1137.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1111-1137
    • Ponka, P.1    Lok, C.N.2
  • 3
    • 0011938460 scopus 로고
    • Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse: A rodent model for hemochromatosis
    • Craven CM, Alexander J, Eldridge M, Kushner JP, Bernstein S, Kaplan J. Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse: A rodent model for hemochromatosis. Proc Natl Acad Sci U S A 1987;84:3457-3461.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 3457-3461
    • Craven, C.M.1    Alexander, J.2    Eldridge, M.3    Kushner, J.P.4    Bernstein, S.5    Kaplan, J.6
  • 4
    • 0034006860 scopus 로고    scopus 로고
    • Genetic disorders affecting proteins of iron metabolism: Clinical implications
    • Sheth S, Brittenham GM. Genetic disorders affecting proteins of iron metabolism: Clinical implications. Ann Rev Med 2000;51:443-464.
    • (2000) Ann Rev Med , vol.51 , pp. 443-464
    • Sheth, S.1    Brittenham, G.M.2
  • 5
    • 9344224529 scopus 로고    scopus 로고
    • A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
    • Feder JN, Gnirke A, Thomas W, Tsuchihashi Z, Ruddy DA, Basava A, et al. A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat Genet 1996;13:399-408.
    • (1996) Nat Genet , vol.13 , pp. 399-408
    • Feder, J.N.1    Gnirke, A.2    Thomas, W.3    Tsuchihashi, Z.4    Ruddy, D.A.5    Basava, A.6
  • 6
    • 2542560427 scopus 로고    scopus 로고
    • Hereditary hemochromatosis - a new look at an old disease
    • Pietrangelo A. Hereditary hemochromatosis - a new look at an old disease. N Engl J Med 2004;350:2383-2397.
    • (2004) N Engl J Med , vol.350 , pp. 2383-2397
    • Pietrangelo, A.1
  • 7
    • 0342264467 scopus 로고    scopus 로고
    • Determination of non-transferrin-bound iron in genetic hemochromatosis using a new HPLC-based method
    • Loreal O, Gosriwatana I, Guyader D, Porter J, Brissot P, Hider RC. Determination of non-transferrin-bound iron in genetic hemochromatosis using a new HPLC-based method. J Hepatol 2000;32:727-733.
    • (2000) J Hepatol , vol.32 , pp. 727-733
    • Loreal, O.1    Gosriwatana, I.2    Guyader, D.3    Porter, J.4    Brissot, P.5    Hider, R.C.6
  • 8
    • 4444226451 scopus 로고    scopus 로고
    • Nontransferrin-bound iron uptake by hepatocytes is increased in the Hfe knockout mouse model of hereditary hemochromatosis
    • Chua AC, Olynyk JK, Leedman PJ, Trinder D. Nontransferrin-bound iron uptake by hepatocytes is increased in the Hfe knockout mouse model of hereditary hemochromatosis. Blood 2004;104:1519-1525.
    • (2004) Blood , vol.104 , pp. 1519-1525
    • Chua, A.C.1    Olynyk, J.K.2    Leedman, P.J.3    Trinder, D.4
  • 9
    • 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
  • 10
    • 18244399587 scopus 로고    scopus 로고
    • Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver
    • Gunshin H, Fujiwara Y, Custodio AO, DiRenzo C, Robine S, Andrews NC. Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver. J Clin Invest 2005;115:1258-1266.
    • (2005) J Clin Invest , vol.115 , pp. 1258-1266
    • Gunshin, H.1    Fujiwara, Y.2    Custodio, A.O.3    DiRenzo, C.4    Robine, S.5    Andrews, N.C.6
  • 11
    • 0027256664 scopus 로고
    • Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
    • Kjeldsen L, Johnsen AH, Sengelov H, Borregaard N. Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. J Biol Chem 1993;268:10425-10432.
    • (1993) J Biol Chem , vol.268 , pp. 10425-10432
    • Kjeldsen, L.1    Johnsen, A.H.2    Sengelov, H.3    Borregaard, N.4
  • 12
    • 0037184526 scopus 로고    scopus 로고
    • Mechanisms of cellular iron acquisition: Another iron in the fire
    • Kaplan J. Mechanisms of cellular iron acquisition: Another iron in the fire. Cell 2002;111:603-606.
    • (2002) Cell , vol.111 , pp. 603-606
    • Kaplan, J.1
  • 13
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz DH, Holmes MA, Borregaard N, Bluhm ME, Raymond KN, Strong RK. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol Cell 2002;10: 1033-1043.
    • (2002) Mol Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 15
    • 34248345026 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin as the realtime indicator of active kidney damage
    • Mori K, Nakao K. Neutrophil gelatinase-associated lipocalin as the realtime indicator of active kidney damage. Kidney Int 2007;71:967-970.
    • (2007) Kidney Int , vol.71 , pp. 967-970
    • Mori, K.1    Nakao, K.2
  • 16
    • 51249118191 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin: New paths for an old shuttle
    • Devarajan P. Neutrophil gelatinase-associated lipocalin: New paths for an old shuttle. Cancer Ther 2007;5:463-470.
    • (2007) Cancer Ther , vol.5 , pp. 463-470
    • Devarajan, P.1
  • 17
    • 17144391432 scopus 로고    scopus 로고
    • Lipocalin 2 diminishes invasiveness and metastasis of Ras-transformed cells
    • Hanai J, Mammoto T, Seth P, Mori K, Karumanchi SA, Barasch J, et al. Lipocalin 2 diminishes invasiveness and metastasis of Ras-transformed cells. J Biol Chem 2005;280:13641-13647.
    • (2005) J Biol Chem , vol.280 , pp. 13641-13647
    • Hanai, J.1    Mammoto, T.2    Seth, P.3    Mori, K.4    Karumanchi, S.A.5    Barasch, J.6
  • 18
    • 9644307879 scopus 로고    scopus 로고
    • Amelioration of ischemic acute renal injury by neutrophil gelatinase-associated lipocalin
    • Mishra J, Mori K, Ma Q, Kelly C, Yang J, Mitsnefes M, et al. Amelioration of ischemic acute renal injury by neutrophil gelatinase-associated lipocalin. J Am Soc Nephrol 2004;15:3073-3082.
    • (2004) J Am Soc Nephrol , vol.15 , pp. 3073-3082
    • Mishra, J.1    Mori, K.2    Ma, Q.3    Kelly, C.4    Yang, J.5    Mitsnefes, M.6
  • 19
    • 20044395425 scopus 로고    scopus 로고
    • Endocytic delivery of lipocalin-siderophore-iron complex rescues the kidney from ischemia-reperfusion injury
    • Mori K, Lee HT, Rapoport D, Drexler IR, Foster K, Yang J, et al. Endocytic delivery of lipocalin-siderophore-iron complex rescues the kidney from ischemia-reperfusion injury. J Clin Invest 2005;115:610-621.
    • (2005) J Clin Invest , vol.115 , pp. 610-621
    • Mori, K.1    Lee, H.T.2    Rapoport, D.3    Drexler, I.R.4    Foster, K.5    Yang, J.6
  • 20
    • 2942520091 scopus 로고    scopus 로고
    • Delivery of ferric ion to mouse spermatozoa is mediated by lipocalin internalization
    • Elangovan N, Lee Y-C, Tzeng W-F, Chu S-T. Delivery of ferric ion to mouse spermatozoa is mediated by lipocalin internalization. Biochem Biophys Res Commun 2004;319:1096-1104.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 1096-1104
    • Elangovan, N.1    Lee, Y.-C.2    Tzeng, W.-F.3    Chu, S.-T.4
  • 22
    • 0035800508 scopus 로고    scopus 로고
    • Induction of apoptosis by a secreted lipocalin that is transcriptionally regulated by IL-3 deprivation
    • Devireddy LR, Teodoro JG, Richard FA, Green MR. Induction of apoptosis by a secreted lipocalin that is transcriptionally regulated by IL-3 deprivation. Science 2001;293:829-834.
    • (2001) Science , vol.293 , pp. 829-834
    • Devireddy, L.R.1    Teodoro, J.G.2    Richard, F.A.3    Green, M.R.4
  • 23
    • 11144314814 scopus 로고    scopus 로고
    • Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
    • Flo TH, Smith KD, Sato S, Rodriguez DJ, Holmes MA, Strong RK, et al. Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 2004;432:917-921.
    • (2004) Nature , vol.432 , pp. 917-921
    • Flo, T.H.1    Smith, K.D.2    Sato, S.3    Rodriguez, D.J.4    Holmes, M.A.5    Strong, R.K.6
  • 24
    • 32444442757 scopus 로고    scopus 로고
    • Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury
    • Berger T, Togawa A, Duncan GS, Elia AJ, You-Ten A, Wakeham A, et al. Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury. Proc Natl Acad Sci U S A 2006;103:1834-1839.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 1834-1839
    • Berger, T.1    Togawa, A.2    Duncan, G.S.3    Elia, A.J.4    You-Ten, A.5    Wakeham, A.6
  • 25
    • 40949119413 scopus 로고    scopus 로고
    • Lipocalin 2-mediated growth suppression is evident in human erythroid and monocyte/macrophage lineage cells
    • Miharada K, Hiroyama T, Sudo K, Danjo I, Nagasawa T, Nakamura Y. Lipocalin 2-mediated growth suppression is evident in human erythroid and monocyte/macrophage lineage cells. J Cell Physiol 2008;215:526-537.
    • (2008) J Cell Physiol , vol.215 , pp. 526-537
    • Miharada, K.1    Hiroyama, T.2    Sudo, K.3    Danjo, I.4    Nagasawa, T.5    Nakamura, Y.6
  • 26
    • 27744448101 scopus 로고    scopus 로고
    • Lipocalin 2 functions as a negative regulator of red blood cell production in an autocrine fashion
    • Miharada K, Hiroyama T, Sudo K, Nagasawa T, Nakamura Y. Lipocalin 2 functions as a negative regulator of red blood cell production in an autocrine fashion. FASEB J. 2005;19:1881-1883.
    • (2005) FASEB J , vol.19 , pp. 1881-1883
    • Miharada, K.1    Hiroyama, T.2    Sudo, K.3    Nagasawa, T.4    Nakamura, Y.5
  • 27
    • 12744272449 scopus 로고    scopus 로고
    • The endocytic receptor megalin binds the iron transporting neutrophil-gelatinase-associated lipocalin with high affinity and mediates its cellular uptake
    • Hvidberg V, Jacobsen C, Strong RK, Cowland JB, Moestrup SK, Borregaard N. The endocytic receptor megalin binds the iron transporting neutrophil-gelatinase-associated lipocalin with high affinity and mediates its cellular uptake. FEBS Lett 2005;579:773-777.
    • (2005) FEBS Lett , vol.579 , pp. 773-777
    • Hvidberg, V.1    Jacobsen, C.2    Strong, R.K.3    Cowland, J.B.4    Moestrup, S.K.5    Borregaard, N.6
  • 28
    • 0027079937 scopus 로고
    • Low density lipoprotein receptor-related protein and gp330 bind similar ligands, including plasminogen activator-inhibitor complexes and lactoferrin, an inhibitor of chylomicron remnant clearance
    • Willnow TE, Goldstein JL, Orth K, Brown MS, Herz J. Low density lipoprotein receptor-related protein and gp330 bind similar ligands, including plasminogen activator-inhibitor complexes and lactoferrin, an inhibitor of chylomicron remnant clearance. J Biol Chem 1992;267:26172-26180.
    • (1992) J Biol Chem , vol.267 , pp. 26172-26180
    • Willnow, T.E.1    Goldstein, J.L.2    Orth, K.3    Brown, M.S.4    Herz, J.5
  • 29
    • 0028847966 scopus 로고
    • Removal of lactoferrin from plasma is mediated by binding to low density lipoprotein receptor-related protein/α2-macroglobulin receptor and transport to endosomes
    • Meilinger M, Haumer M, Szakmary KA, Steinbock F, Scheiber B, Goldenberg H, et al. Removal of lactoferrin from plasma is mediated by binding to low density lipoprotein receptor-related protein/α2-macroglobulin receptor and transport to endosomes. FEBS Lett 1995;360:70-74.
    • (1995) FEBS Lett , vol.360 , pp. 70-74
    • Meilinger, M.1    Haumer, M.2    Szakmary, K.A.3    Steinbock, F.4    Scheiber, B.5    Goldenberg, H.6
  • 31
    • 0033168767 scopus 로고    scopus 로고
    • The C282Y mutation causing hereditary hemochromatosis does not produce a null allele
    • Levy JE, Montross LK, Cohen DE, Fleming MD, Andrews NC. The C282Y mutation causing hereditary hemochromatosis does not produce a null allele. Blood 1999;94:9-11.
    • (1999) Blood , vol.94 , pp. 9-11
    • Levy, J.E.1    Montross, L.K.2    Cohen, D.E.3    Fleming, M.D.4    Andrews, N.C.5
  • 33
    • 24344468431 scopus 로고    scopus 로고
    • Contribution of Hfe expression in macrophages to the regulation of hepatic hepcidin levels and iron loading
    • Makui H, Soares RJ, Jiang W, Constante M, Santos MM. Contribution of Hfe expression in macrophages to the regulation of hepatic hepcidin levels and iron loading. Blood 2005;106:2189-2195.
    • (2005) Blood , vol.106 , pp. 2189-2195
    • Makui, H.1    Soares, R.J.2    Jiang, W.3    Constante, M.4    Santos, M.M.5
  • 35
    • 0033677772 scopus 로고    scopus 로고
    • The importance of non-transferrin bound iron in disorders of iron metabolism
    • Breuer W, Hershko C, Cabantchik ZI. The importance of non-transferrin bound iron in disorders of iron metabolism. Transfus Sci 2000;23:185-192.
    • (2000) Transfus Sci , vol.23 , pp. 185-192
    • Breuer, W.1    Hershko, C.2    Cabantchik, Z.I.3
  • 36
    • 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
  • 37
    • 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
  • 38
    • 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
  • 39
    • 0033546223 scopus 로고    scopus 로고
    • Modulation of iron uptake in heart by L-Type Ca2+ channel modifiers: Possible implications in iron overload
    • Tsushima RG, Wickenden AD, Bouchard RA, Oudit GY, Liu PP, Backx PH. Modulation of iron uptake in heart by L-Type Ca2+ channel modifiers: possible implications in iron overload. Circ Res 1999;84:1302-1309.
    • (1999) Circ Res , vol.84 , pp. 1302-1309
    • Tsushima, R.G.1    Wickenden, A.D.2    Bouchard, R.A.3    Oudit, G.Y.4    Liu, P.P.5    Backx, P.H.6
  • 41
    • 34548767817 scopus 로고    scopus 로고
    • Voltage-gated calcium channels provide an alternate route for iron uptake in neuronal cell cultures
    • Gaasch J, Geldenhuys W, Lockman P, Allen D, Van der Schyf C. Voltage-gated calcium channels provide an alternate route for iron uptake in neuronal cell cultures. Neurochem Res 2007;32:1686-1693.
    • (2007) Neurochem Res , vol.32 , pp. 1686-1693
    • Gaasch, J.1    Geldenhuys, W.2    Lockman, P.3    Allen, D.4    Van der Schyf, C.5
  • 42
    • 0141461407 scopus 로고    scopus 로고
    • L-type Ca2+ channels provide a major pathway for iron entry into cardiomyocytes in iron-overload cardiomyopathy
    • Oudit GY, Sun H, Trivieri MG, Koch SE, Dawood F, Ackerley C, et al. L-type Ca2+ channels provide a major pathway for iron entry into cardiomyocytes in iron-overload cardiomyopathy. Nat Med 2003;9:1187-1194.
    • (2003) Nat Med , vol.9 , pp. 1187-1194
    • Oudit, G.Y.1    Sun, H.2    Trivieri, M.G.3    Koch, S.E.4    Dawood, F.5    Ackerley, C.6
  • 43
    • 11844279752 scopus 로고    scopus 로고
    • Structure-function analysis of a novel member of the LIV-1 subfamily of zinc transporters, ZIP14
    • Taylor KM, Morgan HE, Johnson A, Nicholson RI. Structure-function analysis of a novel member of the LIV-1 subfamily of zinc transporters, ZIP14. FEBS Letters 2005;579:427-432.
    • (2005) FEBS Letters , vol.579 , pp. 427-432
    • Taylor, K.M.1    Morgan, H.E.2    Johnson, A.3    Nicholson, R.I.4


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