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Volumn 39, Issue 5, 2007, Pages 1006-1015

Iron-independent specific protein expression pattern in the liver of HFE-deficient mice

Author keywords

Hemochromatosis; Iron overload; Liver; Mass spectrometry; Proteomics

Indexed keywords

GLUTATHIONE TRANSFERASE P1; HFE PROTEIN; IRON; PROTEIN; SARCOSINE DEHYDROGENASE; SELENIUM BINDING PROTEIN; SYNAPSIN I; THIOREDOXIN LIKE PROTEIN 2; UNCLASSIFIED DRUG;

EID: 34147155821     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2007.01.021     Document Type: Article
Times cited : (14)

References (43)
  • 2
    • 0024431912 scopus 로고
    • Induction of hypoferremia and modulation of macrophage iron metabolism by tumor necrosis factor
    • Alvarez-Hernandez X., Liceaga J., McKay I.C., and Brock J.H. Induction of hypoferremia and modulation of macrophage iron metabolism by tumor necrosis factor. Laboratory Investigation 61 (1989) 319-322
    • (1989) Laboratory Investigation , vol.61 , pp. 319-322
    • Alvarez-Hernandez, X.1    Liceaga, J.2    McKay, I.C.3    Brock, J.H.4
  • 3
    • 33646370235 scopus 로고    scopus 로고
    • Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
    • Babitt J.L., Huang F.W., Wrighting D.M., Xia Y., Sidis Y., Samad T.A., et al. Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression. Nature Genetics 38 (2006) 531-539
    • (2006) Nature Genetics , vol.38 , pp. 531-539
    • Babitt, J.L.1    Huang, F.W.2    Wrighting, D.M.3    Xia, Y.4    Sidis, Y.5    Samad, T.A.6
  • 4
    • 0037329161 scopus 로고    scopus 로고
    • Multiple roles of major urinary proteins in the house mouse Mus domesticus
    • Beynon R.J., and Hurst J.L. Multiple roles of major urinary proteins in the house mouse Mus domesticus. Biochemical Society Transactions 31 (2003) 142-146
    • (2003) Biochemical Society Transactions , vol.31 , pp. 142-146
    • Beynon, R.J.1    Hurst, J.L.2
  • 5
    • 0037460697 scopus 로고    scopus 로고
    • Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homoeostasis
    • Bridle K.R., Frazer D.M., Wilkins S.J., Dixon J.L., Purdie D.M., Crawford D.H., et al. Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homoeostasis. Lancet 361 (2003) 669-673
    • (2003) Lancet , vol.361 , pp. 669-673
    • Bridle, K.R.1    Frazer, D.M.2    Wilkins, S.J.3    Dixon, J.L.4    Purdie, D.M.5    Crawford, D.H.6
  • 6
    • 2442688699 scopus 로고    scopus 로고
    • Protein profiling of mouse livers with peroxisome proliferator-activated receptor alpha activation
    • Chu R., Lim H., Brumfield L., Liu H., Herring C., Ulintz P., et al. Protein profiling of mouse livers with peroxisome proliferator-activated receptor alpha activation. Molecular and Cellular Biology 24 (2004) 6288-6297
    • (2004) Molecular and Cellular Biology , vol.24 , pp. 6288-6297
    • Chu, R.1    Lim, H.2    Brumfield, L.3    Liu, H.4    Herring, C.5    Ulintz, P.6
  • 7
    • 29244492306 scopus 로고    scopus 로고
    • A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake
    • Devireddy L.R., Gazin C., Zhu X., and Green M.R. A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake. Cell 123 (2005) 1293-1305
    • (2005) Cell , vol.123 , pp. 1293-1305
    • Devireddy, L.R.1    Gazin, C.2    Zhu, X.3    Green, M.R.4
  • 8
    • 0035877982 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha promoter polymorphisms influence the phenotypic expression of hereditary hemochromatosis
    • Fargion S., Valenti L., Dongiovanni P., Scaccabarozzi A., Fracanzani A.L., Taioli E., et al. Tumor necrosis factor alpha promoter polymorphisms influence the phenotypic expression of hereditary hemochromatosis. Blood 97 (2001) 3707-3712
    • (2001) Blood , vol.97 , pp. 3707-3712
    • Fargion, S.1    Valenti, L.2    Dongiovanni, P.3    Scaccabarozzi, A.4    Fracanzani, A.L.5    Taioli, E.6
  • 9
    • 9344224529 scopus 로고    scopus 로고
    • A Novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
    • Feder J.N., Gnirke A., Thomas W., Tsuchihashi Z., Ruddy D.A., Basava A., et al. A Novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nature Genetics 13 (1996) 399-408
    • (1996) Nature Genetics , 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
  • 11
    • 0036196205 scopus 로고    scopus 로고
    • Mechanisms of iron accumulation in hereditary hemochromatosis
    • Fleming R.E., and Sly W.S. Mechanisms of iron accumulation in hereditary hemochromatosis. Annual Review of Physiology 64 (2002) 663-680
    • (2002) Annual Review of Physiology , vol.64 , pp. 663-680
    • Fleming, R.E.1    Sly, W.S.2
  • 13
    • 0037962795 scopus 로고    scopus 로고
    • Orchestrating body iron intake: how and where do intestinal cells take their cues?
    • Frazer D.M., and Anderson G.J. Orchestrating body iron intake: how and where do intestinal cells take their cues?. Blood Cells, Molecules and Diseases 30 (2003) 288-297
    • (2003) Blood Cells, Molecules and Diseases , vol.30 , pp. 288-297
    • Frazer, D.M.1    Anderson, G.J.2
  • 14
    • 12944291468 scopus 로고    scopus 로고
    • Identification of fibrosis-relevant proteins using DIGE (difference in gel electrophoresis) in different models of hepatic fibrosis
    • Henkel C., Roderfeld M., Weiskirchen R., Scheibe B., Matern S., and Roeb E. Identification of fibrosis-relevant proteins using DIGE (difference in gel electrophoresis) in different models of hepatic fibrosis. Zeitschrift fur Gastroenterologie 43 (2005) 23-29
    • (2005) Zeitschrift fur Gastroenterologie , vol.43 , pp. 23-29
    • Henkel, C.1    Roderfeld, M.2    Weiskirchen, R.3    Scheibe, B.4    Matern, S.5    Roeb, E.6
  • 15
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze M.W., and Kuhn L.C. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proceedings of the National Academy of Sciences of the United States of America 93 (1996) 8175-8182
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 16
    • 0015501428 scopus 로고
    • Competing methyltransferase systems
    • Kerr S.J. Competing methyltransferase systems. Journal of Biological Chemistry 247 (1972) 4248-4252
    • (1972) Journal of Biological Chemistry , vol.247 , pp. 4248-4252
    • Kerr, S.J.1
  • 17
    • 33746602284 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha -308G>A allelic variant modulates iron accumulation in patients with hereditary hemochromatosis
    • Krayenbuehl P.A., Maly F.E., Hersberger M., Wiesli P., Himmelmann A., Eid K., et al. Tumor necrosis factor-alpha -308G>A allelic variant modulates iron accumulation in patients with hereditary hemochromatosis. Clinical Chemistry 52 (2006) 1552-1558
    • (2006) Clinical Chemistry , vol.52 , pp. 1552-1558
    • Krayenbuehl, P.A.1    Maly, F.E.2    Hersberger, M.3    Wiesli, P.4    Himmelmann, A.5    Eid, K.6
  • 18
    • 33745526068 scopus 로고    scopus 로고
    • Tumour necrosis factor alpha causes hypoferraemia and reduced intestinal iron absorption in mice
    • Laftah A.H., Sharma N., Brookes M.J., McKie A.T., Simpson R.J., Iqbal T.H., et al. Tumour necrosis factor alpha causes hypoferraemia and reduced intestinal iron absorption in mice. Biochemical Journal 397 (2006) 61-67
    • (2006) Biochemical Journal , vol.397 , pp. 61-67
    • Laftah, A.H.1    Sharma, N.2    Brookes, M.J.3    McKie, A.T.4    Simpson, R.J.5    Iqbal, T.H.6
  • 19
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
    • Lebron J.A., Bennett M.J., Vaughn D.E., Chirino A.J., Snow P.M., Mintier G.A., et al. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell 93 (1998) 111-123
    • (1998) Cell , vol.93 , pp. 111-123
    • Lebron, J.A.1    Bennett, M.J.2    Vaughn, D.E.3    Chirino, A.J.4    Snow, P.M.5    Mintier, G.A.6
  • 21
    • 20044395425 scopus 로고    scopus 로고
    • Endocytic delivery of lipocalin-siderophore-iron complex rescues the kidney from ischemia-reperfusion injury
    • Mori K., Lee H.T., Rapoport D., Drexler I.R., Foster K., Yang J., et al. Endocytic delivery of lipocalin-siderophore-iron complex rescues the kidney from ischemia-reperfusion injury. Journal of Clinical Investigation 115 (2005) 610-621
    • (2005) Journal of Clinical Investigation , 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
  • 22
    • 0037847496 scopus 로고    scopus 로고
    • Constitutive hepcidin expression prevents iron overload in a mouse model of hemochromatosis
    • Nicolas G., Viatte L., Lou D.Q., Bennoun M., Beaumont C., Kahn A., et al. Constitutive hepcidin expression prevents iron overload in a mouse model of hemochromatosis. Nature Genetics 34 (2003) 97-101
    • (2003) Nature Genetics , vol.34 , pp. 97-101
    • Nicolas, G.1    Viatte, L.2    Lou, D.Q.3    Bennoun, M.4    Beaumont, C.5    Kahn, A.6
  • 26
    • 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. New England Journal of Medicine 350 (2004) 2383-2397
    • (2004) New England Journal of Medicine , vol.350 , pp. 2383-2397
    • Pietrangelo, A.1
  • 27
    • 0035896581 scopus 로고    scopus 로고
    • A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin is overexpressed during iron overload
    • Pigeon C., Ilyin G., Courselaud B., Leroyer P., Turlin B., Brissot P., et al. A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin is overexpressed during iron overload. Journal of Biological Chemistry 276 (2001) 7811-7819
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3    Leroyer, P.4    Turlin, B.5    Brissot, P.6
  • 31
    • 0028784211 scopus 로고
    • The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells
    • Richardson D.R., Neumannova V., Nagy E., and Ponka P. The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells. Blood 86 (1995) 3211-3219
    • (1995) Blood , vol.86 , pp. 3211-3219
    • Richardson, D.R.1    Neumannova, V.2    Nagy, E.3    Ponka, P.4
  • 33
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: un amour impossible?
    • Santoni V., Molloy M., and Rabilloud T. Membrane proteins and proteomics: un amour impossible?. Electrophoresis 21 (2000) 1054-1070
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 35
    • 0024273458 scopus 로고
    • The molecular cloning and characterization of murine ferritin heavy chain, a tumor necrosis factor-inducible gene
    • Torti S.V., Kwak E.L., Miller S.C., Miller L.L., Ringold G.M., Myambo K.B., et al. The molecular cloning and characterization of murine ferritin heavy chain, a tumor necrosis factor-inducible gene. Journal of Biological Chemistry 263 (1988) 12638-12644
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 12638-12644
    • Torti, S.V.1    Kwak, E.L.2    Miller, S.C.3    Miller, L.L.4    Ringold, G.M.5    Myambo, K.B.6
  • 36
    • 33745898241 scopus 로고    scopus 로고
    • Bone morphogenetic proteins 2, 4, and 9 stimulate murine hepcidin 1 expression independently of Hfe, transferrin receptor 2 (Tfr2), and IL-6
    • Truksa J., Peng H., Lee P., and Beutler E. Bone morphogenetic proteins 2, 4, and 9 stimulate murine hepcidin 1 expression independently of Hfe, transferrin receptor 2 (Tfr2), and IL-6. Proceedings of the National Academy of Sciences of the United States of America 103 (2006) 10289-10293
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , pp. 10289-10293
    • Truksa, J.1    Peng, H.2    Lee, P.3    Beutler, E.4
  • 37
    • 0025767108 scopus 로고
    • Tumor necrosis factor-alpha and interleukin 1-alpha regulate transferrin receptor in human diploid fibroblasts. Relationship to the induction of ferritin heavy chain
    • Tsuji Y., Miller L.L., Miller S.C., Torti S.V., and Torti F.M. Tumor necrosis factor-alpha and interleukin 1-alpha regulate transferrin receptor in human diploid fibroblasts. Relationship to the induction of ferritin heavy chain. Journal of Biological Chemistry 266 (1991) 7257-7261
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 7257-7261
    • Tsuji, Y.1    Miller, L.L.2    Miller, S.C.3    Torti, S.V.4    Torti, F.M.5
  • 38
    • 0030732164 scopus 로고    scopus 로고
    • Hereditary hemochromatosis: effects of C282Y and H63D mutations on association with beta2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells
    • Waheed A., Parkkila S., Zhou X.Y., Tomatsu S., Tsuchihashi Z., Feder J.N., et al. Hereditary hemochromatosis: effects of C282Y and H63D mutations on association with beta2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells. Proceedings of the National Academy of Sciences of the United States of America 94 (1997) 12384-12389
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , pp. 12384-12389
    • Waheed, A.1    Parkkila, S.2    Zhou, X.Y.3    Tomatsu, S.4    Tsuchihashi, Z.5    Feder, J.N.6
  • 39
    • 33644876815 scopus 로고    scopus 로고
    • A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression
    • Wang R.H., Li C., Xu X., Zheng Y., Xiao C., Zerfas P., et al. A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression. Cell Metabolism 2 (2005) 399-409
    • (2005) Cell Metabolism , vol.2 , pp. 399-409
    • Wang, R.H.1    Li, C.2    Xu, X.3    Zheng, Y.4    Xiao, C.5    Zerfas, P.6
  • 40
    • 0034695550 scopus 로고    scopus 로고
    • Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain
    • Witte S., Villalba M., Bi K., Liu Y., Isakov N., and Altman A. Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain. Journal of Biological Chemistry 275 (2000) 1902-1909
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 1902-1909
    • Witte, S.1    Villalba, M.2    Bi, K.3    Liu, Y.4    Isakov, N.5    Altman, A.6
  • 41
    • 33748919803 scopus 로고    scopus 로고
    • Human glutathione-S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals
    • Wu Y., Fan Y., Xue B., Luo L., Shen J., Zhang S., et al. Human glutathione-S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals. Oncogene 25 (2006) 5787-5800
    • (2006) Oncogene , vol.25 , pp. 5787-5800
    • Wu, Y.1    Fan, Y.2    Xue, B.3    Luo, L.4    Shen, J.5    Zhang, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.