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Volumn 1784, Issue 12, 2008, Pages 2029-2037

Secretion of bioactive hepcidin-25 by liver cells correlates with its gene transcription and points towards synergism between iron and inflammation signaling pathways

Author keywords

Ferroportin; Hepcidin; Mass spectrometry; Prohepcidin; Secretory pathway

Indexed keywords

BONE MORPHOGENETIC PROTEIN; FERROPORTIN; HEPCIDIN; HEPCIDIN 25; INTERLEUKIN 6; IRON; UNCLASSIFIED DRUG;

EID: 54549087621     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.08.004     Document Type: Article
Times cited : (28)

References (57)
  • 1
    • 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 102 (2003) 783-788
    • (2003) Blood , vol.102 , pp. 783-788
    • Ganz, T.1
  • 3
    • 33646899011 scopus 로고    scopus 로고
    • Hereditary hemochromatosis: genetic complexity and new diagnostic approaches
    • Swinkels D.W., Janssen M.C., Bergmans J., and Marx J.J. Hereditary hemochromatosis: genetic complexity and new diagnostic approaches. Clin. Chem. 52 (2006) 950-968
    • (2006) Clin. Chem. , vol.52 , pp. 950-968
    • Swinkels, D.W.1    Janssen, M.C.2    Bergmans, J.3    Marx, J.J.4
  • 4
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth E., Tuttle M.S., Powelson J., Vaughn M.B., Donovan A., Ward D.M., Ganz T., and Kaplan J. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306 (2004) 2090-2093
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.B.4    Donovan, A.5    Ward, D.M.6    Ganz, T.7    Kaplan, J.8
  • 6
    • 14544298717 scopus 로고    scopus 로고
    • Hepcidin-a regulator of intestinal iron absorption and iron recycling by macrophages
    • Ganz T. Hepcidin-a regulator of intestinal iron absorption and iron recycling by macrophages. Best. Pract. Res. Clin. Haematol. 18 (2005) 171-182
    • (2005) Best. Pract. Res. Clin. Haematol. , vol.18 , pp. 171-182
    • Ganz, T.1
  • 7
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • Nemeth E., Rivera S., Gabayan V., Keller C., Taudorf S., Pedersen B.K., and Ganz T. IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. J. Clin. Invest. 113 (2004) 1271-1276
    • (2004) J. Clin. Invest. , vol.113 , pp. 1271-1276
    • Nemeth, E.1    Rivera, S.2    Gabayan, V.3    Keller, C.4    Taudorf, S.5    Pedersen, B.K.6    Ganz, T.7
  • 9
    • 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. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 10289-10293
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 10289-10293
    • Truksa, J.1    Peng, H.2    Lee, P.3    Beutler, E.4
  • 11
    • 34447137331 scopus 로고    scopus 로고
    • Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance
    • Babitt J.L., Huang F.W., Xia Y., Sidis Y., Andrews N.C., and Lin H.Y. Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance. J. Clin. Invest. 117 (2007) 1933-1939
    • (2007) J. Clin. Invest. , vol.117 , pp. 1933-1939
    • Babitt, J.L.1    Huang, F.W.2    Xia, Y.3    Sidis, Y.4    Andrews, N.C.5    Lin, H.Y.6
  • 12
    • 34548825938 scopus 로고    scopus 로고
    • Iron transferrin regulates hepcidin synthesis in primary hepatocyte culture through hemojuvelin and BMP2/4
    • Lin L., Valore E.V., Nemeth E., Goodnough J.B., Gabayan V., and Ganz T. Iron transferrin regulates hepcidin synthesis in primary hepatocyte culture through hemojuvelin and BMP2/4. Blood 110 (2007) 2182-2189
    • (2007) Blood , vol.110 , pp. 2182-2189
    • Lin, L.1    Valore, E.V.2    Nemeth, E.3    Goodnough, J.B.4    Gabayan, V.5    Ganz, T.6
  • 13
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling from cell membrane to the nucleus
    • Shi Y., and Massague J. Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 113 (2003) 685-700
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 14
    • 23944502314 scopus 로고    scopus 로고
    • Time-course analysis of hepcidin, serum iron, and plasma cytokine levels in humans injected with LPS
    • Kemna E.H., Pickkers P., Nemeth E., van der Hoeven H., and Swinkels D. Time-course analysis of hepcidin, serum iron, and plasma cytokine levels in humans injected with LPS. Blood 106 (2005) 1864-1866
    • (2005) Blood , vol.106 , pp. 1864-1866
    • Kemna, E.H.1    Pickkers, P.2    Nemeth, E.3    van der Hoeven, H.4    Swinkels, D.5
  • 15
    • 33751175421 scopus 로고    scopus 로고
    • Interleukin-6 induces hepcidin expression through STAT3
    • Wrighting D.M., and Andrews N.C. Interleukin-6 induces hepcidin expression through STAT3. Blood 108 (2006) 3204-3209
    • (2006) Blood , vol.108 , pp. 3204-3209
    • Wrighting, D.M.1    Andrews, N.C.2
  • 18
    • 34548559118 scopus 로고    scopus 로고
    • Different regulatory elements are required for response of hepcidin to interleukin-6 and bone morphogenetic proteins 4 and 9
    • Truksa J., Peng H., Lee P., and Beutler E. Different regulatory elements are required for response of hepcidin to interleukin-6 and bone morphogenetic proteins 4 and 9. Br. J. Haematol. 139 (2007) 138-147
    • (2007) Br. J. Haematol. , vol.139 , pp. 138-147
    • Truksa, J.1    Peng, H.2    Lee, P.3    Beutler, E.4
  • 19
    • 36148955432 scopus 로고    scopus 로고
    • The distal location of the iron responsive region of the hepcidin promoter
    • Truksa J., Lee P., Peng H., Flanagan J., and Beutler E. The distal location of the iron responsive region of the hepcidin promoter. Blood 110 (2007) 3436-3437
    • (2007) Blood , vol.110 , pp. 3436-3437
    • Truksa, J.1    Lee, P.2    Peng, H.3    Flanagan, J.4    Beutler, E.5
  • 21
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • Park C.H., Valore E.V., Waring A.J., and Ganz T. Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J. Biol. Chem. 276 (2001) 7806-7810
    • (2001) J. Biol. Chem. , vol.276 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3    Ganz, T.4
  • 22
    • 30144432585 scopus 로고    scopus 로고
    • The N-terminus of hepcidin is essential for its interaction with ferroportin: structure-function study
    • Nemeth E., Preza G.C., Jung C.L., Kaplan J., Waring A.J., and Ganz T. The N-terminus of hepcidin is essential for its interaction with ferroportin: structure-function study. Blood 107 (2006) 328-333
    • (2006) Blood , vol.107 , pp. 328-333
    • Nemeth, E.1    Preza, G.C.2    Jung, C.L.3    Kaplan, J.4    Waring, A.J.5    Ganz, T.6
  • 24
    • 33747167627 scopus 로고    scopus 로고
    • Detection of serum hepcidin in renal failure and inflammation by using ProteinChip System
    • Tomosugi N., Kawabata H., Wakatabe R., Higuchi M., Yamaya H., Umehara H., and Ishikawa I. Detection of serum hepcidin in renal failure and inflammation by using ProteinChip System. Blood 108 (2006) 1381-1387
    • (2006) Blood , vol.108 , pp. 1381-1387
    • Tomosugi, N.1    Kawabata, H.2    Wakatabe, R.3    Higuchi, M.4    Yamaya, H.5    Umehara, H.6    Ishikawa, I.7
  • 25
    • 34547940326 scopus 로고    scopus 로고
    • Quantitation of hepcidin from human and mouse serum using liquid chromatography tandem mass spectrometry
    • Murphy A.T., Witcher D.R., Luan P., and Wroblewski V.J. Quantitation of hepcidin from human and mouse serum using liquid chromatography tandem mass spectrometry. Blood 110 (2007) 1048-1054
    • (2007) Blood , vol.110 , pp. 1048-1054
    • Murphy, A.T.1    Witcher, D.R.2    Luan, P.3    Wroblewski, V.J.4
  • 27
    • 34147197662 scopus 로고    scopus 로고
    • Mass spectrometry-based hepcidin measurements in serum and urine: analytical aspects and clinical implications
    • Kemna E.H., Tjalsma H., Podust V.N., and Swinkels D.W. Mass spectrometry-based hepcidin measurements in serum and urine: analytical aspects and clinical implications. Clin. Chem. 53 (2007) 620-628
    • (2007) Clin. Chem. , vol.53 , pp. 620-628
    • Kemna, E.H.1    Tjalsma, H.2    Podust, V.N.3    Swinkels, D.W.4
  • 30
    • 34250850987 scopus 로고    scopus 로고
    • The iron regulatory peptide hepcidin is expressed in the heart and regulated by hypoxia and inflammation
    • Merle U., Fein E., Gehrke S.G., Stremmel W., and Kulaksiz H. The iron regulatory peptide hepcidin is expressed in the heart and regulated by hypoxia and inflammation. Endocrinology 148 (2007) 2663-2668
    • (2007) Endocrinology , vol.148 , pp. 2663-2668
    • Merle, U.1    Fein, E.2    Gehrke, S.G.3    Stremmel, W.4    Kulaksiz, H.5
  • 33
    • 33646427702 scopus 로고    scopus 로고
    • TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens
    • Peyssonnaux C., Zinkernagel A.S., Datta V., Lauth X., Johnson R.S., and Nizet V. TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens. Blood 107 (2006) 3727-3732
    • (2006) Blood , vol.107 , pp. 3727-3732
    • Peyssonnaux, C.1    Zinkernagel, A.S.2    Datta, V.3    Lauth, X.4    Johnson, R.S.5    Nizet, V.6
  • 34
    • 36549034762 scopus 로고    scopus 로고
    • Posttranslational processing of hepcidin in human hepatocytes is mediated by the prohormone convertase furin
    • Valore E.V., and Ganz T. Posttranslational processing of hepcidin in human hepatocytes is mediated by the prohormone convertase furin. Blood Cells Mol. Dis. 40 (2008) 132-138
    • (2008) Blood Cells Mol. Dis. , vol.40 , pp. 132-138
    • Valore, E.V.1    Ganz, T.2
  • 37
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29 (2001) e45
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 40
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O., Brunak S., von Heijne G., and Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat. Protoc. 2 (2007) 953-971
    • (2007) Nat. Protoc. , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 41
    • 0842313260 scopus 로고    scopus 로고
    • Prediction of proprotein convertase cleavage sites
    • Duckert P., Brunak S., and Blom N. Prediction of proprotein convertase cleavage sites. Protein Eng. Des. Sel. 17 (2004) 107-112
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 107-112
    • Duckert, P.1    Brunak, S.2    Blom, N.3
  • 42
    • 0027270903 scopus 로고
    • The synthesis of inhibitors for processing proteinases and their action on the Kex2 proteinase of yeast
    • Angliker H., Wikstrom P., Shaw E., Brenner C., and Fuller R.S. The synthesis of inhibitors for processing proteinases and their action on the Kex2 proteinase of yeast. Biochem. J. 293 (1993) 75-81
    • (1993) Biochem. J. , vol.293 , pp. 75-81
    • Angliker, H.1    Wikstrom, P.2    Shaw, E.3    Brenner, C.4    Fuller, R.S.5
  • 43
    • 0030725756 scopus 로고    scopus 로고
    • Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins
    • Nakayama K. Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327 Pt 3 (1997) 625-635
    • (1997) Biochem. J. , vol.327 , Issue.PART 3 , pp. 625-635
    • Nakayama, K.1
  • 44
    • 0025989238 scopus 로고
    • Multiple targets for brefeldin A
    • Pelham H.R. Multiple targets for brefeldin A. Cell 67 (1991) 449-451
    • (1991) Cell , vol.67 , pp. 449-451
    • Pelham, H.R.1
  • 46
    • 33747406251 scopus 로고    scopus 로고
    • Iron absorption by healthy women is not associated with either serum or urinary prohepcidin
    • Hadley K.B., Johnson L.K., and Hunt J.R. Iron absorption by healthy women is not associated with either serum or urinary prohepcidin. Am. J. Clin. Nutr. 84 (2006) 150-155
    • (2006) Am. J. Clin. Nutr. , vol.84 , pp. 150-155
    • Hadley, K.B.1    Johnson, L.K.2    Hunt, J.R.3
  • 47
    • 34047261779 scopus 로고    scopus 로고
    • Serum prohepcidin concentration: no association with iron absorption in healthy men; and no relationship with iron status in men carrying HFE mutations, hereditary haemochromatosis patients undergoing phlebotomy treatment, or pregnant women
    • Roe M.A., Spinks C., Heath A.L., Harvey L.J., Foxall R., Wimperis J., Wolf C., and Fairweather-Tait S.J. Serum prohepcidin concentration: no association with iron absorption in healthy men; and no relationship with iron status in men carrying HFE mutations, hereditary haemochromatosis patients undergoing phlebotomy treatment, or pregnant women. Br. J. Nutr. 97 (2007) 544-549
    • (2007) Br. J. Nutr. , vol.97 , pp. 544-549
    • Roe, M.A.1    Spinks, C.2    Heath, A.L.3    Harvey, L.J.4    Foxall, R.5    Wimperis, J.6    Wolf, C.7    Fairweather-Tait, S.J.8
  • 50
    • 0034194815 scopus 로고    scopus 로고
    • Pathways for protein disulphide bond formation
    • Frand A.R., Cuozzo J.W., and Kaiser C.A. Pathways for protein disulphide bond formation. Trends Cell Biol. 10 (2000) 203-210
    • (2000) Trends Cell Biol. , vol.10 , pp. 203-210
    • Frand, A.R.1    Cuozzo, J.W.2    Kaiser, C.A.3
  • 51
    • 36549006459 scopus 로고    scopus 로고
    • Commentary to: "Post-translational processing of hepcidin in human hepatocytes is mediated by the prohormone convertase furin," by Erika Valore and Tomas Ganz
    • Lee P. Commentary to: "Post-translational processing of hepcidin in human hepatocytes is mediated by the prohormone convertase furin," by Erika Valore and Tomas Ganz. Blood Cells Mol. Dis. 40 (2008) 139-140
    • (2008) Blood Cells Mol. Dis. , vol.40 , pp. 139-140
    • Lee, P.1
  • 52
    • 21044450599 scopus 로고    scopus 로고
    • Prohepcidin localises to the Golgi compartment and secretory pathway in hepatocytes
    • Wallace D.F., Summerville L., Lusby P.E., and Subramaniam V.N. Prohepcidin localises to the Golgi compartment and secretory pathway in hepatocytes. J. Hepatol. 43 (2005) 720-728
    • (2005) J. Hepatol. , vol.43 , pp. 720-728
    • Wallace, D.F.1    Summerville, L.2    Lusby, P.E.3    Subramaniam, V.N.4
  • 53
    • 33746600246 scopus 로고    scopus 로고
    • Proprotein convertase furin is preferentially expressed in T helper 1 cells and regulates interferon gamma
    • Pesu M., Muul L., Kanno Y., and O'Shea J.J. Proprotein convertase furin is preferentially expressed in T helper 1 cells and regulates interferon gamma. Blood 108 (2006) 983-985
    • (2006) Blood , vol.108 , pp. 983-985
    • Pesu, M.1    Muul, L.2    Kanno, Y.3    O'Shea, J.J.4
  • 55
    • 0030612684 scopus 로고    scopus 로고
    • TGFbeta1 regulates gene expression of its own converting enzyme furin
    • Blanchette F., Day R., Dong W., Laprise M.H., and Dubois C.M. TGFbeta1 regulates gene expression of its own converting enzyme furin. J. Clin. Invest 99 (1997) 1974-1983
    • (1997) J. Clin. Invest , vol.99 , pp. 1974-1983
    • Blanchette, F.1    Day, R.2    Dong, W.3    Laprise, M.H.4    Dubois, C.M.5
  • 57
    • 43049132128 scopus 로고    scopus 로고
    • A bone morphogenetic protein (BMP)-responsive element in the hepcidin promoter controls HFE2-mediated hepatic hepcidin expression and its response to IL-6 in cultured cells
    • Verga Falzacappa M.V., Casanovas G., Hentze M.W., and Muckenthaler M.U. A bone morphogenetic protein (BMP)-responsive element in the hepcidin promoter controls HFE2-mediated hepatic hepcidin expression and its response to IL-6 in cultured cells. J. Mol. Med. 86 (2008) 531-540
    • (2008) J. Mol. Med. , vol.86 , pp. 531-540
    • Verga Falzacappa, M.V.1    Casanovas, G.2    Hentze, M.W.3    Muckenthaler, M.U.4


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