메뉴 건너뛰기




Volumn 36, Issue 2, 2010, Pages 88-97

Regulatory mechanisms of intestinal iron absorption - Uncovering of a fast-response mechanism based on DMT1 and ferroportin endocytosis

Author keywords

Antisense; Divalent metal transporter 1; Iron transport; Mucosal block

Indexed keywords

ERYTHROPOIETIN; FERROPORTIN; FERROPORTIN 1; GLUCOSE TRANSPORTER 4; HEPCIDIN; HEPHAESTIN; IRON; IRON REGULATORY PROTEIN 1; IRON REGULATORY PROTEIN 2; MESSENGER RNA; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2;

EID: 77951116454     PISSN: 09516433     EISSN: 18728081     Source Type: Journal    
DOI: 10.1002/biof.84     Document Type: Review
Times cited : (27)

References (87)
  • 4
    • 34147189116 scopus 로고    scopus 로고
    • Functional properties of multiple isoforms of human divalent metal-ion transporter 1 (DMT1)
    • DOI 10.1042/BJ20061290
    • Mackenzie, B., Takanaga, H., Hubert, N., Rolfs, A., and Hediger, M. A. (2007) Functional properties of multiple isoforms of human divalent metal-ion transporter 1 (DMT1). Biochem. J. 403, 59-69. (Pubitemid 46569867)
    • (2007) Biochemical Journal , vol.403 , Issue.1 , pp. 59-69
    • Mackenzie, B.1    Takanaga, H.2    Hubert, N.3    Rolfs, A.4    Hediger, M.A.5
  • 6
    • 3242780850 scopus 로고    scopus 로고
    • The role of labile iron pool in cardiovascular diseases
    • Kruszewski, M. (2004) The role of labile iron pool in cardiovascular diseases. Acta. Biochim. Pol. 51, 471-480.
    • (2004) Acta. Biochim. Pol. , vol.51 , pp. 471-480
    • Kruszewski, M.1
  • 7
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: Characterization, measurement, and participation in cellular processes(1)
    • Kakhlon, O. and Cabantchik, Z. I. (2002) The labile iron pool: characterization, measurement, and participation in cellular processes(1). Free Radic. Biol. Med. 33, 1037-1046.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 8
    • 0036249684 scopus 로고    scopus 로고
    • The chelatable iron pool in living cells: A methodically defined quantity
    • Petrat, F., de Groot, H., Sustmann, R., and Rauen, U. (2002) The chelatable iron pool in living cells: a methodically defined quantity. Biol. Chem. 383, 489-502.
    • (2002) Biol. Chem. , vol.383 , pp. 489-502
    • Petrat, F.1    De Groot, H.2    Sustmann, R.3    Rauen, U.4
  • 9
    • 0017762642 scopus 로고
    • Mucosal transferrin and ferritin factors in the regulation of iron absorption
    • El-Shobaki, F. A. and Rummel, W. (1977) Mucosal transferrin and ferritin factors in the regulation of iron absorption. Res. Exp. Med. (Berl) 171, 243-253.
    • (1977) Res. Exp. Med. (Berl) , vol.171 , pp. 243-253
    • El-Shobaki, F.A.1    Rummel, W.2
  • 10
    • 34047130786 scopus 로고    scopus 로고
    • Evidence for a sequential transfer of iron amongst ferritin, transferrin and transferrin receptor during duodenal absorption of iron in rat and human
    • Kolachala, V. L., Sesikeran, B., and Nair, K. M. (2007) Evidence for a sequential transfer of iron amongst ferritin, transferrin and transferrin receptor during duodenal absorption of iron in rat and human. World J. Gastroenterol. 13, 1042-1052.
    • (2007) World J. Gastroenterol. , vol.13 , pp. 1042-1052
    • Kolachala, V.L.1    Sesikeran, B.2    Nair, K.M.3
  • 12
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • Vulpe, C. D., Kuo, Y. M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., and Anderson, G. J. (1999) Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat. Genet. 21, 195-199.
    • (1999) Nat. Genet. , vol.21 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.M.2    Murphy, T.L.3    Cowley, L.4    Askwith, C.5    Libina, N.6    Gitschier, J.7    Anderson, G.J.8
  • 13
    • 27744522979 scopus 로고    scopus 로고
    • Recombinant expression and functional characterization of human hephaestin: A multicopper oxidase with ferroxidase activity
    • Griffiths, T. A., Mauk, A. G., and MacGillivray, R. T. (2005) Recombinant expression and functional characterization of human hephaestin: a multicopper oxidase with ferroxidase activity. Biochemistry 44, 14725-14731.
    • (2005) Biochemistry , vol.44 , pp. 14725-14731
    • Griffiths, T.A.1    Mauk, A.G.2    MacGillivray, R.T.3
  • 14
    • 20444416123 scopus 로고    scopus 로고
    • The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
    • DOI 10.1016/j.cmet.2005.01.003, PII S1550413105000306
    • Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., and Andrews, N. C. (2005) The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis. Cell Metab. 1, 191-200. (Pubitemid 43960600)
    • (2005) Cell Metabolism , vol.1 , Issue.3 , pp. 191-200
    • Donovan, A.1    Lima, C.A.2    Pinkus, J.L.3    Pinkus, G.S.4    Zon, L.I.5    Robine, S.6    Andrews, N.C.7
  • 15
    • 0036230638 scopus 로고    scopus 로고
    • Analysis of the human hephaestin gene and protein: Comparative modelling of the N-terminus ecto-domain based upon ceruloplasmin
    • Syed, B. A., Beaumont, N. J., Patel, A., Naylor, C. E., Bayele, H. K., Joannou, C. L., Rowe, P. S., Evans, R. W., and Srai, S. K. (2002) Analysis of the human hephaestin gene and protein: comparative modelling of the N-terminus ecto-domain based upon ceruloplasmin. Protein Eng. 15, 205-214. (Pubitemid 34429231)
    • (2002) Protein Engineering , vol.15 , Issue.3 , pp. 205-214
    • Syed, B.A.1    Beaumont, N.J.2    Patel, A.3    Naylor, C.E.4    Bayele, H.K.5    Joannou, C.L.6    Rowe, P.S.N.7    Evans, R.W.8    Srai, S.K.S.9
  • 16
    • 50949102412 scopus 로고    scopus 로고
    • Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
    • Muckenthaler, M. U., Galy, B., and Hentze, M. W. (2008) Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network. Annu. Rev. Nutr. 28, 197-213.
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 197-213
    • Muckenthaler, M.U.1    Galy, B.2    Hentze, M.W.3
  • 17
    • 0030870020 scopus 로고    scopus 로고
    • Intracellular iron regulates iron absorption and IRP activity in intestinal epithelial (Caco-2) cells
    • Arredondo, M., Orellana, A., Garate, M. A., and Núñez, M. T. (1997) Intracellular iron regulates iron absorption and IRP activity in intestinal epithelial (Caco-2) cells. Am. J. Physiol. 273, G275-G280.
    • (1997) Am. J. Physiol. , vol.273
    • Arredondo, M.1    Orellana, A.2    Garate, M.A.3    Núñez, M.T.4
  • 18
    • 0033106390 scopus 로고    scopus 로고
    • Iron regulatory protein as an endogenous sensor of iron in rat intestinal mucosa. Possible implications for the regulation of iron absorption
    • Schumann, K., Moret, R., Kunzle, H., and Kuhn, L. C. (1999) Iron regulatory protein as an endogenous sensor of iron in rat intestinal mucosa. Possible implications for the regulation of iron absorption. Eur. J. Biochem. 260, 362-372.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 362-372
    • Schumann, K.1    Moret, R.2    Kunzle, H.3    Kuhn, L.C.4
  • 19
    • 0343986454 scopus 로고    scopus 로고
    • Overexpression of the ferritin iron-responsive element decreases the labile iron pool and abolishes the regulation of iron absorption by intestinal epithelial (Caco-2) cells
    • Garate, M. A. and Núñez, M. T. (2000) Overexpression of the ferritin iron-responsive element decreases the labile iron pool and abolishes the regulation of iron absorption by intestinal epithelial (Caco-2) cells. J. Biol. Chem. 275, 1651-1655.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1651-1655
    • Garate, M.A.1    Núñez, M.T.2
  • 21
    • 2142717374 scopus 로고    scopus 로고
    • Rat duodenal IRP1 activity and iron absorption in iron deficiency and after HO perfusion
    • Schumann, K., Brennan, K., Weiss, M., Pantopoulos, K., and Hentze, M. W. (2004) Rat duodenal IRP1 activity and iron absorption in iron deficiency and after HO perfusion. Eur. J. Clin. Invest. 34, 275-282.
    • (2004) Eur. J. Clin. Invest. , vol.34 , pp. 275-282
    • Schumann, K.1    Brennan, K.2    Weiss, M.3    Pantopoulos, K.4    Hentze, M.W.5
  • 22
    • 35148886724 scopus 로고    scopus 로고
    • The relevance of the intestinal crypt and enterocyte in regulating iron absorption
    • Oates, P. S. (2007) The relevance of the intestinal crypt and enterocyte in regulating iron absorption. Pflugers Arch. 455, 201-213.
    • (2007) Pflugers Arch. , vol.455 , pp. 201-213
    • Oates, P.S.1
  • 23
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome
    • Guo, B., Phillips, J. D., Yu, Y., and Leibold, E. A. (1995) Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome. J. Biol. Chem. 270, 21645-21651.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 24
    • 33746864096 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron homeostasis by iron regulatory proteins
    • Wallander, M. L., Leibold, E. A., and Eisenstein, R. S. (2006) Molecular control of vertebrate iron homeostasis by iron regulatory proteins. Biochim. Biophys. Acta. 1763, 668-689.
    • (2006) Biochim. Biophys. Acta. , vol.1763 , pp. 668-689
    • Wallander, M.L.1    Leibold, E.A.2    Eisenstein, R.S.3
  • 25
    • 0037126002 scopus 로고    scopus 로고
    • Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: Implications for regulation and cellular function
    • Hubert, N. and Hentze, M. W. (2002) Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function. Proc. Natl. Acad. Sci. USA 99, 12345-12350.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12345-12350
    • Hubert, N.1    Hentze, M.W.2
  • 26
    • 37449009448 scopus 로고    scopus 로고
    • Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum
    • Galy, B., Ferring-Appel, D., Kaden, S., Grone, H. J., and Hentze, M. W. (2008) Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum. Cell. Metab. 7, 79-85.
    • (2008) Cell. Metab. , vol.7 , pp. 79-85
    • Galy, B.1    Ferring-Appel, D.2    Kaden, S.3    Grone, H.J.4    Hentze, M.W.5
  • 27
    • 0035049419 scopus 로고    scopus 로고
    • Expression of the duodenal iron transporters divalent-metal transporter 1 and ferroportin 1 in iron deficiency and iron overload
    • Zoller, H., Koch, R. O., Theurl, I., Obrist, P., Pietrangelo, A., Montosi, G., Haile, D. J., Vogel, W., and Weiss, G. (2001) Expression of the duodenal iron transporters divalent-metal transporter 1 and ferroportin 1 in iron deficiency and iron overload. Gastroenterology 120, 1412-1419. (Pubitemid 32322315)
    • (2001) Gastroenterology , vol.120 , Issue.6 , pp. 1412-1419
    • Zoller, H.1    Koch, R.O.2    Theurl, I.3    Obrist, P.4    Pietrangelo, A.5    Montosi, G.6    Haile, D.J.7    Vogel, W.8    Weiss, G.9
  • 28
    • 0142126132 scopus 로고    scopus 로고
    • Mechanisms of iron mediated regulation of the duodenal iron transporters divalent metal transporter 1 and ferroportin 1
    • Zoller, H., Theurl, I., Koch, R., Kaser, A., and Weiss, G. (2002) Mechanisms of iron mediated regulation of the duodenal iron transporters divalent metal transporter 1 and ferroportin 1. Blood Cells Mol. Dis. 29, 488-497.
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 488-497
    • Zoller, H.1    Theurl, I.2    Koch, R.3    Kaser, A.4    Weiss, G.5
  • 30
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud, S. and Haile, D. J. (2000) A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 275, 19906-19912.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 31
    • 65349126484 scopus 로고    scopus 로고
    • A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression
    • Zhang, D. L., Hughes, R. M., Ollivierre-Wilson, H., Ghosh, M. C., and Rouault, T. A. (2009) A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression. Cell Metab. 9, 461-473.
    • (2009) Cell Metab. , vol.9 , pp. 461-473
    • Zhang, D.L.1    Hughes, R.M.2    Ollivierre-Wilson, H.3    Ghosh, M.C.4    Rouault, T.A.5
  • 33
    • 33847660940 scopus 로고    scopus 로고
    • Expression of the 1B isoforms of divalent metal transporter (DMT1) is regulated by interaction of NF-Y with a CCAAT-box element near the transcription start site
    • Paradkar, P. N. and Roth, J. A. (2007) Expression of the 1B isoforms of divalent metal transporter (DMT1) is regulated by interaction of NF-Y with a CCAAT-box element near the transcription start site. J. Cell Physiol. 211, 183-188.
    • (2007) J. Cell Physiol. , vol.211 , pp. 183-188
    • Paradkar, P.N.1    Roth, J.A.2
  • 35
    • 58749094789 scopus 로고    scopus 로고
    • Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency
    • Shah, Y. M., Matsubara, T., Ito, S., Yim, S. H., and Gonzalez, F. J. (2009) Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency. Cell Metab. 9, 152-164.
    • (2009) Cell Metab. , vol.9 , pp. 152-164
    • Shah, Y.M.1    Matsubara, T.2    Ito, S.3    Yim, S.H.4    Gonzalez, F.J.5
  • 36
    • 41649110613 scopus 로고    scopus 로고
    • Sequential regulation of ferroportin expression after erythrophagocytosis in murine macrophages: Early mRNA induction by haem, followed by iron-dependent protein expression
    • DOI 10.1042/BJ20071474
    • Delaby, C., Pilard, N., Puy, H., and Canonne-Hergaux, F. (2008) Sequential regulation of ferroportin expression after erythrophagocytosis in murine macrophages: early mRNA induction by haem, followed by iron-dependent protein expression. Biochem. J. 411, 123-131. (Pubitemid 351482354)
    • (2008) Biochemical Journal , vol.411 , Issue.1 , pp. 123-131
    • Delaby, C.1    Pilard, N.2    Puy, H.3    Canonne-Hergaux, F.4
  • 37
    • 62749098683 scopus 로고    scopus 로고
    • Iron loading increases ferroportin heterogeneous nuclear RNA and mRNA levels in murine J774 macrophages
    • Aydemir, F., Jenkitkasemwong, S., Gulec, S., and Knutson, M. D. (2009) Iron loading increases ferroportin heterogeneous nuclear RNA and mRNA levels in murine J774 macrophages. J. Nutr. 139, 434-438.
    • (2009) J. Nutr. , vol.139 , pp. 434-438
    • Aydemir, F.1    Jenkitkasemwong, S.2    Gulec, S.3    Knutson, M.D.4
  • 38
    • 0345688910 scopus 로고    scopus 로고
    • Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages
    • Knutson, M. D., Vafa, M. R., Haile, D. J., and Wessling-Resnick, M. (2003) Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages. Blood 102, 4191-4197.
    • (2003) Blood , vol.102 , pp. 4191-4197
    • Knutson, M.D.1    Vafa, M.R.2    Haile, D.J.3    Wessling-Resnick, M.4
  • 39
    • 0036838570 scopus 로고    scopus 로고
    • Duodenal mRNA expression of iron related genes in response to iron loading and iron deficiency in four strains of mice
    • DOI 10.1136/gut.51.5.648
    • Dupic, F., Fruchon, S., Bensaid, M., Loreal, O., Brissot, P., Borot, N., Roth, M. P., and Coppin, H. (2002) Duodenal mRNA expression of iron related genes in response to iron loading and iron deficiency in four strains of mice. Gut 51, 648-653. (Pubitemid 35216850)
    • (2002) Gut , vol.51 , Issue.5 , pp. 648-653
    • Dupic, F.1    Fruchon, S.2    Bensaid, M.3    Loreal, O.4    Brissot, P.5    Borot, N.6    Roth, M.P.7    Coppin, H.8
  • 42
    • 0028049495 scopus 로고
    • Regulators of iron balance in humans
    • Finch, C. (1994) Regulators of iron balance in humans. Blood 84, 1697-1702.
    • (1994) Blood , vol.84 , pp. 1697-1702
    • Finch, C.1
  • 44
    • 33750133047 scopus 로고    scopus 로고
    • Regulation of iron metabolism by hepcidin
    • Nemeth, E. and Ganz, T. (2006) Regulation of iron metabolism by hepcidin. Annu. Rev. Nutr. 26, 323-342.
    • (2006) Annu. Rev. Nutr. , vol.26 , pp. 323-342
    • Nemeth, E.1    Ganz, T.2
  • 45
    • 33644862202 scopus 로고    scopus 로고
    • Iron imports. IV. Hepcidin and regulation of body iron metabolism
    • Ganz, T. and Nemeth, E. (2006) Iron imports. IV. Hepcidin and regulation of body iron metabolism. Am. J. Physiol. Gastrointest. Liver Physiol. 290, G199-G203.
    • (2006) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.290
    • Ganz, T.1    Nemeth, E.2
  • 48
    • 39649097642 scopus 로고    scopus 로고
    • Evidence for differential effects of hepcidin in macrophages and intestinal epithelial cells
    • DOI 10.1136/gut.2007.131722
    • Chaston, T., Chung, B., Mascarenhas, M., Marks, J., Patel, B., Srai, S. K., and Sharp, P. (2008) Evidence for differential effects of hepcidin in macrophages and intestinal epithelial cells. Gut 57, 374-382. (Pubitemid 351288105)
    • (2008) Gut , vol.57 , Issue.3 , pp. 374-382
    • Chaston, T.1    Chung, B.2    Mascarenhas, M.3    Marks, J.4    Patel, B.5    Srai, S.K.6    Sharp, P.7
  • 49
    • 67749109895 scopus 로고    scopus 로고
    • Hepcidin decreases iron transporter expression in vivo in mouse duodenum and spleen and in vitro in THP-1 macrophages and intestinal Caco-2 cells
    • Chung, B., Chaston, T., Marks, J., Srai, S. K., and Sharp, P. A. (2009) Hepcidin decreases iron transporter expression in vivo in mouse duodenum and spleen and in vitro in THP-1 macrophages and intestinal Caco-2 cells. J. Nutr. 139, 1457-1462.
    • (2009) J. Nutr. , vol.139 , pp. 1457-1462
    • Chung, B.1    Chaston, T.2    Marks, J.3    Srai, S.K.4    Sharp, P.A.5
  • 50
    • 40449129401 scopus 로고    scopus 로고
    • Effect of erythropoietin on hepcidin, DMT1 with IRE, and hephaestin gene expression in duodenum of rats
    • Kong, W. N., Chang, Y. Z., Wang, S. M., Zhai, X. L., Shang, J. X., Li, L. X., and Duan, X. L. (2008) Effect of erythropoietin on hepcidin, DMT1 with IRE, and hephaestin gene expression in duodenum of rats. J. Gastroenterol. 43, 136-143.
    • (2008) J. Gastroenterol. , vol.43 , pp. 136-143
    • Kong, W.N.1    Chang, Y.Z.2    Wang, S.M.3    Zhai, X.L.4    Shang, J.X.5    Li, L.X.6    Duan, X.L.7
  • 51
    • 28444488323 scopus 로고    scopus 로고
    • Presence of the iron exporter ferroportin at the plasma membrane of macrophages is enhanced by iron loading and down-regulated by hepcidin
    • DOI 10.1182/blood-2005-06-2398
    • Delaby, C., Pilard, N., Goncalves, A. S., Beaumont, C., and Canonne-Hergaux, F. (2005) Presence of the iron exporter ferroportin at the plasma membrane of macrophages is enhanced by iron loading and down-regulated by hepcidin. Blood 106, 3979-3984. (Pubitemid 41739041)
    • (2005) Blood , vol.106 , Issue.12 , pp. 3979-3984
    • Delaby, C.1    Pilard, N.2    Goncalves, A.S.3    Beaumont, C.4    Canonne-Hergaux, F.5
  • 52
    • 4644301624 scopus 로고    scopus 로고
    • Delayed hepcidin response explains the lag period in iron absorption following a stimulus to increase erythropoiesis
    • Frazer, D. M., Inglis, H. R., Wilkins, S. J., Millard, K. N., Steele, T. M., McLaren, G. D., McKie, A. T., Vulpe, C. D., and Anderson, G. J. (2004) Delayed hepcidin response explains the lag period in iron absorption following a stimulus to increase erythropoiesis. Gut 53, 1509-1515.
    • (2004) Gut , vol.53 , pp. 1509-1515
    • Frazer, D.M.1    Inglis, H.R.2    Wilkins, S.J.3    Millard, K.N.4    Steele, T.M.5    McLaren, G.D.6    McKie, A.T.7    Vulpe, C.D.8    Anderson, G.J.9
  • 53
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • DOI 10.1126/science.1104742
    • Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., and Kaplan, J. (2004) Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306, 2090-2093. (Pubitemid 40007660)
    • (2004) Science , vol.306 , Issue.5704 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.D.4    Donovan, A.5    Ward, D.M.6    Ganz, T.7    Kaplan, J.8
  • 56
    • 0025343574 scopus 로고
    • Erythropoietin retards DNA breakdown and prevents programmed death in erythroid progenitor cells
    • Koury, M. J. and Bondurant, M. C. (1990) Erythropoietin retards DNA breakdown and prevents programmed death in erythroid progenitor cells. Science 248, 378-381. (Pubitemid 20150851)
    • (1990) Science , vol.248 , Issue.4953 , pp. 378-381
    • Koury, M.J.1    Bondurant, M.C.2
  • 59
    • 34347389655 scopus 로고    scopus 로고
    • Iron homeostasis during transfusional iron overload in beta-thalassemia and sickle cell disease: Changes in iron regulatory protein, hepcidin, and ferritin expression
    • Jenkins, Z. A., Hagar, W., Bowlus, C. L., Johansson, H. E., Harmatz, P., Vichinsky, E. P., and Theil, E. C. (2007) Iron homeostasis during transfusional iron overload in beta-thalassemia and sickle cell disease: changes in iron regulatory protein, hepcidin, and ferritin expression. Pediatr. Hematol. Oncol. 24, 237-243.
    • (2007) Pediatr. Hematol. Oncol. , vol.24 , pp. 237-243
    • Jenkins, Z.A.1    Hagar, W.2    Bowlus, C.L.3    Johansson, H.E.4    Harmatz, P.5    Vichinsky, E.P.6    Theil, E.C.7
  • 61
    • 70450212841 scopus 로고    scopus 로고
    • Anemia of chronic disease (anemia of inflammation)
    • Agarwal, N. and Prchal, J. T. (2009) Anemia of chronic disease (anemia of inflammation). Acta. Haematol. 122, 103-108.
    • (2009) Acta. Haematol. , vol.122 , pp. 103-108
    • Agarwal, N.1    Prchal, J.T.2
  • 62
    • 0037372606 scopus 로고    scopus 로고
    • A rapid decrease in the expression of DMT1 and Dcytb but not Ireg1 or hephaestin explains the mucosal block phenomenon of iron absorption
    • Frazer, D. M., Wilkins, S. J., Becker, E. M., Murphy, T. L., Vulpe, C. D., McKie, A. T., and Anderson, G. J. (2003) A rapid decrease in the expression of DMT1 and Dcytb but not Ireg1 or hephaestin explains the mucosal block phenomenon of iron absorption. Gut 52, 340-346.
    • (2003) Gut , vol.52 , pp. 340-346
    • Frazer, D.M.1    Wilkins, S.J.2    Becker, E.M.3    Murphy, T.L.4    Vulpe, C.D.5    McKie, A.T.6    Anderson, G.J.7
  • 63
    • 0023132037 scopus 로고
    • Blocking of iron absorption by a preliminary oral dose of iron
    • O'Neil-Cutting, M. A. and Crosby, W. H. (1987) Blocking of iron absorption by a preliminary oral dose of iron. Arch. Intern. Med. 147, 489-491.
    • (1987) Arch. Intern. Med. , vol.147 , pp. 489-491
    • O'Neil-Cutting, M.A.1    Crosby, W.H.2
  • 64
    • 0008089888 scopus 로고
    • Absorption of inorganic iron from graded doses: Its significance in relation to iron absorption tests and mucosal block theory
    • Smith, M. D. and Pannacciulli, I. M. (1958) Absorption of inorganic iron from graded doses: its significance in relation to iron absorption tests and mucosal block theory. Br. J. Haematol. 4, 428-434.
    • (1958) Br. J. Haematol. , vol.4 , pp. 428-434
    • Smith, M.D.1    Pannacciulli, I.M.2
  • 65
    • 0001592844 scopus 로고
    • Radioiron absorption in anemic dogs; fluctuations in the mucosal block and evidence for a gradient of absorption in the gastrointestinal tract
    • Stewart, W. B., Yuile, C. L., Claiborne, H. A., Snowman, R. T., and Whipple, G. H. (1950) Radioiron absorption in anemic dogs; fluctuations in the mucosal block and evidence for a gradient of absorption in the gastrointestinal tract. J. Exp. Med. 92, 375-382.
    • (1950) J. Exp. Med. , vol.92 , pp. 375-382
    • Stewart, W.B.1    Yuile, C.L.2    Claiborne, H.A.3    Snowman, R.T.4    Whipple, G.H.5
  • 66
    • 0013955042 scopus 로고
    • Mucosal block. An evaluation of concepts relating to control of iron absorption
    • Crosby, W. H. (1966) Mucosal block. An evaluation of concepts relating to control of iron absorption. Semin. Hematol. 3, 299-313.
    • (1966) Semin. Hematol. , vol.3 , pp. 299-313
    • Crosby, W.H.1
  • 70
    • 28544450844 scopus 로고    scopus 로고
    • Glucose transporter 4: Cycling, compartments and controversies
    • Dugani, C. B. and Klip, A. (2005) Glucose transporter 4: cycling, compartments and controversies. EMBO Rep. 6, 1137-1142.
    • (2005) EMBO Rep. , vol.6 , pp. 1137-1142
    • Dugani, C.B.1    Klip, A.2
  • 71
    • 33748568155 scopus 로고    scopus 로고
    • Regulation of aquaporin-2 trafficking and its binding protein complex
    • Noda, Y. and Sasaki, S. (2006) Regulation of aquaporin-2 trafficking and its binding protein complex. Biochim. Biophys. Acta. 1758, 1117-1125.
    • (2006) Biochim. Biophys. Acta. , vol.1758 , pp. 1117-1125
    • Noda, Y.1    Sasaki, S.2
  • 72
    • 34447098373 scopus 로고    scopus 로고
    • Intracellular trafficking of TRP channels
    • Cayouette, S. and Boulay, G. (2007) Intracellular trafficking of TRP channels. Cell Calcium 42, 225-232.
    • (2007) Cell Calcium , vol.42 , pp. 225-232
    • Cayouette, S.1    Boulay, G.2
  • 73
    • 38149016966 scopus 로고    scopus 로고
    • The cell biology of synaptic plasticity: AMPA receptor trafficking
    • Shepherd, J. D. and Huganir, R. L. (2007) The cell biology of synaptic plasticity: AMPA receptor trafficking. Annu. Rev. Cell Dev. Biol. 23, 613-643.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 613-643
    • Shepherd, J.D.1    Huganir, R.L.2
  • 74
    • 34547943623 scopus 로고    scopus 로고
    • Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking
    • Hou, J. C. and Pessin, J. E. (2007) Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking. Curr. Opin. Cell Biol. 19, 466-473.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 466-473
    • Hou, J.C.1    Pessin, J.E.2
  • 75
    • 0036906608 scopus 로고    scopus 로고
    • Alternative splicing regulates the subcellular localization of divalent metal transporter 1 isoforms
    • Tabuchi, M., Tanaka, N., Nishida-Kitayama, J., Ohno, H. and Kishi, F. (2002) Alternative splicing regulates the subcellular localization of divalent metal transporter 1 isoforms. Mol. Biol. Cell. 13, 4371-4387.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 4371-4387
    • Tabuchi, M.1    Tanaka, N.2    Nishida-Kitayama, J.3    Ohno, H.4    Kishi, F.5
  • 76
    • 33144468560 scopus 로고    scopus 로고
    • Distinct targeting and recycling properties of two isoforms of the iron transporter DMT1 (NRAMP2, Slc11A2)
    • DOI 10.1021/bi052307m
    • Lam-Yuk-Tseung, S. and Gros, P. (2006) Distinct targeting and recycling properties of two isoforms of the iron transporter DMT1 (NRAMP2, Slc11A2). Biochemistry 45, 2294-2301. (Pubitemid 43271329)
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2294-2301
    • Lam-Yuk-Tseung, S.1    Gros, P.2
  • 77
    • 24644489085 scopus 로고    scopus 로고
    • Carboxyl-terminus determinants of the iron transporter DMT1/SLC11A2 isoform II (-IRE/1B) mediate internalization from the plasma membrane into recycling endosomes
    • DOI 10.1021/bi050911r
    • Lam-Yuk-Tseung, S., Touret, N., Grinstein, S., and Gros, P. (2005) Carboxyl- terminus determinants of the iron transporter DMT1/SLC11A2 isoform II (-IRE/1B) mediate internalization from the plasma membrane into recycling endosomes. Biochemistry 44, 12149-12159. (Pubitemid 41285713)
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 12149-12159
    • Lam-Yuk-Tseung, S.1    Touret, N.2    Grinstein, S.3    Gros, P.4
  • 78
    • 77749264614 scopus 로고    scopus 로고
    • Iron supply determines apical/basolateral membrane distribution of intestinal iron transporters DMT1 and ferroportin 1
    • Núñez, M. T., Tapia, V., Rojas, A., Aguirre, P., Gómez, F., and Nualart, F. (2010) Iron supply determines apical/basolateral membrane distribution of intestinal iron transporters DMT1 and ferroportin 1. Am. J. Physiol. Cell Physiol., 298, C477-485.
    • (2010) Am. J. Physiol. Cell Physiol. , vol.298
    • Núñez, M.T.1    Tapia, V.2    Rojas, A.3    Aguirre, P.4    Gómez, F.5    Nualart, F.6
  • 79
    • 0346461664 scopus 로고    scopus 로고
    • Ferroportin/IREG-1/MTP-1/SLC40A1 modulates the uptake of iron at the apical membrane of enterocytes
    • DOI 10.1136/gut.53.1.44
    • Thomas, C. and Oates, P. S. (2004) Ferroportin/IREG-1/MTP-1/SLC40A1 modulates the uptake of iron at the apical membrane of enterocytes. Gut 53, 44-49. (Pubitemid 38083009)
    • (2004) Gut , vol.53 , Issue.1 , pp. 44-49
    • Thomas, C.1    Oates, P.S.2
  • 80
    • 33745984180 scopus 로고    scopus 로고
    • Apical distribution of HFE-β2-microglobulin is associated with inhibition of apical iron uptake in intestinal epithelia cells
    • DOI 10.1007/s10534-005-6687-x
    • Arredondo, M., Tapia, V., Rojas, A., Aguirre, P., Reyes, F., Marzolo, M. P., and Núñez, M. T. (2006) Apical distribution of HFE-beta2-microglobulin is associated with inhibition of apical iron uptake in intestinal epithelia cells. Biometals 19, 379-388. (Pubitemid 44066275)
    • (2006) BioMetals , vol.19 , Issue.4 , pp. 379-388
    • Arredondo, M.1    Tapia, V.2    Rojas, A.3    Aguirre, P.4    Reyes, F.5    Marzolo, M.P.6    Nunez, M.T.7
  • 81
    • 0035344458 scopus 로고    scopus 로고
    • HFE inhibits apical iron uptake by intestinal epithelial (Caco-2) cells
    • Arredondo, M., Muñoz, P., Mura, C. V., and Núñez, M. T. (2001) HFE inhibits apical iron uptake by intestinal epithelial (Caco-2) cells. Faseb J. 15, 1276-1278.
    • (2001) Faseb J. , vol.15 , pp. 1276-1278
    • Arredondo, M.1    Muñoz, P.2    Mura, C.V.3    Núñez, M.T.4
  • 82
    • 0029024637 scopus 로고
    • Membrane protein trafficking through the common apical endosome compartment of polarized Caco-2 cells
    • Knight, A., Hughson, E., Hopkins, C. R., and Cutler, D. F. (1995) Membrane protein trafficking through the common apical endosome compartment of polarized Caco-2 cells. Mol. Biol. Cell 6, 597-610.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 597-610
    • Knight, A.1    Hughson, E.2    Hopkins, C.R.3    Cutler, D.F.4
  • 84
    • 0025173762 scopus 로고
    • Endocytic pathways in polarized Caco-2 cells: Identification of an endosomal compartment accessible from both apical and basolateral surfaces
    • Hughson, E. J. and Hopkins, C. R. (1990) Endocytic pathways in polarized Caco-2 cells: identification of an endosomal compartment accessible from both apical and basolateral surfaces. J. Cell. Biol. 110, 337-348.
    • (1990) J. Cell. Biol. , vol.110 , pp. 337-348
    • Hughson, E.J.1    Hopkins, C.R.2
  • 85
    • 58249101179 scopus 로고    scopus 로고
    • Iron feeding induces ferroportin 1 and hephaestin migration and interaction in rat duodenal epithelium
    • Yeh, K. Y., Yeh, M., Mims, L., and Glass, J. (2009) Iron feeding induces ferroportin 1 and hephaestin migration and interaction in rat duodenal epithelium. Am. J. Physiol. Gastrointest. Liver Physiol. 296, G55-G65.
    • (2009) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.296
    • Yeh, K.Y.1    Yeh, M.2    Mims, L.3    Glass, J.4
  • 86
    • 0036727925 scopus 로고    scopus 로고
    • Hepcidin expression inversely correlates with the expression of duodenal iron transporters and iron absorption in rats
    • DOI 10.1053/gast.2002.35353
    • Frazer, D. M., Wilkins, S. J., Becker, E. M., Vulpe, C. D., McKie, A. T., Trinder, D., and Anderson, G. J. (2002) Hepcidin expression inversely correlates with the expression of duodenal iron transporters and iron absorption in rats. Gastroenterology 123, 835-844. (Pubitemid 34977090)
    • (2002) Gastroenterology , vol.123 , Issue.3 , pp. 835-844
    • Frazer, D.M.1    Wilkins, S.J.2    Becker, E.M.3    Vulpe, C.D.4    Mckie, A.T.5    Trinder, D.6    Anderson, G.J.7
  • 87
    • 1342322891 scopus 로고    scopus 로고
    • Hepcidin regulation of ferroportin 1 expression in the liver and intestine of the rat
    • Yeh, K. Y., Yeh, M., and Glass, J. (2004) Hepcidin regulation of ferroportin 1 expression in the liver and intestine of the rat. Am. J. Physiol. Gastrointest. Liver Physiol. 286, G385-G394.
    • (2004) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.286
    • Yeh, K.Y.1    Yeh, M.2    Glass, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.