메뉴 건너뛰기




Volumn 27, Issue 1, 2013, Pages 288-298

Ferritin is the key to dietary iron absorption and tissue iron detoxification in Drosophila melanogaster

Author keywords

Iron export; Midgut; Secretory ferritin

Indexed keywords

ACONITATE HYDRATASE; FERRITIN; IRON; MESSENGER RNA;

EID: 84871860130     PISSN: None     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.12-213595     Document Type: Article
Times cited : (82)

References (43)
  • 1
    • 14544268521 scopus 로고    scopus 로고
    • Molecular control of iron metabolism
    • Andrews, N. (2005) Molecular control of iron metabolism. Best Pract. Res. Clin. Haematol. 18, 159-169
    • (2005) Best Pract. Res. Clin. Haematol. , vol.18 , pp. 159-169
    • Andrews, N.1
  • 3
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: A family of molecules for iron storage, antioxidation and more
    • Arosio, P., Ingrassia, R., and Cavadini, P. (2009) Ferritins: a family of molecules for iron storage, antioxidation and more. Biochim. Biophys. Acta Gen. Sub. 1790, 589-599
    • (2009) Biochim. Biophys. Acta Gen. Sub. , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 4
    • 0025637618 scopus 로고
    • The localization of ferritin in insects
    • Nichol, H., and Locke, M. (1990) The localization of ferritin in insects. Tissue Cell 22, 767-777
    • (1990) Tissue Cell , vol.22 , pp. 767-777
    • Nichol, H.1    Locke, M.2
  • 7
    • 0017644189 scopus 로고
    • Characterization of serum ferritin in iron overload: possible identity to natural apoferritin
    • Arosio, P., Yokota, M., and Drysdale, J. W. (1977) Characterization of serum ferritin in iron overload: possible identity to natural apoferritin. Br. J. Haematol. 36, 199-207 (Pubitemid 8110644)
    • (1977) British Journal of Haematology , vol.36 , Issue.2 , pp. 199-207
    • Arosio, P.1    Yokota, M.2    Drysdale, J.W.3
  • 10
    • 35048859798 scopus 로고    scopus 로고
    • Homeostatic mechanisms for iron storage revealed by genetic manipulations and live imaging of Drosophila ferritin
    • DOI 10.1534/genetics.107.075150
    • Missirlis, F., Kosmidis, S., Brody, T., Mavrakis, M., Holmberg, S., Odenwald, W. F., Skoulakis, E. M., and Rouault, T. A. (2007) Homeostatic mechanisms for iron storage revealed by genetic manipulations and live imaging of Drosophila ferritin. Genetics 177, 89-100 (Pubitemid 47555833)
    • (2007) Genetics , vol.177 , Issue.1 , pp. 89-100
    • Missirlis, F.1    Kosmidis, S.2    Brody, T.3    Mavrakis, M.4    Holmberg, S.5    Odenwald, W.F.6    Skoulakis, E.M.C.7    Rouault, T.A.8
  • 11
    • 77957550503 scopus 로고    scopus 로고
    • Identification of iron-loaded ferritin as an essential mitogen for cell proliferation and postembryonic development in Drosophila
    • Li, S. (2010) Identification of iron-loaded ferritin as an essential mitogen for cell proliferation and postembryonic development in Drosophila. Cell Res. 20, 1148-1157
    • (2010) Cell Res. , vol.20 , pp. 1148-1157
    • Li, S.1
  • 13
    • 0023898498 scopus 로고
    • Characteristics and expression of binding sites specific for ferritin H-chain on human cell lines
    • Fargion, S., Arosio, P., Fracanzani, A. L., Cislaghi, V., Levi, S., Cozzi, A., Piperno, A., and Fiorelli, G. (1988) Characteristics and expression of binding sites specific for ferritin H-chain on human cell lines. Blood 71, 753-757
    • (1988) Blood , vol.71 , pp. 753-757
    • Fargion, S.1    Arosio, P.2    Fracanzani, A.L.3    Cislaghi, V.4    Levi, S.5    Cozzi, A.6    Piperno, A.7    Fiorelli, G.8
  • 17
    • 63349103637 scopus 로고    scopus 로고
    • Ferritin functions as a proinflammatory cytokine via iron-independent protein kinase C zeta/nuclear factor kappaB-regulated signaling in rat hepatic stellate cells
    • Ruddell, R. G., Hoang-Le, D., Barwood, J. M., Rutherford, P. S., Piva, T. J., Watters, D. J., Santambrogio, P., Arosio, P., and Ramm, G. A. (2009) Ferritin functions as a proinflammatory cytokine via iron-independent protein kinase C zeta/nuclear factor kappaB-regulated signaling in rat hepatic stellate cells. Hepatology 49, 887-900
    • (2009) Hepatology , vol.49 , pp. 887-900
    • Ruddell, R.G.1    Hoang-Le, D.2    Barwood, J.M.3    Rutherford, P.S.4    Piva, T.J.5    Watters, D.J.6    Santambrogio, P.7    Arosio, P.8    Ramm, G.A.9
  • 18
    • 0036489168 scopus 로고    scopus 로고
    • Drosophila melanogaster ferritin: cDNA encoding a light chain homologue, temporal and tissue specific expression of both subunit types
    • DOI 10.1016/S0965-1748(01)00090-X, PII S096517480100090X
    • Georgieva, T., Dunkov, B. C., Dimov, S., Ralchev, K., and Law, J. H. (2002) Drosophila melanogaster ferritin: cDNA encoding a light chain homologue, temporal and tissue specific expression of both subunit types. Insect Biochem. Mol. Biol. 32, 295-302 (Pubitemid 34145745)
    • (2002) Insect Biochemistry and Molecular Biology , vol.32 , Issue.3 , pp. 295-302
    • Georgieva, T.1    Dunkov, B.C.2    Dimov, S.3    Ralchev, K.4    Law, J.H.5
  • 19
    • 2542448595 scopus 로고    scopus 로고
    • Aedes aegypti ferritin heavy chain homologue: Feeding of iron or blood influences message levels, lengths and subunit abundance
    • Dunkov, B. C., Georgieva, T., Yoshiga, T., Hall, M., and Law, J. H. (2002) Aedes aegypti ferritin heavy chain homologue: feeding of iron or blood influences message levels, lengths and subunit abundance. J. Insect Sci. 2, 7
    • (2002) J. Insect Sci. , vol.2 , pp. 7
    • Dunkov, B.C.1    Georgieva, T.2    Yoshiga, T.3    Hall, M.4    Law, J.H.5
  • 24
    • 34247530855 scopus 로고    scopus 로고
    • Dissection of the pathway required for generation of vitamin A and for Drosophila phototransduction
    • DOI 10.1083/jcb.200610081
    • Wang, T., Jiao, Y., and Montell, C. (2007) Dissection of the pathway required for generation of vitamin A and for Drosophila phototransduction. J. Cell Biol. 177, 305-316 (Pubitemid 46658641)
    • (2007) Journal of Cell Biology , vol.177 , Issue.2 , pp. 305-316
    • Wang, T.1    Jiao, Y.2    Montell, C.3
  • 25
    • 68849129637 scopus 로고    scopus 로고
    • Dietary zinc absorption is mediated by ZnT1 in Drosophila melanogaster
    • Wang, X., Wu, Y., and Zhou, B. (2009) Dietary zinc absorption is mediated by ZnT1 in Drosophila melanogaster. FASEB J. 23, 2650-2661
    • (2009) FASEB J. , vol.23 , pp. 2650-2661
    • Wang, X.1    Wu, Y.2    Zhou, B.3
  • 26
    • 70449288910 scopus 로고
    • Metabolic activity in calcified tissues: Aconitase and isocitric dehydrogenase activities in rabbit and dog femurs
    • Van Reen, R. (1959) Metabolic activity in calcified tissues: aconitase and isocitric dehydrogenase activities in rabbit and dog femurs. J. Biol. Chem. 234, 1951-1954
    • (1959) J. Biol. Chem. , vol.234 , pp. 1951-1954
    • Van Reen, R.1
  • 27
    • 70350774174 scopus 로고    scopus 로고
    • Pantothenate kinase-associated neurodegeneration: Insights from a Drosophila model
    • Wu, Z., Li, C., Lv, S., and Zhou, B. (2009) Pantothenate kinase-associated neurodegeneration: insights from a Drosophila model. Human Mol. Genet. 18, 3659-3672
    • (2009) Human Mol. Genet. , vol.18 , pp. 3659-3672
    • Wu, Z.1    Li, C.2    Lv, S.3    Zhou, B.4
  • 28
    • 0033391431 scopus 로고    scopus 로고
    • Organization of the ferritin genes in Drosophila melanogaster
    • DOI 10.1089/104454999314791
    • Dunkov, B. C., and Georgieva, T. (1999) Organization of the ferritin genes in Drosophila melanogaster. DNA Cell Biol. 18, 937-944 (Pubitemid 30013446)
    • (1999) DNA and Cell Biology , vol.18 , Issue.12 , pp. 937-944
    • Dunkov, B.C.1    Georgieva, T.2
  • 30
    • 79951977041 scopus 로고    scopus 로고
    • Iron depletion in the intestines of Malvolio mutant flies does not occur in the absence of a multicopper oxidase
    • Bettedi, L., Aslam, M. F., Szular, J., Mandilaras, K., and Missirlis, F. (2011) Iron depletion in the intestines of Malvolio mutant flies does not occur in the absence of a multicopper oxidase. J. Exp. Biol. 214, 971-978
    • (2011) J. Exp. Biol. , vol.214 , pp. 971-978
    • Bettedi, L.1    Aslam, M.F.2    Szular, J.3    Mandilaras, K.4    Missirlis, F.5
  • 31
    • 0028797538 scopus 로고
    • Malvolio, the Drosophila homologue of mouse NRAMP-1 (Bcg), is expressed in macrophages and in the nervous system and is required for normal taste behaviour
    • Rodrigues, V., Cheah, P. Y., Ray, K., and Chia, W. (1995) malvolio, the Drosophila homologue of mouse NRAMP-1 (Bcg), is expressed in macrophages and in the nervous system and is required for normal taste behaviour. EMBO J. 14, 3007-3020
    • (1995) EMBO J. , vol.14 , pp. 3007-3020
    • Rodrigues, V.1    Cheah, P.Y.2    Ray, K.3    Chia, W.4
  • 32
    • 0018853501 scopus 로고
    • Analysis of cell movements and fate mapping during early embryogenesis in Drosophila melanogaster
    • Underwood, E. M., Turner, F. R., and Mahowald, A. P. (1980) Analysis of cell movements and fate mapping during early embryogenesis in Drosophila melanogaster. Dev. Biol. 74, 286-301 (Pubitemid 10137929)
    • (1980) Developmental Biology , vol.74 , Issue.2 , pp. 286-301
    • Underwood, E.M.1    Turner, F.R.2    Mahowald, A.P.3
  • 33
    • 69749094882 scopus 로고    scopus 로고
    • Ferritin accumulation under iron scarcity in Drosophila iron cells
    • Mehta, A., Deshpande, A., Bettedi, L., and Missirlis, F. (2009) Ferritin accumulation under iron scarcity in Drosophila iron cells. Biochimie (Paris) 91, 1331-1334
    • (2009) Biochimie (Paris) , vol.91 , pp. 1331-1334
    • Mehta, A.1    Deshpande, A.2    Bettedi, L.3    Missirlis, F.4
  • 34
    • 33644551295 scopus 로고    scopus 로고
    • Secreted ferritin: Mosquito defense against iron overload?
    • Geiser, D. L., Zhang, D., and Winzerling, J. J. (2006) Secreted ferritin: mosquito defense against iron overload? Insect Biochem. Mol. Biol. 36, 177-187
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 177-187
    • Geiser, D.L.1    Zhang, D.2    Winzerling, J.J.3
  • 36
    • 77956327702 scopus 로고    scopus 로고
    • Intestinal ferritin H is required for an accurate control of iron absorption
    • Vanoaica, L., Darshan, D., Richman, L., Schümann, K., and Kühn, L. C. (2010) Intestinal ferritin H is required for an accurate control of iron absorption. Cell Metabol. 12, 273-282
    • (2010) Cell Metabol. , vol.12 , pp. 273-282
    • Vanoaica, L.1    Darshan, D.2    Richman, L.3    Schümann, K.4    Kühn, L.C.5
  • 37
    • 70349237065 scopus 로고    scopus 로고
    • Conditional deletion of ferritin H in mice induces loss of iron storage and liver damage
    • Darshan, D., Vanoaica, L., Richman, L., Beermann, F., and Kühn, L. C. (2009) Conditional deletion of ferritin H in mice induces loss of iron storage and liver damage. Hepatology 50, 852-860
    • (2009) Hepatology , vol.50 , pp. 852-860
    • Darshan, D.1    Vanoaica, L.2    Richman, L.3    Beermann, F.4    Kühn, L.C.5
  • 39
    • 33745650085 scopus 로고    scopus 로고
    • Immunolocalisation of the D. melanogaster Nramp homologue Malvolio to gut and Malpighian tubules provides evidence that Malvolio and Nramp2 are orthologous
    • Folwell, J. L. (2006) Immunolocalisation of the D. melanogaster Nramp homologue Malvolio to gut and Malpighian tubules provides evidence that Malvolio and Nramp2 are orthologous. J. Exp. Biol. 209, 1988-1995
    • (2006) J. Exp. Biol. , vol.209 , pp. 1988-1995
    • Folwell, J.L.1
  • 40
    • 0031933728 scopus 로고    scopus 로고
    • Metal ions suppress the abnormal taste behavior of the Drosophila mutant malvolio
    • Orgad, S., Nelson, H., Segal, D., and Nelson, N. (1998) Metal ions suppress the abnormal taste behavior of the Drosophila mutant malvolio. J. Exp. Biol. 201, 115-120 (Pubitemid 28065669)
    • (1998) Journal of Experimental Biology , vol.201 , Issue.1 , pp. 115-120
    • Orgad, S.1    Nelson, H.2    Segal, D.3    Nelson, N.4
  • 41
    • 0033166065 scopus 로고    scopus 로고
    • Functional complementation of the malvolio mutation in the taste pathway of Drosophila melanogaster by the human natural resistance-associated macrophage protein 1 (Nramp-1)
    • D'Souza, J., Cheah, P. Y., Gros, P., Chia, W., and Rodrigues, V. (1999) Functional complementation of the malvolio mutation in the taste pathway of Drosophila melanogaster by the human natural resistance-associated macrophage protein 1 (Nramp-1). J. Exp. Biol. 202, 1909-1915 (Pubitemid 29368553)
    • (1999) Journal of Experimental Biology , vol.202 , Issue.14 , pp. 1909-1915
    • D'Souza, J.1    Cheah, P.Y.2    Gros, P.3    Chia, W.4    Rodrigues, V.5
  • 43
    • 78650908746 scopus 로고    scopus 로고
    • Decoupling ferritin synthesis from free cytosolic iron results in ferritin secretion
    • De Domenico, I., Vaughn, M. B., Paradkar, P. N., Lo, E., Ward, D. M., and Kaplan, J. (2011) Decoupling ferritin synthesis from free cytosolic iron results in ferritin secretion. Cell Metabol. 13, 57-67
    • (2011) Cell Metabol. , vol.13 , pp. 57-67
    • De Domenico, I.1    Vaughn, M.B.2    Paradkar, P.N.3    Lo, E.4    Ward, D.M.5    Kaplan, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.