메뉴 건너뛰기




Volumn 106, Issue 4, 2009, Pages 1033-1038

Knockdown of proteins involved in iron metabolism limits tick reproduction and development

Author keywords

Cytosolic aconitase; Ferritin; IRP; RNAi

Indexed keywords

FERRITIN; FERRITIN 1; FERRITIN 2; IRON REGULATORY FACTOR; UNCLASSIFIED DRUG;

EID: 59049100529     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0807961106     Document Type: Article
Times cited : (139)

References (40)
  • 2
    • 0001599068 scopus 로고
    • Bloodsucking ticks (Ixodoidea) - vectors of disease of man and animals (English translation)
    • Balashov YS (1972) Bloodsucking ticks (Ixodoidea) - vectors of disease of man and animals (English translation). Misc Publ Entomol Soc Amer 8:163-376.
    • (1972) Misc Publ Entomol Soc Amer , vol.8 , pp. 163-376
    • Balashov, Y.S.1
  • 3
    • 57549115852 scopus 로고    scopus 로고
    • Profiling of proteolytic enzymes in the gut of the tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases
    • Sojka D, et al. (2008) Profiling of proteolytic enzymes in the gut of the tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases. Parasit Vectors 1:7.
    • (2008) Parasit Vectors , vol.1 , pp. 7
    • Sojka, D.1
  • 4
    • 0037506077 scopus 로고    scopus 로고
    • A new intracellular pathway of haem detoxification in the midgut of the cattle tick Boophilus microplus: Aggregation inside a specialized organelle, the hemosome
    • Lara FA, et al. (2003) A new intracellular pathway of haem detoxification in the midgut of the cattle tick Boophilus microplus: Aggregation inside a specialized organelle, the hemosome. J Exp Biol 206:1707-1715.
    • (2003) J Exp Biol , vol.206 , pp. 1707-1715
    • Lara, F.A.1
  • 5
    • 25144490692 scopus 로고    scopus 로고
    • Tracing heme in a living cell: Hemoglobin degradation and heme traffic in digest cells of the cattle tick Boophilus microplus
    • Lara FA, Lins U, Bechara GH, Oliveira PL (2005) Tracing heme in a living cell: Hemoglobin degradation and heme traffic in digest cells of the cattle tick Boophilus microplus. J Exp Biol 208:3093-3101.
    • (2005) J Exp Biol , vol.208 , pp. 3093-3101
    • Lara, F.A.1    Lins, U.2    Bechara, G.H.3    Oliveira, P.L.4
  • 6
    • 0034711311 scopus 로고    scopus 로고
    • HeLp, a heme lipoprotein from the hemolymph of the cattle tick, Boophilus microplus
    • Maya-Monteiro CM, et al. (2000) HeLp, a heme lipoprotein from the hemolymph of the cattle tick, Boophilus microplus. J Biol Chem 275:36584-36589.
    • (2000) J Biol Chem , vol.275 , pp. 36584-36589
    • Maya-Monteiro, C.M.1
  • 7
    • 0033166924 scopus 로고    scopus 로고
    • A missing metabolic pathway in the cattle tick Boophilus microplus
    • Braz GR, Coelho HS, Masuda H, Oliveira PL (1999) A missing metabolic pathway in the cattle tick Boophilus microplus. Curr Biol 9:703-706.
    • (1999) Curr Biol , vol.9 , pp. 703-706
    • Braz, G.R.1    Coelho, H.S.2    Masuda, H.3    Oliveira, P.L.4
  • 8
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze MW, Muckenthaler MU, Andrews NC (2004) Balancing acts: Molecular control of mammalian iron metabolism. Cell 117:285-297.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 10
    • 33845865301 scopus 로고    scopus 로고
    • Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA
    • Walden WE, et al. (2006) Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA. Science 314:1903-1908.
    • (2006) Science , vol.314 , pp. 1903-1908
    • Walden, W.E.1
  • 13
    • 35548958227 scopus 로고    scopus 로고
    • Fate of blood meal iron in mosquitoes
    • Zhou G, et al. (2007) Fate of blood meal iron in mosquitoes. J Insect Physiol 53:1169-1178.
    • (2007) J Insect Physiol , vol.53 , pp. 1169-1178
    • Zhou, G.1
  • 14
    • 33745809125 scopus 로고    scopus 로고
    • Of two cytosolic aconitases expressed in Drosophila, only one functions as an iron-regulatory protein
    • Lind MI, et al. (2006) Of two cytosolic aconitases expressed in Drosophila, only one functions as an iron-regulatory protein. J Biol Chem 281:18707-18714.
    • (2006) J Biol Chem , vol.281 , pp. 18707-18714
    • Lind, M.I.1
  • 15
    • 0037211912 scopus 로고    scopus 로고
    • Molecular cloning, expression and isolation of ferritins from two tick species-Ornithodoros moubata and Ixodes ricinus
    • Kopacek P, et al. (2003) Molecular cloning, expression and isolation of ferritins from two tick species-Ornithodoros moubata and Ixodes ricinus. Insect Biochem Mol Biol 33:103-113.
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 103-113
    • Kopacek, P.1
  • 17
  • 18
    • 33745808620 scopus 로고    scopus 로고
    • DMT1: Which metals does it transport?
    • Garrick MD, et al. (2006) DMT1: Which metals does it transport? Biol Res 39:79-85.
    • (2006) Biol Res , vol.39 , pp. 79-85
    • Garrick, M.D.1
  • 19
    • 33645091619 scopus 로고    scopus 로고
    • Insect iron binding proteins: Insights from the genomes
    • Dunkov B, Georgieva T (2006) Insect iron binding proteins: Insights from the genomes. Insect Biochem Mol Biol 36:300-309.
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 300-309
    • Dunkov, B.1    Georgieva, T.2
  • 20
    • 33644804529 scopus 로고    scopus 로고
    • Crystal structure of human iron regulatory protein 1 as cytosolic aconitase
    • Dupuy J, et al. (2006) Crystal structure of human iron regulatory protein 1 as cytosolic aconitase. Structure 14:129-139.
    • (2006) Structure , vol.14 , pp. 129-139
    • Dupuy, J.1
  • 21
    • 0026587755 scopus 로고
    • Crystal structures of aconitase with isocitrate and nitroisocitrate bound
    • Lauble H, Kennedy MC, Beinert H, Stout CD (1992) Crystal structures of aconitase with isocitrate and nitroisocitrate bound. Biochemistry 31:2735-2748.
    • (1992) Biochemistry , vol.31 , pp. 2735-2748
    • Lauble, H.1    Kennedy, M.C.2    Beinert, H.3    Stout, C.D.4
  • 22
    • 0031547971 scopus 로고    scopus 로고
    • Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution
    • Hempstead PD, et al. (1997) Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution. J Mol Biol 268:424-448.
    • (1997) J Mol Biol , vol.268 , pp. 424-448
    • Hempstead, P.D.1
  • 23
    • 27644444230 scopus 로고    scopus 로고
    • The response of ferritin to LPS and acute phase of Pseudomonas infection
    • Ong DS, Wang L, Zhu Y, Ho B, Ding JL (2005) The response of ferritin to LPS and acute phase of Pseudomonas infection. J Endotoxin Res 11:267-280.
    • (2005) J Endotoxin Res , vol.11 , pp. 267-280
    • Ong, D.S.1    Wang, L.2    Zhu, Y.3    Ho, B.4    Ding, J.L.5
  • 24
    • 0028357845 scopus 로고
    • cDNA cloning and deduced amino acid sequence of two ferritins: Soma ferritin and yolk ferritin, from the snail Lymnaea stagnalis L
    • von Darl M, Harrison PM, Bottke W (1994) cDNA cloning and deduced amino acid sequence of two ferritins: Soma ferritin and yolk ferritin, from the snail Lymnaea stagnalis L. Eur J Biochem 222:353-366.
    • (1994) Eur J Biochem , vol.222 , pp. 353-366
    • von Darl, M.1    Harrison, P.M.2    Bottke, W.3
  • 25
    • 0034603062 scopus 로고    scopus 로고
    • Early embryonic lethality of H ferritin gene deletion in mice
    • Ferreira C, et al. (2000) Early embryonic lethality of H ferritin gene deletion in mice. J Biol Chem 275:3021-3024.
    • (2000) J Biol Chem , vol.275 , pp. 3021-3024
    • Ferreira, C.1
  • 26
    • 33645307993 scopus 로고    scopus 로고
    • Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development
    • Smith SR, Ghosh MC, Ollivierre-Wilson H, Hang Tong W, Rouault TA (2006) Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development. Blood Cells Mol Dis 36:283-287.
    • (2006) Blood Cells Mol Dis , vol.36 , pp. 283-287
    • Smith, S.R.1    Ghosh, M.C.2    Ollivierre-Wilson, H.3    Hang Tong, W.4    Rouault, T.A.5
  • 27
    • 35048859798 scopus 로고    scopus 로고
    • Homeostatic mechanisms for iron storage revealed by genetic manipulations and live imaging of Drosophila ferritin
    • Missirlis F, et al. (2007) Homeostatic mechanisms for iron storage revealed by genetic manipulations and live imaging of Drosophila ferritin. Genetics 177:89-100.
    • (2007) Genetics , vol.177 , pp. 89-100
    • Missirlis, F.1
  • 28
    • 0038035611 scopus 로고    scopus 로고
    • Kinetics of ingested host immunoglobulin G in hemolymph and whole body homogenates during nymphal development of Dermacentor variabilis and Ixodes scapularis ticks (Acari: Ixodidae)
    • Vaughan JA, Sonenshine DE, Azad AF (2002) Kinetics of ingested host immunoglobulin G in hemolymph and whole body homogenates during nymphal development of Dermacentor variabilis and Ixodes scapularis ticks (Acari: Ixodidae). Exp Appl Acarol 27:329-340.
    • (2002) Exp Appl Acarol , vol.27 , pp. 329-340
    • Vaughan, J.A.1    Sonenshine, D.E.2    Azad, A.F.3
  • 29
    • 0004151015 scopus 로고
    • Oxford Univ Press, New York, pp
    • Sonenshine DE (1991) in Biology of ticks (Oxford Univ Press, New York), pp 159-188.
    • (1991) Biology of ticks , pp. 159-188
    • Sonenshine, D.E.1
  • 32
    • 0029557688 scopus 로고
    • Succinate dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element in its 5′-untranslated region
    • Kohler SA, Henderson BR, Kuhn LC (1995) Succinate dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element in its 5′-untranslated region. J Biol Chem 270:30781-30786.
    • (1995) J Biol Chem , vol.270 , pp. 30781-30786
    • Kohler, S.A.1    Henderson, B.R.2    Kuhn, L.C.3
  • 33
    • 0030791329 scopus 로고    scopus 로고
    • Isolation and properties of Drosophila melanogaster ferritin - molecular cloning of a cDNA that encodes one subunit, and localization of the gene on the third chromosome
    • Charlesworth A, et al. (1997) Isolation and properties of Drosophila melanogaster ferritin - molecular cloning of a cDNA that encodes one subunit, and localization of the gene on the third chromosome. Eur J Biochem 247:470-475.
    • (1997) Eur J Biochem , vol.247 , pp. 470-475
    • Charlesworth, A.1
  • 35
    • 33646363763 scopus 로고    scopus 로고
    • Iron-withholding strategy in innate immunity
    • Ong ST, Ho JZ, Ho B, Ding JL (2006) Iron-withholding strategy in innate immunity. Immunobiology 211:295-314.
    • (2006) Immunobiology , vol.211 , pp. 295-314
    • Ong, S.T.1    Ho, J.Z.2    Ho, B.3    Ding, J.L.4
  • 36
    • 34547738955 scopus 로고    scopus 로고
    • Ferritin: A novel mechanism for delivery of iron to the brain and other organs
    • Fisher J, et al. (2007) Ferritin: A novel mechanism for delivery of iron to the brain and other organs. Am J Physiol Cell Physiol 293:C641-C649.
    • (2007) Am J Physiol Cell Physiol , vol.293
    • Fisher, J.1
  • 37
    • 34247593923 scopus 로고    scopus 로고
    • IrAE: An asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus
    • Sojka D, et al. (2007) IrAE: An asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus. Int J Parasitol 37:713-724.
    • (2007) Int J Parasitol , vol.37 , pp. 713-724
    • Sojka, D.1
  • 38
    • 0029556818 scopus 로고
    • The prophenoloxidase from the wax moth Galleria mellonella: Purification and characterization of the proenzyme
    • Kopacek P, Weise C, Gotz P (1995) The prophenoloxidase from the wax moth Galleria mellonella: Purification and characterization of the proenzyme. Insect Biochem Mol Biol 25:1081-1091.
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 1081-1091
    • Kopacek, P.1    Weise, C.2    Gotz, P.3
  • 39
    • 0030587616 scopus 로고    scopus 로고
    • Molecular characterization of prothoracicotropic hormone (PTTH) from the giant silkmoth Antheraea pernyi: Developmental appearance of PTTH-expressing cells and relationship to circadian clock cells in central brain
    • Sauman I, Reppert SM (1996) Molecular characterization of prothoracicotropic hormone (PTTH) from the giant silkmoth Antheraea pernyi: Developmental appearance of PTTH-expressing cells and relationship to circadian clock cells in central brain. Dev Biol 178:418-429.
    • (1996) Dev Biol , vol.178 , pp. 418-429
    • Sauman, I.1    Reppert, S.M.2
  • 40
    • 0035831034 scopus 로고    scopus 로고
    • Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae
    • Levashina EA, et al. (2001) Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae. Cell 104:709-718.
    • (2001) Cell , vol.104 , pp. 709-718
    • Levashina, E.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.