메뉴 건너뛰기




Volumn 109, Issue 33, 2012, Pages 13337-13342

Multicopper oxidase-1 is a ferroxidase essential for iron homeostasis in Drosophila melanogaster

Author keywords

[No Author keywords available]

Indexed keywords

CERULOPLASMIN; FERROUS ION; IRON; MULTICOPPER OXIDASE 1; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 84865186973     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1208703109     Document Type: Article
Times cited : (55)

References (36)
  • 1
    • 77956256281 scopus 로고    scopus 로고
    • Redox cycling in iron uptake, efflux, and trafficking
    • Kosman DJ (2010) Redox cycling in iron uptake, efflux, and trafficking. J Biol Chem 285:26729-26735.
    • (2010) J Biol Chem , vol.285 , pp. 26729-26735
    • Kosman, D.J.1
  • 2
    • 40649120516 scopus 로고    scopus 로고
    • Response to iron deprivation in Saccharomyces cerevisiae
    • DOI 10.1128/EC.00354-07
    • Philpott CC, Protchenko O (2008) Response to iron deprivation in Saccharomyces cerevisiae. Eukaryot Cell 7:20-27. (Pubitemid 351959590)
    • (2008) Eukaryotic Cell , vol.7 , Issue.1 , pp. 20-27
    • Philpott, C.C.1    Protchenko, O.2
  • 3
    • 77953524181 scopus 로고    scopus 로고
    • Analysis of the high-affinity iron uptake system at the Chlamydomonas reinhardtii plasma membrane
    • Terzulli A, Kosman DJ (2010) Analysis of the high-affinity iron uptake system at the Chlamydomonas reinhardtii plasma membrane. Eukaryot Cell 9:815-826.
    • (2010) Eukaryot Cell , vol.9 , pp. 815-826
    • Terzulli, A.1    Kosman, D.J.2
  • 4
    • 34250800318 scopus 로고    scopus 로고
    • Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin
    • DOI 10.1038/sj.emboj.7601735, PII 7601735
    • De Domenico I, et al. (2007) Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin. EMBO J 26:2823-2831. (Pubitemid 46975784)
    • (2007) EMBO Journal , vol.26 , Issue.12 , pp. 2823-2831
    • De Domenico, I.1    Ward, D.M.2    Di, P.M.C.B.3    Jeong, S.Y.4    David, S.5    Musci, G.6    Kaplan, J.7
  • 5
    • 79951497417 scopus 로고    scopus 로고
    • Molecular mechanism of intestinal iron absorption
    • Han O (2011) Molecular mechanism of intestinal iron absorption. Metallomics 3: 103-109.
    • (2011) Metallomics , vol.3 , pp. 103-109
    • Han, O.1
  • 7
    • 0036400025 scopus 로고    scopus 로고
    • Ceruloplasmin metabolism and function
    • DOI 10.1146/annurev.nutr.22.012502.114457
    • Hellman NE, Gitlin JD (2002) Ceruloplasmin metabolism and function. Annu Rev Nutr 22:439-458. (Pubitemid 35221468)
    • (2002) Annual Review of Nutrition , vol.22 , pp. 439-458
    • Hellman, N.E.1    Gitlin, J.D.2
  • 8
    • 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 MF, Szular J, Mandilaras K, 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
  • 10
    • 0023714837 scopus 로고
    • Iron binding proteins and their roles in the tobacco hornworm, Manduca sexta (L.)
    • Huebers HA, et al. (1988) Iron binding proteins and their roles in the tobacco hornworm, Manduca sexta (L.). J Comp Physiol B 158:291-300.
    • (1988) J Comp Physiol B , vol.158 , pp. 291-300
    • Huebers, H.A.1
  • 11
    • 0025695557 scopus 로고
    • Isolation and molecular cloning of transferrin from the tobacco hornworm, Manduca sexta: Sequence similarity to the vertebrate transferrins
    • Bartfeld NS, Law JH (1990) Isolation and molecular cloning of transferrin from the tobacco hornworm, Manduca sexta. Sequence similarity to the vertebrate transferrins. J Biol Chem 265:21684-21691. (Pubitemid 120014212)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.35 , pp. 21684-21691
    • Bartfeld, N.S.1    Law, J.H.2
  • 12
    • 84857358614 scopus 로고    scopus 로고
    • Insect transferrins: Multifunctional proteins
    • Geiser DL, Winzerling JJ (2012) Insect transferrins: Multifunctional proteins. Biochim Biophys Acta 1820:437-451.
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 437-451
    • Geiser, D.L.1    Winzerling, J.J.2
  • 13
    • 0036032176 scopus 로고    scopus 로고
    • The multicopper oxidase of Pseudomonas aeruginosa is a ferroxidase with a central role in iron acquisition
    • DOI 10.1046/j.1365-2958.2002.03132.x
    • Huston WM, Jennings MP, McEwan AG (2002) The multicopper oxidase of Pseudomonas aeruginosa is a ferroxidase with a central role in iron acquisition. Mol Microbiol 45:1741-1750. (Pubitemid 35231987)
    • (2002) Molecular Microbiology , vol.45 , Issue.6 , pp. 1741-1750
    • Huston, W.M.1    Jennings, M.P.2    McEwan, A.G.3
  • 14
    • 1642444735 scopus 로고    scopus 로고
    • Ferroxidase activity in a laccase-like multicopper oxidase from Liriodendron tulipifera
    • DOI 10.1016/j.plaphy.2003.10.011
    • Hoopes JT, Dean JFD (2004) Ferroxidase activity in a laccase-like multicopper oxidase from Liriodendron tulipifera. Plant Physiol Biochem 42:27-33. (Pubitemid 38106245)
    • (2004) Plant Physiology and Biochemistry , vol.42 , Issue.1 , pp. 27-33
    • Hoopes, J.T.1    Dean, J.F.D.2
  • 15
    • 77950518275 scopus 로고    scopus 로고
    • Insect multicopper oxidases: Diversity, properties, and physiological roles
    • Dittmer NT, Kanost MR (2010) Insect multicopper oxidases: Diversity, properties, and physiological roles. Insect Biochem Mol Biol 40:179-188.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 179-188
    • Dittmer, N.T.1    Kanost, M.R.2
  • 16
    • 34848846870 scopus 로고    scopus 로고
    • Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase
    • Sakurai T, Kataoka K (2007) Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase. Chem Rec 7:220-229.
    • (2007) Chem Rec , vol.7 , pp. 220-229
    • Sakurai, T.1    Kataoka, K.2
  • 17
    • 79953043801 scopus 로고    scopus 로고
    • The developmental transcriptome of Drosophila melanogaster
    • Graveley BR, et al. (2011) The developmental transcriptome of Drosophila melanogaster. Nature 471:473-479.
    • (2011) Nature , vol.471 , pp. 473-479
    • Graveley, B.R.1
  • 18
    • 34249804498 scopus 로고    scopus 로고
    • Using FlyAtlas to identify better Drosophila melanogaster models of human disease
    • DOI 10.1038/ng2049, PII NG2049
    • Chintapalli VR, Wang J, Dow JAT (2007) Using FlyAtlas to identify better Drosophila melanogaster models of human disease. Nat Genet 39:715-720. (Pubitemid 46848596)
    • (2007) Nature Genetics , vol.39 , Issue.6 , pp. 715-720
    • Chintapalli, V.R.1    Wang, J.2    Dow, J.A.T.3
  • 20
    • 79957940736 scopus 로고    scopus 로고
    • A comprehensive gene expression atlas of sex- And tissue-specificity in the malaria vector, Anopheles gambiae
    • Baker DA, et al. (2011) A comprehensive gene expression atlas of sex- and tissue-specificity in the malaria vector, Anopheles gambiae. BMC Genomics 12:296.
    • (2011) BMC Genomics , vol.12 , pp. 296
    • Baker, D.A.1
  • 21
    • 0742305629 scopus 로고    scopus 로고
    • Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae
    • DOI 10.1016/j.ibmb.2003.08.003
    • Dittmer NT, et al. (2004) Characterization of cDNAs encoding putative laccase-like multicopper oxidases and developmental expression in the tobacco hornworm, Manduca sexta, and the malaria mosquito, Anopheles gambiae. Insect Biochem Mol Biol 34:29-41. (Pubitemid 38157610)
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , Issue.1 , pp. 29-41
    • Dittmer, N.T.1    Suderman, R.J.2    Jiang, H.3    Zhu, Y.-C.4    Gorman, M.J.5    Kramer, K.J.6    Kanost, M.R.7
  • 24
    • 34447310586 scopus 로고    scopus 로고
    • Shall we dance? How a multicopper oxidase chooses its electron transfer partner
    • Quintanar L, et al. (2007) Shall we dance? How a multicopper oxidase chooses its electron transfer partner. Acc Chem Res 40:445-452.
    • (2007) Acc Chem Res , vol.40 , pp. 445-452
    • Quintanar, L.1
  • 25
    • 33750310022 scopus 로고    scopus 로고
    • Structural basis of the ferrous iron specificity of the yeast ferroxidase, Fet3p
    • DOI 10.1021/bi061543+
    • Stoj CS, Augustine AJ, Zeigler L, Solomon EI, Kosman DJ (2006) Structural basis of the ferrous iron specificity of the yeast ferroxidase, Fet3p. Biochemistry 45:12741-12749. (Pubitemid 44630860)
    • (2006) Biochemistry , vol.45 , Issue.42 , pp. 12741-12749
    • Stoj, C.S.1    Augustine, A.J.2    Zeigler, L.3    Solomon, E.I.4    Kosman, D.J.5
  • 26
    • 84862777900 scopus 로고    scopus 로고
    • Kinetic properties of alternatively spliced isoforms of laccase- 2 from Tribolium castaneum and Anopheles gambiae
    • Gorman MJ, et al. (2012) Kinetic properties of alternatively spliced isoforms of laccase- 2 from Tribolium castaneum and Anopheles gambiae. Insect Biochem Mol Biol 42:193-202.
    • (2012) Insect Biochem Mol Biol , vol.42 , pp. 193-202
    • Gorman, M.J.1
  • 27
    • 84858973704 scopus 로고    scopus 로고
    • Multicopper oxidase-3 is a laccase associated with the peritrophic matrix of Anopheles gambiae
    • Lang M, Kanost MR, Gorman MJ (2012) Multicopper oxidase-3 is a laccase associated with the peritrophic matrix of Anopheles gambiae. PLoS ONE 7:e33985.
    • (2012) PLoS ONE , vol.7
    • Lang, M.1    Kanost, M.R.2    Gorman, M.J.3
  • 29
    • 69749094882 scopus 로고    scopus 로고
    • Ferritin accumulation under iron scarcity in Drosophila iron cells
    • Mehta A, Deshpande A, Bettedi L, Missirlis F (2009) Ferritin accumulation under iron scarcity in Drosophila iron cells. Biochimie 91:1331-1334.
    • (2009) Biochimie , vol.91 , pp. 1331-1334
    • Mehta, A.1    Deshpande, A.2    Bettedi, L.3    Missirlis, F.4
  • 30
    • 33645827980 scopus 로고    scopus 로고
    • Characterization of mitochondrial ferritin in Drosophila
    • Missirlis F, et al. (2006) Characterization of mitochondrial ferritin in Drosophila. Proc Natl Acad Sci USA 103:5893-5898.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 5893-5898
    • Missirlis, F.1
  • 32
    • 33646363763 scopus 로고    scopus 로고
    • Iron-withholding strategy in innate immunity
    • Ong ST, Ho JZS, 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.S.2    Ho, B.3    Ding, J.L.4
  • 34
    • 78149283974 scopus 로고    scopus 로고
    • Epithelial septate junction assembly relies on melanotransferrin iron binding and endocytosis in Drosophila
    • Tiklová K, Senti KA, Wang S, Gräslund A, Samakovlis C (2010) Epithelial septate junction assembly relies on melanotransferrin iron binding and endocytosis in Drosophila. Nat Cell Biol 12:1071-1077.
    • (2010) Nat Cell Biol , vol.12 , pp. 1071-1077
    • Tiklová, K.1    Senti, K.A.2    Wang, S.3    Gräslund, A.4    Samakovlis, C.5
  • 35
    • 84901971317 scopus 로고
    • Chemical differentiation of the larval mid gut of Drosophila
    • Poulson DF (1950) Chemical differentiation of the larval mid gut of Drosophila. Genetics 35:130-131.
    • (1950) Genetics , vol.35 , pp. 130-131
    • Poulson, D.F.1
  • 36
    • 33847670407 scopus 로고
    • Ferrozine - A new spectrophotometric reagent for iron
    • Stookey LL (1970) Ferrozine - a new spectrophotometric reagent for iron. Anal Chem 42:779-781.
    • (1970) Anal Chem , vol.42 , pp. 779-781
    • Stookey, L.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.