메뉴 건너뛰기




Volumn 150, Issue 2, 2008, Pages 161-169

Insect transferrin functions as an antioxidant protein in a beetle larva

Author keywords

Antioxidant protein; Apoptotic cell death; Insect; Iron; Oxidative stress; RNA interference; Stress response; Transferrin

Indexed keywords

HYDROGEN PEROXIDE; IRON; MESSENGER RNA; TRANSFERRIN; VITELLOGENIN;

EID: 43049178199     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2008.02.009     Document Type: Article
Times cited : (45)

References (44)
  • 1
    • 0029851856 scopus 로고    scopus 로고
    • High-yield production of functionally active human serum transferrin using a baculovirus system, and its structural characterization
    • Ali S.A. Joao H.C. Csonga R. hammerschmid F. Steinkasserer A. High-yield production of functionally active human serum transferrin using a baculovirus system, and its structural characterization Biochem. J. 319 1996 191 195
    • (1996) Biochem. J. , vol.319 , pp. 191-195
    • Ali, S.A.1    Joao, H.C.2    Csonga, R.3    hammerschmid, F.4    Steinkasserer, A.5
  • 3
    • 0037388042 scopus 로고    scopus 로고
    • Dealing with iron: common structural principles in proteins that transport iron and heme
    • Baker H.M. Anderson B.F. Baker E.N. Dealing with iron: common structural principles in proteins that transport iron and heme Proc. Natl. Acad. Sci. U. S. A. 100 2003 3579 3583
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 3579-3583
    • Baker, H.M.1    Anderson, B.F.2    Baker, E.N.3
  • 4
    • 4444347472 scopus 로고    scopus 로고
    • Oxidative stress in autism: Increased lipid peroxidation and reduced serum levels of ceruloplasmin and transferrin — the antioxidant proteins
    • Chauhan A. Chauhan V. Brown W.T. Cohen I. Oxidative stress in autism: Increased lipid peroxidation and reduced serum levels of ceruloplasmin and transferrin — the antioxidant proteins Life Sci. 75 2004 2539 2549
    • (2004) Life Sci. , vol.75 , pp. 2539-2549
    • Chauhan, A.1    Chauhan, V.2    Brown, W.T.3    Cohen, I.4
  • 6
    • 4444269748 scopus 로고    scopus 로고
    • Apotransferrin is internalized and distributed in the same way as holotransferrin in K562 cells
    • Du X.L. Wang K. Yuan L. Li R.C. Chang Y.Z. Ho K.P. Qian Z.M. Apotransferrin is internalized and distributed in the same way as holotransferrin in K562 cells J. Cell. Physiol. 201 2004 45 54
    • (2004) J. Cell. Physiol. , vol.201 , pp. 45-54
    • Du, X.L.1    Wang, K.2    Yuan, L.3    Li, R.C.4    Chang, Y.Z.5    Ho, K.P.6    Qian, Z.M.7
  • 7
    • 33645091619 scopus 로고    scopus 로고
    • Insect iron binding proteins: Insights from the genomes
    • Dunkov B. Georgieva T. Insect iron binding proteins: Insights from the genomes Insect Biochem. Mol. Biol. 36 2006 300 309
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 300-309
    • Dunkov, B.1    Georgieva, T.2
  • 8
    • 0036968089 scopus 로고    scopus 로고
    • Transferrin regulates transcription of the MBP gene and its action synergizes with IGF-1 to enhance myelinogenesis in the md rat
    • Espinosa-Jeffrey A. Kumar S. Zhao P.M. Awosika O. Agbo C. Huang A. Chang R. De Vellis J. Transferrin regulates transcription of the MBP gene and its action synergizes with IGF-1 to enhance myelinogenesis in the md rat Develop. Neurosci. 24 2002 227 241
    • (2002) Develop. Neurosci. , vol.24 , pp. 227-241
    • Espinosa-Jeffrey, A.1    Kumar, S.2    Zhao, P.M.3    Awosika, O.4    Agbo, C.5    Huang, A.6    Chang, R.7    De Vellis, J.8
  • 9
    • 33644880803 scopus 로고    scopus 로고
    • Reactivity of carbon nanotubes: free radical generation or scavenging activity? Free Radic
    • Fenoglio I. Tomatis M. Lison D. Muller J. Fonseca A. Nagy J.B. Fubini B. Reactivity of carbon nanotubes: free radical generation or scavenging activity? Free Radic Biol. Med. 40 2006 1227 1233
    • (2006) Biol. Med. , vol.40 , pp. 1227-1233
    • Fenoglio, I.1    Tomatis, M.2    Lison, D.3    Muller, J.4    Fonseca, A.5    Nagy, J.B.6    Fubini, B.7
  • 11
    • 34447509457 scopus 로고    scopus 로고
    • Molecular aspects of transferrin expression in the tsetse fly (Glossina morsitans morsitans)
    • Guz N. Attardo G.M. Wu Y. Aksoy S. Molecular aspects of transferrin expression in the tsetse fly ( Glossina morsitans morsitans ) J. Insect Physiol. 53 2007 715 723
    • (2007) J. Insect Physiol. , vol.53 , pp. 715-723
    • Guz, N.1    Attardo, G.M.2    Wu, Y.3    Aksoy, S.4
  • 13
    • 0001590580 scopus 로고    scopus 로고
    • Free radicals, other reactive species and disease
    • Halliwell B. Gutteridge J.M.C. Free radicals, other reactive species and disease Free Radicals in Biology and Medicine 1999 Oxford Univ. Press New York 617 783
    • (1999) , pp. 617-783
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 15
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze M.W. Kuhn L.C. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress Proc. Natl. Acad. Sci. USA 93 1996 8175 8182
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 16
    • 0034185884 scopus 로고    scopus 로고
    • A juvenile hormone-responsible transferrin-like protein from the bean bug, Riptortus clavatus: cDNA sequence analysis and protein identification during diapause and vitellogenesis
    • Hirai M. Watanabe D. Chinzei Y. A juvenile hormone-responsible transferrin-like protein from the bean bug, Riptortus clavatus : cDNA sequence analysis and protein identification during diapause and vitellogenesis Arch. Insect Biochem. Physiol. 44 2000 17 26
    • (2000) Arch. Insect Biochem. Physiol. , vol.44 , pp. 17-26
    • Hirai, M.1    Watanabe, D.2    Chinzei, Y.3
  • 17
    • 0027453014 scopus 로고
    • Transferrin in a cockroach: molecular cloning, characterization and suppression by juvenile hormone
    • Jamroz R.C. Gasdaska J.R. Bradfield J.Y. Law J.H. Transferrin in a cockroach: molecular cloning, characterization and suppression by juvenile hormone Proc. Natl. Acad. Sci. U. S. A. 90 1993 1320 1324
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 1320-1324
    • Jamroz, R.C.1    Gasdaska, J.R.2    Bradfield, J.Y.3    Law, J.H.4
  • 18
    • 0035038211 scopus 로고    scopus 로고
    • A defective viral genome maintained in Escherichia coli for the generation of baculovirus expression vectors
    • Je Y.H. Chang J.H. Choi J.Y. Roh J.Y. Jin B.R. O’Reilly D.R. Kang S.K. A defective viral genome maintained in Escherichia coli for the generation of baculovirus expression vectors Biotechnol. Lett. 23 2001 575 582
    • (2001) Biotechnol. Lett. , vol.23 , pp. 575-582
    • Je, Y.H.1    Chang, J.H.2    Choi, J.Y.3    Roh, J.Y.4    Jin, B.R.5    O’Reilly, D.R.6    Kang, S.K.7
  • 20
    • 43049163230 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a transferrin cDNA from the white-spotted flower chafer, Protaetia brevitarsis
    • Kim B.Y. Lee K.S. Choo Y.M. Kim I. Hwang J.S. Sohn H.D. Jin B.R. Molecular cloning and characterization of a transferrin cDNA from the white-spotted flower chafer, Protaetia brevitarsis DNA Seq. 19 2008 146 150
    • (2008) DNA Seq. , vol.19 , pp. 146-150
    • Kim, B.Y.1    Lee, K.S.2    Choo, Y.M.3    Kim, I.4    Hwang, J.S.5    Sohn, H.D.6    Jin, B.R.7
  • 21
    • 1942429543 scopus 로고    scopus 로고
    • Transcriptional profiling reveals multifunctional roles for transferrin in the honeybee, Apis mellifera
    • Kucharski D. Maleszka R. Transcriptional profiling reveals multifunctional roles for transferrin in the honeybee, Apis mellifera J. Insect Sci. 3 2003 27
    • (2003) J. Insect Sci. , vol.3 , pp. 27
    • Kucharski, D.1    Maleszka, R.2
  • 22
    • 0028902673 scopus 로고
    • Molecular characterization of an insect transferrin and its selective incorporation into eggs during oogenesis
    • Kurama T. Kurata S. Natori S. Molecular characterization of an insect transferrin and its selective incorporation into eggs during oogenesis Eur. J. Biochem. 228 1995 229 235
    • (1995) Eur. J. Biochem. , vol.228 , pp. 229-235
    • Kurama, T.1    Kurata, S.2    Natori, S.3
  • 23
    • 24344475974 scopus 로고    scopus 로고
    • Evolution of the transferrin family: conservation of residues associated with iron and anion binding
    • Lambert L.A. Perri H. Halbrooks P.J. Mason A.B. Evolution of the transferrin family: conservation of residues associated with iron and anion binding Comp. Biochem. Physiol. B 142 2005 129 141
    • (2005) Comp. Biochem. Physiol. B , vol.142 , pp. 129-141
    • Lambert, L.A.1    Perri, H.2    Halbrooks, P.J.3    Mason, A.B.4
  • 27
    • 0018671415 scopus 로고
    • Distribution of iron between the binding sites of transferrin in serum: methods and results in normal human subjects
    • Leibman A. Aisen P. Distribution of iron between the binding sites of transferrin in serum: methods and results in normal human subjects Blood 53 1979 1058 1065
    • (1979) Blood , vol.53 , pp. 1058-1065
    • Leibman, A.1    Aisen, P.2
  • 28
    • 1942470608 scopus 로고    scopus 로고
    • Honey bee (Apis mellifera) transferrin-gene structure and the role of ecdysteroids in the developmental regulation of its expression
    • Nascimento A.M. Cuvillier-Hot V. Barchuk A.R. Simoes Z.L.P. Hartfelder K. Honey bee (Apis mellifera) transferrin-gene structure and the role of ecdysteroids in the developmental regulation of its expression Insect Biochem. Mol. Biol. 34 2004 415 424
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , pp. 415-424
    • Nascimento, A.M.1    Cuvillier-Hot, V.2    Barchuk, A.R.3    Simoes, Z.L.P.4    Hartfelder, K.5
  • 30
    • 13844262622 scopus 로고    scopus 로고
    • Intracellular generation of reactive oxygen species by mitochondria
    • Nohl H. Gille L. Staniek K. Intracellular generation of reactive oxygen species by mitochondria Biochem. Pharmacol. 69 2005 719 723
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 719-723
    • Nohl, H.1    Gille, L.2    Staniek, K.3
  • 31
    • 0030857377 scopus 로고    scopus 로고
    • Iron homeostasis, oxidative stress, and DNA damage
    • Meneghini R. Iron homeostasis, oxidative stress, and DNA damage Free Radic. Biol. Med. 23 1997 783 792
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 783-792
    • Meneghini, R.1
  • 32
    • 36749008309 scopus 로고
    • General characteristics of the white-spotted flower chafer, Protaetia brevitarsis reared in the laboratory
    • Park H.Y. Park S.S. Oh H.W. Kim J.I. General characteristics of the white-spotted flower chafer, Protaetia brevitarsis reared in the laboratory Korean J. Entomol. 24 1994 1 5
    • (1994) Korean J. Entomol. , vol.24 , pp. 1-5
    • Park, H.Y.1    Park, S.S.2    Oh, H.W.3    Kim, J.I.4
  • 33
    • 0032964289 scopus 로고    scopus 로고
    • Cellular iron metabolism
    • Ponka P. Cellular iron metabolism Kidney Int. Suppl. 69 1999 S2 S11
    • (1999) Kidney Int. Suppl. , vol.69 , pp. S2-S11
    • Ponka, P.1
  • 34
    • 0025786711 scopus 로고
    • Transfferin receptor expression and iron uptake in the injured and regenerating rat sciatic nerve
    • Raivich G. Graeber M.B. Gehrmann J. Kreutzberg G.W. Transfferin receptor expression and iron uptake in the injured and regenerating rat sciatic nerve Eur. J. Neurosci. 3 1991 919 927
    • (1991) Eur. J. Neurosci. , vol.3 , pp. 919-927
    • Raivich, G.1    Graeber, M.B.2    Gehrmann, J.3    Kreutzberg, G.W.4
  • 35
    • 0343247761 scopus 로고    scopus 로고
    • Comparison of Trichoplusia ni BTI-Tn-5B1-4 (High Five) and Spodoptera frugiperda Sf-9 insect cell line metabolism in suspension cultures
    • Rhiel M. Mitchell-Logean C.M. Murhammer D.W. Comparison of Trichoplusia ni BTI-Tn-5B1-4 (High Five) and Spodoptera frugiperda Sf-9 insect cell line metabolism in suspension cultures Biotechnol. Bioeng. 55 1997 909 920
    • (1997) Biotechnol. Bioeng. , vol.55 , pp. 909-920
    • Rhiel, M.1    Mitchell-Logean, C.M.2    Murhammer, D.W.3
  • 36
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • Stohs S.J. Bagchi D. Oxidative mechanisms in the toxicity of metal ions Free Radic. Biol. Med. 18 1995 321 336
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 321-336
    • Stohs, S.J.1    Bagchi, D.2
  • 37
    • 0037321923 scopus 로고    scopus 로고
    • Isolation and characterization of a termite transferrin gene up-regulation on infection
    • Thompson G.J. Crozier Y.C. Crozier R.H. Isolation and characterization of a termite transferrin gene up-regulation on infection Insect Mol. Biol. 12 2003 1 7
    • (2003) Insect Mol. Biol. , vol.12 , pp. 1-7
    • Thompson, G.J.1    Crozier, Y.C.2    Crozier, R.H.3
  • 38
    • 0033853838 scopus 로고    scopus 로고
    • Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress
    • Tsuji Y. Ayaki H. Whitman S.P. Morrow C.S. Torti S.V. Torti F.M. Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress Mol. Cell. Biol. 20 2000 5818 5827
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5818-5827
    • Tsuji, Y.1    Ayaki, H.2    Whitman, S.P.3    Morrow, C.S.4    Torti, S.V.5    Torti, F.M.6
  • 39
    • 24944515848 scopus 로고    scopus 로고
    • Solenopsis invicta transferrin: cDNA cloning, gene architecture, and up-regulation in response to Beauveria bassiana infection
    • Valles S.M. Pereira R.M. Solenopsis invicta transferrin: cDNA cloning, gene architecture, and up-regulation in response to Beauveria bassiana infection Gene 358 2005 60 66
    • (2005) Gene , vol.358 , pp. 60-66
    • Valles, S.M.1    Pereira, R.M.2
  • 40
    • 0035370768 scopus 로고    scopus 로고
    • Antioxidant defense systems of two lepidopteran insect cell lines
    • Wang Y. Oberley L.W. Murhammer D.Q. Antioxidant defense systems of two lepidopteran insect cell lines Free Radic. Biol. Med. 30 2001 1254 1262
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1254-1262
    • Wang, Y.1    Oberley, L.W.2    Murhammer, D.Q.3
  • 41
    • 0030817280 scopus 로고    scopus 로고
    • Mosquito transferrin, an acute-phase protein that is up-regulated upon infection
    • Yoshiga T. Hernandez V.P. Fallon A.M. Law J.H. Mosquito transferrin, an acute-phase protein that is up-regulated upon infection Proc. Natl. Acad. Sci. USA 94 1997 12337 12342
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12337-12342
    • Yoshiga, T.1    Hernandez, V.P.2    Fallon, A.M.3    Law, J.H.4
  • 42
    • 0033106306 scopus 로고    scopus 로고
    • Drosophila melanogaster — cloning, deduced protein sequence, expression during the life cycle, gene localization and up-regulation on bacterial infection
    • Yoshiga T. Georgieva T. Dunkov B.C. Harizanova N. Ralchev K. Law J.H. Drosophila melanogaster — cloning, deduced protein sequence, expression during the life cycle, gene localization and up-regulation on bacterial infection Eur. J. Biochem. 260 1999 414 420
    • (1999) Eur. J. Biochem. , vol.260 , pp. 414-420
    • Yoshiga, T.1    Georgieva, T.2    Dunkov, B.C.3    Harizanova, N.4    Ralchev, K.5    Law, J.H.6
  • 43
    • 0033388612 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA encoding a transferrin homologue from Bombyx mori
    • Yun E.Y. Kang S.W. Hwang J.S. Goo T.W. Kim S.H. Jin B.R. Kwon O.Y. Kim K.Y. Molecular cloning and characterization of a cDNA encoding a transferrin homologue from Bombyx mori Biol. Chem. 380 1999 1455 1459
    • (1999) Biol. Chem. , vol.380 , pp. 1455-1459
    • Yun, E.Y.1    Kang, S.W.2    Hwang, J.S.3    Goo, T.W.4    Kim, S.H.5    Jin, B.R.6    Kwon, O.Y.7    Kim, K.Y.8
  • 44
    • 0034610286 scopus 로고    scopus 로고
    • Genome-wide study of aging and oxidative stress response in Drosophila melanogaster
    • Zou S. Meadows S. Sharp L. Jan L.Y. Jan Y.N. Genome-wide study of aging and oxidative stress response in Drosophila melanogaster Proc. Natl. Acad. Sci. USA 97 2000 13726 13731
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13726-13731
    • Zou, S.1    Meadows, S.2    Sharp, L.3    Jan, L.Y.4    Jan, Y.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.