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Volumn 303, Issue 1-2, 2007, Pages 201-209

Studies on resistance characteristic and cDNA sequence conservation of transferrin from crucian carp, Carassius auratus

Author keywords

Carassius auratus; cDNA sequence; Conservation; Iron ion (Fe3+); Resistance characteristic; Transferrin(Tf)

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BETA GLOBULIN; COMPLEMENTARY DNA; IRON; IRON BINDING PROTEIN; LACTATE DEHYDROGENASE; MESSENGER RNA; OXYGEN; TRANSFERRIN;

EID: 34547857759     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-007-9476-8     Document Type: Article
Times cited : (4)

References (41)
  • 2
    • 34547855606 scopus 로고
    • Studies on the serum capacity of serum to bind iron
    • Holmberg CG, Lauerll CB (1945) Studies on the serum capacity of serum to bind iron. Acta Physiol Scand 10:227-228
    • (1945) Acta Physiol Scand , vol.10 , pp. 227-228
    • Holmberg, C.G.1    Lauerll, C.B.2
  • 3
    • 34547863255 scopus 로고
    • The stability constants of the iron-transferrin complex
    • Benson DB (1962) The stability constants of the iron-transferrin complex. Biochem Biophys Res Commun 8:56-60
    • (1962) Biochem Biophys Res Commun , vol.8 , pp. 56-60
    • Benson, D.B.1
  • 4
    • 0001900119 scopus 로고
    • Relative resistances of three transferrin genotypes of Coho Salmon (Oncorhynchus kisutch) and their hematological responses to bacterial kidney disease
    • Suzumoto BK, Schreck CB, McIntyre JD (1977) Relative resistances of three transferrin genotypes of Coho Salmon (Oncorhynchus kisutch) and their hematological responses to bacterial kidney disease. J Fish Res Board Can 34:1-7
    • (1977) J Fish Res Board Can , vol.34 , pp. 1-7
    • Suzumoto, B.K.1    Schreck, C.B.2    McIntyre, J.D.3
  • 5
    • 0033588524 scopus 로고    scopus 로고
    • Evaluation of a 74-kDa transferrin-binding protein from Moraxella (Branhamella) catarrhalis as a vaccine candidate
    • Chen D, McMichael JC, VanDerMeid KR et al (1999) Evaluation of a 74-kDa transferrin-binding protein from Moraxella (Branhamella) catarrhalis as a vaccine candidate. Vaccine 18:109-118
    • (1999) Vaccine , vol.18 , pp. 109-118
    • Chen, D.1    McMichael, J.C.2    VanDerMeid, K.R.3
  • 6
    • 0037409637 scopus 로고    scopus 로고
    • Transferrin and innate immune response of fish: Identification of a novel mechanism of macrophage activation
    • Stafford JL, Belosevic M (2003) Transferrin and innate immune response of fish: Identification of a novel mechanism of macrophage activation. Dev Comp Immunol 27:539-554
    • (2003) Dev Comp Immunol , vol.27 , pp. 539-554
    • Stafford, J.L.1    Belosevic, M.2
  • 7
    • 33646363763 scopus 로고    scopus 로고
    • Iron-withholding strategy in innate immunity
    • Onga ST, Hob JZS, Hoc B et al (2006) Iron-withholding strategy in innate immunity. Immunobiology 211:295-314
    • (2006) Immunobiology , vol.211 , pp. 295-314
    • Onga, S.T.1    Hob, J.Z.S.2    Hoc, B.3
  • 8
    • 34547857119 scopus 로고    scopus 로고
    • Study and development on transferrins
    • Long H, Li G, Zheng Y (2001) Study and development on transferrins. J Bioeng Dev 21:32-39
    • (2001) J Bioeng Dev , vol.21 , pp. 32-39
    • Long, H.1    Li, G.2    Zheng, Y.3
  • 9
    • 33745229698 scopus 로고    scopus 로고
    • Isolation, cloning and sequencing of transferrins from red-eared turtle, African ostrich, and turkey
    • Ciuraszkiewicz J, Olczak M, Watorek W (2006) Isolation, cloning and sequencing of transferrins from red-eared turtle, African ostrich, and turkey. Comp Biochem Physiol B 144:301-310
    • (2006) Comp Biochem Physiol B , vol.144 , pp. 301-310
    • Ciuraszkiewicz, J.1    Olczak, M.2    Watorek, W.3
  • 10
    • 0026458234 scopus 로고
    • Regulation of transferrin gene expression
    • Zakin MM (1992) Regulation of transferrin gene expression. FASEB J 6:3252-3258
    • (1992) FASEB J , vol.6 , pp. 3252-3258
    • Zakin, M.M.1
  • 11
    • 0030040549 scopus 로고    scopus 로고
    • Distinct positive and negative regulatory elements control neuronal and hepatic transcription of the human transferrin gene
    • Sawaya BE, Aunis D, Schaeffer E (1996) Distinct positive and negative regulatory elements control neuronal and hepatic transcription of the human transferrin gene. J Neurosci Res 43:261-272
    • (1996) J Neurosci Res , vol.43 , pp. 261-272
    • Sawaya, B.E.1    Aunis, D.2    Schaeffer, E.3
  • 12
    • 0030792094 scopus 로고    scopus 로고
    • Oxygen-regulated transferrin expression is mediated by hypoxiainducible factor-1
    • Rolfs A, Kvietikova I, Gassmann M et al (1997) Oxygen-regulated transferrin expression is mediated by hypoxiainducible factor-1. J Biol Chem 272:20055-20062
    • (1997) J Biol Chem , vol.272 , pp. 20055-20062
    • Rolfs, A.1    Kvietikova, I.2    Gassmann, M.3
  • 13
    • 0033230181 scopus 로고    scopus 로고
    • HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation
    • Bianchi L, Tacchini L, Cairo G (1999) HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation. Nucleic Acids Res 27:4223-4227
    • (1999) Nucleic Acids Res , vol.27 , pp. 4223-4227
    • Bianchi, L.1    Tacchini, L.2    Cairo, G.3
  • 14
    • 0024523006 scopus 로고
    • Cell type-specific expression of the human transferrin gene
    • Schaeffer E, Boissier F, Py MC et al (1989) Cell type-specific expression of the human transferrin gene. J Biol Chem 264:7153-7160
    • (1989) J Biol Chem , vol.264 , pp. 7153-7160
    • Schaeffer, E.1    Boissier, F.2    Py, M.C.3
  • 15
    • 0025823885 scopus 로고
    • The enhancer of the human transferrin gene is organized in two structural and functional domains
    • Boissier F, Corinne AG, Schaeffer E et al (1991) The enhancer of the human transferrin gene is organized in two structural and functional domains. J Biol Chem 266:9822-9828
    • (1991) J Biol Chem , vol.266 , pp. 9822-9828
    • Boissier, F.1    Corinne, A.G.2    Schaeffer, E.3
  • 16
    • 24344475974 scopus 로고    scopus 로고
    • Evolution of the transferrin family: Conservation of residues associated with iron and anion binding
    • Lambert LA, Perri H, Halbrooks PJ et al (2005) Evolution of the transferrin family: Conservation of residues associated with iron and anion binding. Comp Biochem Physiol B 142:129-141
    • (2005) Comp Biochem Physiol B , vol.142 , pp. 129-141
    • Lambert, L.A.1    Perri, H.2    Halbrooks, P.J.3
  • 17
    • 34547886241 scopus 로고
    • The role of a metal-transferrin-transferrin-receptor mechanism if the in vitro uptake of metals by human lymphoblasts (WIL-2)
    • Duffield J, Planas-Bohne F, Taylor DM (1983) The role of a metal-transferrin-transferrin-receptor mechanism if the in vitro uptake of metals by human lymphoblasts (WIL-2). Inorganica Chim Acta 79:223-224
    • (1983) Inorganica Chim Acta , vol.79 , pp. 223-224
    • Duffield, J.1    Planas-Bohne, F.2    Taylor, D.M.3
  • 19
    • 18744376270 scopus 로고    scopus 로고
    • Sinauer Associates Inc., Massachusetts, Sunderland
    • Hill RW, Wyse GA, Anderson M (2004) Animal physiology. Sinauer Associates Inc., Massachusetts, Sunderland, pp 577-605
    • (2004) Animal Physiology , pp. 577-605
    • Hill, R.W.1    Wyse, G.A.2    Anderson, M.3
  • 20
    • 33751072118 scopus 로고    scopus 로고
    • Baffled by bafilomycin: An anticancer agent that induces hypoxia-inducible factor-1α expression
    • Semenza GL (2006) Baffled by bafilomycin: An anticancer agent that induces hypoxia-inducible factor-1α expression. Mol Pharmacol 70:1841-1843
    • (2006) Mol Pharmacol , vol.70 , pp. 1841-1843
    • Semenza, G.L.1
  • 21
    • 33746206425 scopus 로고    scopus 로고
    • Comparison of the serum ferritin and percentage of transferrin saturation as exposure markers of iron-driven oxidative stress-related disease outcomes
    • Lee D-H, Zacharski LR, Jacobs DR (2006) Comparison of the serum ferritin and percentage of transferrin saturation as exposure markers of iron-driven oxidative stress-related disease outcomes. Am Heart J 151:1247.e1-1247.e7
    • (2006) Am Heart J , vol.151
    • Lee, D.-H.1    Zacharski, L.R.2    Jacobs, D.R.3
  • 23
    • 0002562771 scopus 로고
    • Some physicochemical properties of transferrins in brook trout
    • Herschberger WK (1970) Some physicochemical properties of transferrins in brook trout. Trans Amer Fish Soc 99:207-218
    • (1970) Trans Amer Fish Soc , vol.99 , pp. 207-218
    • Herschberger, W.K.1
  • 24
    • 0014019313 scopus 로고
    • Serum transferrins in some gadoid fishes
    • Møller D, Naevdal G (1966) Serum transferrins in some gadoid fishes. Nature 210:317-318
    • (1966) Nature , vol.210 , pp. 317-318
    • Møller, D.1    Naevdal, G.2
  • 25
    • 34547906221 scopus 로고
    • Oxygen consumption rates of Grass carp, sliver carp and bighead carp
    • Chen N-S, Shi Q-F (1995) Oxygen consumption rates of Grass carp, sliver carp and bighead carp. Acta Zoologica Sinica 7:43-57
    • (1995) Acta Zoologica Sinica , vol.7 , pp. 43-57
    • Chen, N.-S.1    Shi, Q.-F.2
  • 26
    • 0000123372 scopus 로고
    • Cloning, nucleotide sequence analysis, and characterization of cDNA for medaka (Oryzias latipes) transferrin
    • Hirono I, Uchiyama T, Aoki T (1995) Cloning, nucleotide sequence analysis, and characterization of cDNA for medaka (Oryzias latipes) transferrin. J Mar Biotechnol 3:193-198
    • (1995) J Mar Biotechnol , vol.3 , pp. 193-198
    • Hirono, I.1    Uchiyama, T.2    Aoki, T.3
  • 27
    • 33750943170 scopus 로고    scopus 로고
    • Integrating iron and oxygen/antioxidant signals via a combinatorial array of DNA - (Antioxidant response elements) and mRNA (iron responsive elements) sequences
    • Elizabeth CT (2006) Integrating iron and oxygen/antioxidant signals via a combinatorial array of DNA - (antioxidant response elements) and mRNA (iron responsive elements) sequences. J Inorg Biochem 100:2074-2078
    • (2006) J Inorg Biochem , vol.100 , pp. 2074-2078
    • Elizabeth, C.T.1
  • 28
    • 33745936535 scopus 로고    scopus 로고
    • Differential response of iron metabolism to oxidative stress generated by antimycin A and nitrofurantoin
    • Brigitte S, Teresa T, Birgit K et al (2006) Differential response of iron metabolism to oxidative stress generated by antimycin A and nitrofurantoin. Biochimie 88:575-581
    • (2006) Biochimie , vol.88 , pp. 575-581
    • Brigitte, S.1    Teresa, T.2    Birgit, K.3
  • 29
    • 0035847120 scopus 로고    scopus 로고
    • Effects of hypoxia and iron on iron regulatory protein-1 activity and the ferritin synthesis in mouse peritoneal macrophages
    • Kuriyama-Matsumura K, Sato H, Suzuki M et al (2001) Effects of hypoxia and iron on iron regulatory protein-1 activity and the ferritin synthesis in mouse peritoneal macrophages. Biochim Biophys Acta 1544:370-377
    • (2001) Biochim Biophys Acta , vol.1544 , pp. 370-377
    • Kuriyama-Matsumura, K.1    Sato, H.2    Suzuki, M.3
  • 30
    • 0043157360 scopus 로고    scopus 로고
    • Identification of differentially expressed genes of acute hypoxia-treated HepG2 cells and hypoxia-acclimatized HepG2 cells
    • Wang J-H, Shan Y-J, Cong Y-W et al (2003) Identification of differentially expressed genes of acute hypoxia-treated HepG2 cells and hypoxia-acclimatized HepG2 cells. Acta Biochim Biophys Sin 55:324-330
    • (2003) Acta Biochim Biophys Sin , vol.55 , pp. 324-330
    • Wang, J.-H.1    Shan, Y.-J.2    Cong, Y.-W.3
  • 31
    • 0035745978 scopus 로고    scopus 로고
    • Mechanisms of cell survival in hypoxia and hypothermia
    • Boutilier RG (2001) Mechanisms of cell survival in hypoxia and hypothermia. J Exp Biol 204:3171-3181
    • (2001) J Exp Biol , vol.204 , pp. 3171-3181
    • Boutilier, R.G.1
  • 32
    • 0141814610 scopus 로고    scopus 로고
    • Gene expression profile of zebrafish exposed to hypoxia during development
    • Ton C, Stamatiou D, Liew C-C (2003) Gene expression profile of zebrafish exposed to hypoxia during development. Physiol Genomics 13:97-106
    • (2003) Physiol Genomics , vol.13 , pp. 97-106
    • Ton, C.1    Stamatiou, D.2    Liew, C.-C.3
  • 33
    • 23744473294 scopus 로고    scopus 로고
    • Gene expression after freshwater transfer in gills and opercular epithelia of killifish: Insight into divergent mechanisms of ion transport
    • Scott GR, Claiborne JB, Edwards SL et al (2005) Gene expression after freshwater transfer in gills and opercular epithelia of killifish: insight into divergent mechanisms of ion transport. J Exp Biol 208:2719-2729
    • (2005) J Exp Biol , vol.208 , pp. 2719-2729
    • Scott, G.R.1    Claiborne, J.B.2    Edwards, S.L.3
  • 34
    • 33751194112 scopus 로고    scopus 로고
    • Oxygen availability regulates metabolism and gene expression in trout hepatocyte cultures
    • Rissanen E, Tranberg HK, Nikinmaa M (2006) Oxygen availability regulates metabolism and gene expression in trout hepatocyte cultures. Am J Physiol Regul Integr Comp Physiol 291:R1507-R1515
    • (2006) Am J Physiol Regul Integr Comp Physiol , vol.291
    • Rissanen, E.1    Tranberg, H.K.2    Nikinmaa, M.3
  • 35
    • 33750320043 scopus 로고    scopus 로고
    • Metabolic capacity regulates iron homeostasis in endothelial cells
    • Carraway MS, Suliman HB, Madden MC et al (2006) Metabolic capacity regulates iron homeostasis in endothelial cells. Free Radic Biol Med 41:1662-1669
    • (2006) Free Radic Biol Med , vol.41 , pp. 1662-1669
    • Carraway, M.S.1    Suliman, H.B.2    Madden, M.C.3
  • 36
    • 27744475649 scopus 로고    scopus 로고
    • Metabolic arrest and its regulation in anoxic eel hepatocytes
    • Busk M, Boutilier RG (2005) Metabolic arrest and its regulation in anoxic eel hepatocytes. Physiol Biochem Zool 78:926-936
    • (2005) Physiol Biochem Zool , vol.78 , pp. 926-936
    • Busk, M.1    Boutilier, R.G.2
  • 37
    • 33748152298 scopus 로고    scopus 로고
    • Oncological implications of hypoxia inducible factor-1a (HIF-1a) expression
    • O'Donnell JL, Joyce MR, Shannon AM et al (2006) Oncological implications of hypoxia inducible factor-1a (HIF-1a) expression. Cancer Treat Rev 32:407-416
    • (2006) Cancer Treat Rev , vol.32 , pp. 407-416
    • O'Donnell, J.L.1    Joyce, M.R.2    Shannon, A.M.3
  • 38
    • 0018850440 scopus 로고
    • Iron transport and storage proteins
    • Aisen P, Listowsky I (1980) Iron transport and storage proteins. Annu Rev Biochem 49:357-393
    • (1980) Annu Rev Biochem , vol.49 , pp. 357-393
    • Aisen, P.1    Listowsky, I.2
  • 39
    • 34547891974 scopus 로고
    • Studies on transferrin structure domains and transferrin evolution
    • Hou X-y, Feng Y-m (1988) Studies on transferrin structure domains and transferrin evolution. Prog Biochem Biophys 15:270-283
    • (1988) Prog Biochem Biophys , vol.15 , pp. 270-283
    • Hou, X.-Y.1    Feng, Y.-M.2
  • 40
    • 0005196482 scopus 로고
    • Studies on structures and functions of transferrins VI: Studies on comparison of binding abilities receptors and antibodies and their special absorbing spectras between human transferrin and animal serum transferrin of different species and genus
    • Zhang X-T, Ji R-h, Shen Z-m et al (1991) Studies on structures and functions of transferrins VI: Studies on comparison of binding abilities receptors and antibodies and their special absorbing spectras between human transferrin and animal serum transferrin of different species and genus. Acta Biochim Biophys Sin 23:134-139
    • (1991) Acta Biochim Biophys Sin , vol.23 , pp. 134-139
    • Zhang, X.-T.1    Ji, R.-H.2    Shen, Z.-M.3
  • 41
    • 0019332452 scopus 로고
    • The effects of trypsin digestion on the structure and iron-donating properties of transferrins from several species
    • Espara I, Brock JH (1980) The effects of trypsin digestion on the structure and iron-donating properties of transferrins from several species. Biochim Biophys Acta 622:297-307
    • (1980) Biochim Biophys Acta , vol.622 , pp. 297-307
    • Espara, I.1    Brock, J.H.2


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