메뉴 건너뛰기




Volumn 336, Issue 3, 2013, Pages 134-141

Middle ferritin genes from the icefish Chionodraco rastrospinosus: Comparative analysis and evolution of fish ferritins

Author keywords

Antarctic fish; Ferritin; Gene expression; Phylogeny

Indexed keywords

CERULOPLASMIN; FERRIC HYDROXIDE; FERRITIN; MESSENGER RNA;

EID: 84877579847     PISSN: 16310691     EISSN: 17683238     Source Type: Journal    
DOI: 10.1016/j.crvi.2013.03.003     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • P.M. Harrison, and P. Arosio The ferritins: molecular properties, iron storage function and cellular regulation Biochim. Biophys. Acta 1275 1996 161 203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 2
    • 0037101879 scopus 로고    scopus 로고
    • Ferritin, iron homeostasis, and oxidative damage
    • P. Arosio, and S. Levi Ferritin, iron homeostasis, and oxidative damage Free Rad. Biol. Med. 33 2002 457 463
    • (2002) Free Rad. Biol. Med. , vol.33 , pp. 457-463
    • Arosio, P.1    Levi, S.2
  • 3
    • 77953809618 scopus 로고    scopus 로고
    • The iron redox and hydrolysis chemistry of the ferritins
    • F. Bou-Abdallah The iron redox and hydrolysis chemistry of the ferritins Biochim. Biophys. Acta 1800 2010 719 731
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 719-731
    • Bou-Abdallah, F.1
  • 4
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: A family of molecules for iron storage, antioxidation and more
    • P. Arosio, R. Ingrassia, and P. Cavadini Ferritins: a family of molecules for iron storage, antioxidation and more Biochim. Biophys. Acta 1790 2009 589 599
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 6
    • 14744304889 scopus 로고    scopus 로고
    • Unique iron binding and oxidation properties of human mitochondrial ferritin: A comparative analysis with human H-chain ferritin
    • F. Bou-Abdallaha, P. Santambrogio, S. Levi, P. Arosio, and N.D. Chasteen Unique iron binding and oxidation properties of human mitochondrial ferritin: a comparative analysis with human H-chain ferritin J. Mol. Biol. 347 2005 543 554
    • (2005) J. Mol. Biol. , vol.347 , pp. 543-554
    • Bou-Abdallaha, F.1    Santambrogio, P.2    Levi, S.3    Arosio, P.4    Chasteen, N.D.5
  • 9
    • 0030020621 scopus 로고    scopus 로고
    • Evidence that the specificity of iron incorporation into homopolymers of human ferritin L- and H-chains is conferred by the nucleation and ferroxidase centres
    • P. Santambrogio, S. Levi, A. Cozzi, B. Corsi, and P. Arosio Evidence that the specificity of iron incorporation into homopolymers of human ferritin L- and H-chains is conferred by the nucleation and ferroxidase centres Biochem. J. 314 1996 139 144
    • (1996) Biochem. J. , vol.314 , pp. 139-144
    • Santambrogio, P.1    Levi, S.2    Cozzi, A.3    Corsi, B.4    Arosio, P.5
  • 10
    • 0000171802 scopus 로고    scopus 로고
    • Ferritin
    • A. Messerschmidt, R. Huber, K. Wieghardt, T. Poulos, Chichester Wiley
    • E.C. Theil Ferritin A. Messerschmidt, R. Huber, K. Wieghardt, T. Poulos, Handbook of Metalloproteins 2010 Chichester Wiley 771 781
    • (2010) Handbook of Metalloproteins , pp. 771-781
    • Theil, E.C.1
  • 11
    • 77953812371 scopus 로고    scopus 로고
    • X-ray structures of ferritins and related proteins
    • R.R. Crichton, and J.P. Declercq X-ray structures of ferritins and related proteins Biochim. Biophys. Acta 1800 2010 706 718
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 706-718
    • Crichton, R.R.1    Declercq, J.P.2
  • 12
    • 0023645028 scopus 로고
    • Differences in the regulation of messenger RNA for housekeeping and specialized-cell ferritin. A comparison of three distinct ferritin complementary DNAs, the corresponding subunits, and identification of the first processed in Amphibia
    • L.F. Dickey, S. Sreedharan, E.C. Theil, J.R. Didsbury, Y.H. Wang, and R.E. Kaufman Differences in the regulation of messenger RNA for housekeeping and specialized-cell ferritin. A comparison of three distinct ferritin complementary DNAs, the corresponding subunits, and identification of the first processed in Amphibia J. Biol. Chem. 262 1987 7901 7907
    • (1987) J. Biol. Chem. , vol.262 , pp. 7901-7907
    • Dickey, L.F.1    Sreedharan, S.2    Theil, E.C.3    Didsbury, J.R.4    Wang, Y.H.5    Kaufman, R.E.6
  • 14
    • 0032103144 scopus 로고    scopus 로고
    • Regulation of iron metabolism in the sanguivore lamprey Lampetra fluviatilis. Molecular cloning of two ferritin subunits and two iron-regulatory proteins (IRP) reveals evolutionary conservation of the iron-regulatory element (IRE)/IRP regulatory system
    • ∅. Andersen, K. Pantopoulos, H.T. Kao, M. Muckenthaler, J.H. Youson, and V. Pieribone Regulation of iron metabolism in the sanguivore lamprey Lampetra fluviatilis. Molecular cloning of two ferritin subunits and two iron-regulatory proteins (IRP) reveals evolutionary conservation of the iron-regulatory element (IRE)/IRP regulatory system Eur. J. Biochem. 254 1998 223 229
    • (1998) Eur. J. Biochem. , vol.254 , pp. 223-229
    • Andersen, O.1    Pantopoulos, K.2    Kao, H.T.3    Muckenthaler, M.4    Youson, J.H.5    Pieribone, V.6
  • 16
    • 77951135184 scopus 로고    scopus 로고
    • Gene cloning and characterization of ferritin H and M subunits from large yellow croaker (Pseudosciaena crocea)
    • X. Zhang, W. Wei, H. Wu, H. Xu, K. Chang, and Y. Zhang Gene cloning and characterization of ferritin H and M subunits from large yellow croaker (Pseudosciaena crocea) Fish Shellfish Immunol. 28 2010 735 742
    • (2010) Fish Shellfish Immunol. , vol.28 , pp. 735-742
    • Zhang, X.1    Wei, W.2    Wu, H.3    Xu, H.4    Chang, K.5    Zhang, Y.6
  • 18
    • 0026236758 scopus 로고
    • Isolation and characterization of ferritin from the liver of the rainbow trout (Salmo gairdneri R.)
    • J.L. Miguel, M.I. Pablos, M.T. Agapito, and J.M. Recio Isolation and characterization of ferritin from the liver of the rainbow trout (Salmo gairdneri R.) Biochem. Cell Biol. 69 1991 735 741
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 735-741
    • Miguel, J.L.1    Pablos, M.I.2    Agapito, M.T.3    Recio, J.M.4
  • 19
    • 34250898026 scopus 로고    scopus 로고
    • Structure and expression of genes involved in transport and storage of iron in red-blooded and hemoglobin-less Antarctic notothenioids
    • R. Scudiero, F. Trinchella, M. Riggio, and E. Parisi Structure and expression of genes involved in transport and storage of iron in red-blooded and hemoglobin-less Antarctic notothenioids Gene 397 2007 1 11
    • (2007) Gene , vol.397 , pp. 1-11
    • Scudiero, R.1    Trinchella, F.2    Riggio, M.3    Parisi, E.4
  • 20
    • 63049138087 scopus 로고    scopus 로고
    • Iron metabolism genes in Antarctic notothenioids: A review
    • R. Scudiero, F. Trinchella, and E. Parisi Iron metabolism genes in Antarctic notothenioids: a review Mar. Genomics 1 2008 79 85
    • (2008) Mar. Genomics , vol.1 , pp. 79-85
    • Scudiero, R.1    Trinchella, F.2    Parisi, E.3
  • 21
    • 84877576481 scopus 로고    scopus 로고
    • Iron-binding proteins in fishes of the Southern Ocean
    • L.V. Berhardt, Nova Science Publisher Hauppauge NY
    • R. Scudiero, and F. Trinchella Iron-binding proteins in fishes of the Southern Ocean L.V. Berhardt, Advances in Medicine and Biology vol 36 2012 Nova Science Publisher Hauppauge NY 49 66
    • (2012) Advances in Medicine and Biology , vol.36 , pp. 49-66
    • Scudiero, R.1    Trinchella, F.2
  • 22
  • 24
    • 84864754580 scopus 로고    scopus 로고
    • Metallothionein primary structure in amphibians: Insights from comparative evolutionary analysis in vertebrates
    • F. Trinchella, M.G. Esposito, and R. Scudiero Metallothionein primary structure in amphibians: insights from comparative evolutionary analysis in vertebrates C. R. Biol. 335 2012 480 487
    • (2012) C. R. Biol. , vol.335 , pp. 480-487
    • Trinchella, F.1    Esposito, M.G.2    Scudiero, R.3
  • 25
    • 3042830460 scopus 로고    scopus 로고
    • Gene amplification and cold adaptation of pepsin in Antarctic fish. A possible strategy for food digestion at low temperature
    • V. Carginale, F. Trinchella, C. Capasso, R. Scudiero, and E. Parisi Gene amplification and cold adaptation of pepsin in Antarctic fish. A possible strategy for food digestion at low temperature Gene 336 2004 195 205
    • (2004) Gene , vol.336 , pp. 195-205
    • Carginale, V.1    Trinchella, F.2    Capasso, C.3    Scudiero, R.4    Parisi, E.5
  • 27
    • 74549125386 scopus 로고    scopus 로고
    • SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building
    • M. Gouy, S. Guindon, and O. Gascuel SeaView version 4: a multiplatform graphical user interface for sequence alignment and phylogenetic tree building Mol. Biol. Evol. 27 2010 221 224
    • (2010) Mol. Biol. Evol. , vol.27 , pp. 221-224
    • Gouy, M.1    Guindon, S.2    Gascuel, O.3
  • 28
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolution genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • K. Tamura, D. Peterson, N. Peterson, G. Stecher, M. Nei, and S. Kumar MEGA5: molecular evolution genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods Mol. Biol. Evol. 28 2011 2731 2739
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 29
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: Selection of best-fit models of protein evolution
    • F. Abascal, R. Zardoya, and D. Posada ProtTest: selection of best-fit models of protein evolution Bioinformatics 21 2005 2104 2105
    • (2005) Bioinformatics , vol.21 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 30
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • J.P. Huelsenbeck, and F. Ronquist MRBAYES: Bayesian inference of phylogenetic trees Bioinformatics 17 2001 754 755
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 31
    • 84860620069 scopus 로고    scopus 로고
    • Molecular adaptations in Antarctic fish and marine microorganisms
    • D. Giordano, R. Russo, G. di Prisco, and C. Verde Molecular adaptations in Antarctic fish and marine microorganisms Mar.Genomics 6 2012 1 6
    • (2012) Mar.Genomics , vol.6 , pp. 1-6
    • Giordano, D.1    Russo, R.2    Di Prisco, G.3    Verde, C.4
  • 33
    • 0001063415 scopus 로고
    • Vertebrates without erythrocytes and blood pigment
    • J.T. Ruud Vertebrates without erythrocytes and blood pigment Nature 173 1954 848 850
    • (1954) Nature , vol.173 , pp. 848-850
    • Ruud, J.T.1
  • 34
    • 42949161697 scopus 로고    scopus 로고
    • The adaptation of polar fishes to climatic changes: Structure, function and phylogeny of haemoglobin
    • C. Verde, D. Giordano, and G. di Prisco The adaptation of polar fishes to climatic changes: structure, function and phylogeny of haemoglobin IUBMB Life 60 2008 29 40
    • (2008) IUBMB Life , vol.60 , pp. 29-40
    • Verde, C.1    Giordano, D.2    Di Prisco, G.3
  • 35
    • 0014947695 scopus 로고
    • Oxygen uptake and circulation by a hemoglobinless Antarctic fish (Chaenocephalus aceratus, Lonnberg) compared with three red-blooded Antarctic fish
    • G.F. Holeton Oxygen uptake and circulation by a hemoglobinless Antarctic fish (Chaenocephalus aceratus, Lonnberg) compared with three red-blooded Antarctic fish Comp. Biochem. Physiol. 34 1970 457 471
    • (1970) Comp. Biochem. Physiol. , vol.34 , pp. 457-471
    • Holeton, G.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.