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Volumn 254, Issue 2, 1998, Pages 223-229

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

Author keywords

Ferritin; Iron; Iron regulatory protein; Iron responsive element; Lamprey

Indexed keywords

FERRITIN; IRON REGULATORY FACTOR;

EID: 0032103144     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2540223.x     Document Type: Article
Times cited : (33)

References (49)
  • 1
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P. M. & Arosio, P. (1996) The ferritins: molecular properties, iron storage function and cellular regulation, Biochim. Biophys. Acta 1275, 161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 4
    • 0023645028 scopus 로고
    • Differences in the regulation of messenger RNA for housekeeping and specialized-cell ferritin
    • Dickey, L. F., Sreedharan, S., Theil, E. C., Didsbury, J. R., Wang, Y.-H. & Thach, R. E. (1987) Differences in the regulation of messenger RNA for housekeeping and specialized-cell ferritin, J. Biol. Chem. 262, 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    Thach, R.E.6
  • 6
    • 0029861462 scopus 로고    scopus 로고
    • Molecular cloning and cold-inducible gene expression of ferritin H subunit isoforms in rainbow trout cells
    • Yamashita, M., Ojima, N. & Sakamoto, T. (1996) Molecular cloning and cold-inducible gene expression of ferritin H subunit isoforms in rainbow trout cells, J. Biol. Chem. 271, 26908-26913.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26908-26913
    • Yamashita, M.1    Ojima, N.2    Sakamoto, T.3
  • 7
    • 0023067301 scopus 로고
    • Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganisms
    • Theil, E. C. (1987) Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms, Annu. Rev. Biochem. 56, 289-315.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 9
    • 0023713448 scopus 로고
    • Binding of cytosolic protein to the iron-responsive element of human ferritin messenger RNA
    • Rouault, T. A., Hentze, M. W., Caughman, S. W., Harford, J. B. & Klausner, R. D. (1988) Binding of cytosolic protein to the iron-responsive element of human ferritin messenger RNA, Science 241, 1207-1210.
    • (1988) Science , vol.241 , pp. 1207-1210
    • Rouault, T.A.1    Hentze, M.W.2    Caughman, S.W.3    Harford, J.B.4    Klausner, R.D.5
  • 10
    • 0024361535 scopus 로고
    • Requirements for the translational repression of ferritin transcripts in wheat germ extracts by a 90-kDa protein from rabbit liver
    • Brown, P. H., Daniels-McQueen, S., Walden, W. E., Patino, M. M., Gaffield, L., Bielser, D. & Thach, R. E. (1989) Requirements for the translational repression of ferritin transcripts in wheat germ extracts by a 90-kDa protein from rabbit liver, J. Biol. Chem. 264, 13383-13386.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13383-13386
    • Brown, P.H.1    Daniels-McQueen, S.2    Walden, W.E.3    Patino, M.M.4    Gaffield, L.5    Bielser, D.6    Thach, R.E.7
  • 11
    • 0026756095 scopus 로고
    • Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: Role of the iron-sulfur cluster
    • Haile, D. J., Rouault, T. A., Tang, C. K., Chin, J., Harford, J. B. & Klausner, R. D. (1992) Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster, Proc. Natl Acad. Sci. USA 89, 7536-7540.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7536-7540
    • Haile, D.J.1    Rouault, T.A.2    Tang, C.K.3    Chin, J.4    Harford, J.B.5    Klausner, R.D.6
  • 12
    • 0028131454 scopus 로고
    • Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase acitivity
    • Guo, B., Yu, Y. & Leibold, E. A. (1994) Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase acitivity, J. Biol. Chem. 269, 24252-24260.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24252-24260
    • Guo, B.1    Yu, Y.2    Leibold, E.A.3
  • 13
    • 0028143071 scopus 로고
    • Molecular characterization of a second iron-responsive protein, iron-regulatory protein 2
    • Samaniego, F., Chin, J., Kazuhiro, I., Rouault, T. A. & Klausner, R. D. (1994) Molecular characterization of a second iron-responsive protein, iron-regulatory protein 2, J. Biol. Chem. 269, 30904-30910.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30904-30910
    • Samaniego, F.1    Chin, J.2    Kazuhiro, I.3    Rouault, T.A.4    Klausner, R.D.5
  • 14
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron-regulatory protein 2 by the proteasome
    • Guo, B., Phillips, J. D., Yu, Y. & Leibold, E. A. (1995) Iron regulates the intracellular degradation of iron-regulatory protein 2 by the proteasome, J. Biol. Chem. 270, 21645-21651.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 15
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron-regulatory protein 2
    • Iwai, K., Klausner, R. D. & Rouault, T. A. (1995) Requirements for iron-regulated degradation of the RNA binding protein, iron-regulatory protein 2, EMBO J. 14, 5350-5357.
    • (1995) EMBO J. , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 17
    • 0026059040 scopus 로고
    • Sequence and expression of the murine iron-responsive element-binding protein
    • Philpott, C. C., Rouault, T. A. & Klausner, R. D. (1991) Sequence and expression of the murine iron-responsive element-binding protein, Nucleic Acids Res. 19, 6333.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6333
    • Philpott, C.C.1    Rouault, T.A.2    Klausner, R.D.3
  • 18
    • 0026629837 scopus 로고
    • Cloning of a functional cDNA for the rabbit ferritin mRNA repressor protein
    • Patino, M. M. & Walden, W. E. (1992) Cloning of a functional cDNA for the rabbit ferritin mRNA repressor protein, J. Biol. Chem. 267, 19011-19016.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19011-19016
    • Patino, M.M.1    Walden, W.E.2
  • 19
    • 0026736834 scopus 로고
    • The iron-responsive element binding protein
    • Yu, Y., Radisky, E. & Leibold, E. A. (1992) The iron-responsive element binding protein, J. Biol. Chem. 267, 19005-19010.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19005-19010
    • Yu, Y.1    Radisky, E.2    Leibold, E.A.3
  • 20
    • 0027688031 scopus 로고
    • Identification and localization of two genes on the chicken Z chromosome: Implication of evolutionary conservation of the Z chromosome among avian species
    • Saitoh, Y., Ogawa, A., Hori, T., Kunita, R. & Mizuno, S. (1993) Identification and localization of two genes on the chicken Z chromosome: implication of evolutionary conservation of the Z chromosome among avian species, Chromosome Res. 1, 239-251.
    • (1993) Chromosome Res. , vol.1 , pp. 239-251
    • Saitoh, Y.1    Ogawa, A.2    Hori, T.3    Kunita, R.4    Mizuno, S.5
  • 21
    • 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. & Kühn, L. C. (1996) Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress, Proc. Natl Acad. Sci. USA 93, 8175-8182.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 22
    • 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, P. M. & 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
  • 23
    • 0029176319 scopus 로고
    • Isolation and characterization of mosquito ferritin and cloning of a cDNA that encodes one subunit
    • Dunkov, B. C., Zhang, D., Choumarov, K., Winzerling, J. J. & Law, J. H. (1995) Isolation and characterization of mosquito ferritin and cloning of a cDNA that encodes one subunit, Arch. Insect Biochem. Physiol. 29, 293-307.
    • (1995) Arch. Insect Biochem. Physiol. , vol.29 , pp. 293-307
    • Dunkov, B.C.1    Zhang, D.2    Choumarov, K.3    Winzerling, J.J.4    Law, J.H.5
  • 24
    • 0029875555 scopus 로고    scopus 로고
    • Purification and cDNA cloning of ferritin from the hepatopancreas of the freshwater crayfish Pacifastacus leniusculus
    • Huang, T., Law, J. H. & Söderhäll, K. (1996) Purification and cDNA cloning of ferritin from the hepatopancreas of the freshwater crayfish Pacifastacus leniusculus, Eur. J. Biochem. 236, 450-456.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 450-456
    • Huang, T.1    Law, J.H.2    Söderhäll, K.3
  • 25
    • 0029951578 scopus 로고    scopus 로고
    • Manduca sexta hemolymph ferritin: CDNA sequence and mRNA expression
    • Pham, D. Q.-D., Zhang, D., Hufnagel, D. H. & Winzerling, J. J. (1996) Manduca sexta hemolymph ferritin: cDNA sequence and mRNA expression, Gene 172, 255-259.
    • (1996) Gene , vol.172 , pp. 255-259
    • Pham, D.Q.-D.1    Zhang, D.2    Hufnagel, D.H.3    Winzerling, J.J.4
  • 26
    • 0025230751 scopus 로고
    • The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution
    • Rothenberger, S., Müllner, E. W. & Kühn, L. C. (1990) The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution, Nucl. Acids Res. 18, 1175-1179.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 1175-1179
    • Rothenberger, S.1    Müllner, E.W.2    Kühn, L.C.3
  • 27
    • 0029557688 scopus 로고
    • Succinate dehydrogenase b mRNA of Drosophila melanagaster has a functional iron-responsive element in its 5′-untranslated region
    • Kohler, S. A., Henderson, B. R. & Kühn, L. C. (1995) Succinate dehydrogenase b mRNA of Drosophila melanagaster 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    Kühn, L.C.3
  • 28
    • 0029899154 scopus 로고    scopus 로고
    • Translational regulation of mammalian and Drosophila citric acid cycle enzymes via iron-responsive elements
    • Gray, N. K., Pantopoulos, K., Dandekar, T. Acrell, B. A. C. & Hentze, M. W. (1996) Translational regulation of mammalian and Drosophila citric acid cycle enzymes via iron-responsive elements, Proc. Natl Acad. Sci. USA 93, 4925-4930.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4925-4930
    • Gray, N.K.1    Pantopoulos, K.2    Dandekar, T.3    Acrell, B.A.C.4    Hentze, M.W.5
  • 29
    • 0020515715 scopus 로고
    • Iron loading in the liver of parasistic adult lampreys, Petromyzon marinus L
    • Youson, J. H., Sargent, P. A. & Sidon, E. W. (1983) Iron loading in the liver of parasistic adult lampreys, Petromyzon marinus L., Am. J. Anat. 168, 37-49.
    • (1983) Am. J. Anat. , vol.168 , pp. 37-49
    • Youson, J.H.1    Sargent, P.A.2    Sidon, E.W.3
  • 30
    • 38249018243 scopus 로고
    • Occurrence and structure of iron inclusions in adipocytes of larval lampreys
    • Macey, D. J. & Youson, J. H. (1990) Occurrence and structure of iron inclusions in adipocytes of larval lampreys, Acta Zool. (Stockh.) 71, 69-76.
    • (1990) Acta Zool. (Stockh.) , vol.71 , pp. 69-76
    • Macey, D.J.1    Youson, J.H.2
  • 31
    • 0030993986 scopus 로고    scopus 로고
    • Distribution of iron during embryogenesis and early larval life in sea lampreys (Petromyzon marinus)
    • Tsioros, K. K. & Youson, J. H. (1997) Distribution of iron during embryogenesis and early larval life in sea lampreys (Petromyzon marinus), Can. J. Zool. 75, 137-147.
    • (1997) Can. J. Zool. , vol.75 , pp. 137-147
    • Tsioros, K.K.1    Youson, J.H.2
  • 32
    • 0020022059 scopus 로고
    • Iron levels and major iron binding proteins in the plasma of ammocoetes and adults of the Southern Hemisphere lamprey Geotria australis Gray
    • Macey, D. J., Webb, J. & Potter, I. C. (1982) Iron levels and major iron binding proteins in the plasma of ammocoetes and adults of the Southern Hemisphere lamprey Geotria australis Gray, Comp. Biochem. Physiol. 72A, 307-312.
    • (1982) Comp. Biochem. Physiol. , vol.72 A , pp. 307-312
    • Macey, D.J.1    Webb, J.2    Potter, I.C.3
  • 33
    • 15444347367 scopus 로고    scopus 로고
    • Identification of ferritin and transferrin during the life cycle of the lamprey Petromyzon marinus L
    • in the press
    • Standal, H., Heinig, J. A., Youson, J. H. & Andersen, Ø. (1998) Identification of ferritin and transferrin during the life cycle of the lamprey Petromyzon marinus L., J. Comp. Physiol. B., in the press.
    • (1998) J. Comp. Physiol. B.
    • Standal, H.1    Heinig, J.A.2    Youson, J.H.3    Andersen, Ø.4
  • 34
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 36
    • 0024212067 scopus 로고    scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleolide primer
    • Frohman, M. A., Dush, M. K. & Martin, G. R. (1998) Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleolide primer, Proc. Natl Acad. Sci. USA 85, 8998-9002.
    • (1998) Proc. Natl Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 37
    • 0032103264 scopus 로고    scopus 로고
    • Iron-regulatory protein-1 (IRP-1) is highly conserved in two invertebrate species. Characterization of IRP-1 homologues in Drosophila melanogaster and Caenorhabditis elegans
    • Muckenthaler, M., Gunkel, N., Frishman, D., Cyrklaff, A., Tomancak, P. & Hentze, M. W. (1998) Iron-regulatory protein-1 (IRP-1) is highly conserved in two invertebrate species. Characterization of IRP-1 homologues in Drosophila melanogaster and Caenorhabditis elegans, Eur. J. Biochem. 254, 230-237.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 230-237
    • Muckenthaler, M.1    Gunkel, N.2    Frishman, D.3    Cyrklaff, A.4    Tomancak, P.5    Hentze, M.W.6
  • 39
    • 0027131432 scopus 로고
    • Recombinant iron-regulatory factor functions as an iron-responsive-element-binding protein, a translational repressor and an aconitase. A functional assay for translational repression and direct demonstration of the iron switch
    • Gray, N. K., Quick, S., Goossen, B., Constable, A., Hirling, H., Kühn, L. C. & Hentze, M. W. (1993) Recombinant iron-regulatory factor functions as an iron-responsive-element-binding protein, a translational repressor and an aconitase. A functional assay for translational repression and direct demonstration of the iron switch, Eur. J. Biochem. 218, 657-667.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 657-667
    • Gray, N.K.1    Quick, S.2    Goossen, B.3    Constable, A.4    Hirling, H.5    Kühn, L.C.6    Hentze, M.W.7
  • 40
    • 0028929741 scopus 로고
    • Nitric oxide signaling to iron-regulatory protein: Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts
    • Pantopoulos, K. & Hentze, M. W. (1995) Nitric oxide signaling to iron-regulatory protein: Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts, Proc. Natl Acad. Sci. USA 92, 1267-1271
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1267-1271
    • Pantopoulos, K.1    Hentze, M.W.2
  • 41
    • 0024121621 scopus 로고
    • Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs
    • Leibold, E. A. & Munro, H. N. (1988) Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy-and light-subunit mRNAs, Proc. Natl Acad. Sci. USA 85, 2171-2175.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 42
    • 0022199982 scopus 로고
    • Structural and functional relationships of human H- and L-chains deduced from cDNAs clones
    • Boyd, D., Vecoli, C., Belcher, D. M., Jain, S. K. & Drysdale, J. W. (1985) Structural and functional relationships of human H-and L-chains deduced from cDNAs clones, J. Biol. Chem. 26, 11755-11761.
    • (1985) J. Biol. Chem. , vol.26 , pp. 11755-11761
    • Boyd, D.1    Vecoli, C.2    Belcher, D.M.3    Jain, S.K.4    Drysdale, J.W.5
  • 43
    • 0027398912 scopus 로고
    • Formation of an Fe(III)-tyrosinate complex during biomineralization of H-subunit ferritin
    • Waldo, G. S., Ling, J., Sanders-Loehr, J. & Theil, E. C. (1993) Formation of an Fe(III)-tyrosinate complex during biomineralization of H-subunit ferritin, Science 259, 796-798.
    • (1993) Science , vol.259 , pp. 796-798
    • Waldo, G.S.1    Ling, J.2    Sanders-Loehr, J.3    Theil, E.C.4
  • 44
    • 0026236758 scopus 로고
    • Isolation and characterization of ferritin from the liver of the rainbow trout (Salmo gairdneri R.)
    • Miguel, J. L., Pablos, M. I., Agapito, M. T. & Recio, J. M. (1991) Isolation and characterization of ferritin from the liver of the rainbow trout (Salmo gairdneri R.), Biochem. Cell Biol. 69, 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
  • 45
    • 0023854055 scopus 로고
    • 55Fe in juvenile adult lampreys, Petromyzon marinus L., following oral intubation of the isotope
    • 55Fe in juvenile adult lampreys, Petromyzon marinus L., following oral intubation of the isotope, J. Comp. Physiol. B. 157, 731-745.
    • (1988) J. Comp. Physiol. B. , vol.157 , pp. 731-745
    • Youson, J.H.1    Sargent, P.A.2    Barrett, A.3    Cheung, R.4
  • 46
    • 2342477708 scopus 로고
    • Distribution of ferric iron in juveniles of the lamprey Petromyzon marinus L
    • Youson, J. H. & Cheung, R. (1987) Distribution of ferric iron in juveniles of the lamprey Petromyzon marinus L., Can. J. Zool. 65, 1833-1841.
    • (1987) Can. J. Zool. , vol.65 , pp. 1833-1841
    • Youson, J.H.1    Cheung, R.2
  • 47
    • 0026587755 scopus 로고
    • Crystal structures of aconitase with isocitrate and nitroisocitrate bound
    • Lauble, H., Kennedy, M. C., Beinert, H. & Stout, C. D. (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
  • 48
    • 0026738940 scopus 로고
    • Mutational analysis of active site residues in pig heart aconitase
    • Zheng, L., Kennedy, M. C., Beinert, H. & Zalkin, H. (1992) Mutational analysis of active site residues in pig heart aconitase, J. Biol. Chem. 267, 7895-7903.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7895-7903
    • Zheng, L.1    Kennedy, M.C.2    Beinert, H.3    Zalkin, H.4
  • 49
    • 0028009430 scopus 로고
    • Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase
    • Hirling, H., Henderson, B. R. & Kühn, L. (1994) Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase, EMBO J. 13, 453-461.
    • (1994) EMBO J. , vol.13 , pp. 453-461
    • Hirling, H.1    Henderson, B.R.2    Kühn, L.3


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