메뉴 건너뛰기




Volumn 90, Issue 7, 2011, Pages 1489-1495

Structural and functional analyses of chicken liver ferritin

Author keywords

Ferritin; H subunit; Heme; Iron; L subunit

Indexed keywords

BOVINAE; MAMMALIA;

EID: 79959347135     PISSN: 00325791     EISSN: 15253171     Source Type: Journal    
DOI: 10.3382/ps.2010-01307     Document Type: Article
Times cited : (11)

References (37)
  • 3
    • 0019482785 scopus 로고
    • Adaptive responses of rat tissue isoferritins to iron administration. Changes in subunit synthesis, isoferritin abundance, and capacity for iron storage
    • Bomford, A., C. Conlon-Hollingshead, and H. N. Munro. 1981. Adaptive responses of rat tissue isoferritins to iron administration. Changes in subunit synthesis, isoferritin abundance, and capacity for iron storage. J. Biol. Chem. 256:948-955.
    • (1981) J. Biol. Chem , vol.256 , pp. 948-955
    • Bomford, A.1    Conlon-Hollingshead, C.2    Munro, H.N.3
  • 4
    • 0022199982 scopus 로고
    • Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones
    • Boyd, D., C. Vecoli, D. M. Belcher, S. K. Jain, and J. W. Drysdale. 1985. Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. J. Biol. Chem. 260:11755-11761.
    • (1985) J. Biol. Chem , vol.260 , pp. 11755-11761
    • Boyd, D.1    Vecoli, C.2    Belcher, D.M.3    Jain, S.K.4    Drysdale, J.W.5
  • 5
    • 0031670727 scopus 로고    scopus 로고
    • Nuclear ferritin protects DNA from UV damage in corneal epithelial cells
    • Cai, C. X., D. E. Birk, and T. F. Linsenmayer. 1998. Nuclear ferritin protects DNA from UV damage in corneal epithelial cells. Mol. Biol. Cell 9:1037-1051.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1037-1051
    • Cai, C.X.1    Birk, D.E.2    Linsenmayer, T.F.3
  • 6
    • 0030723765 scopus 로고    scopus 로고
    • Remarkable ability of horse spleen apoferritin to demetallate hemin and to metallate protoporphyrin IX as a function of pH
    • Crichton, R. R., J. A. Soruco, F. Roland, M. A. Michaux, B. Gallois, G. Précigoux, J. P. Mahy, and D. Mansuy. 1997. Remarkable ability of horse spleen apoferritin to demetallate hemin and to metallate protoporphyrin IX as a function of pH. Biochemistry 36:15049-15054.
    • (1997) Biochemistry , vol.36 , pp. 15049-15054
    • Crichton, R.R.1    Soruco, J.A.2    Roland, F.3    Michaux, M.A.4    Gallois, B.5    Précigoux, G.6    Mahy, J.P.7    Mansuy, D.8
  • 7
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Method and application to human serum proteins
    • Davis, B. J. 1964. Disc electrophoresis. II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121:404-427.
    • (1964) Ann. N. Y. Acad. Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 8
    • 0022127478 scopus 로고
    • Isolation and purification of duck liver ferritin
    • Díez, J. M., M. T. Agapito, and J. M. Recio. 1985. Isolation and purification of duck liver ferritin. Rev. Esp. Fisiol. 41:341-344.
    • (1985) Rev. Esp. Fisiol , vol.41 , pp. 341-344
    • Díez, J.M.1    Agapito, M.T.2    Recio, J.M.3
  • 10
    • 0021010442 scopus 로고
    • Comparative study of ferritins from dove Columbia oena and chicken Gallus domesticus livers
    • Gonzalez del Barrio, P., and M. C. Martin Mateo. 1983. Comparative study of ferritins from dove Columbia oena and chicken Gallus domesticus livers. Comp. Biochem. Physiol. 76B:567-568.
    • (1983) Comp. Biochem. Physiol , vol.76 B , pp. 567-568
    • Gonzalez del Barrio, P.1    Martin Mateo, M.C.2
  • 11
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P. M., and P. Arosio. 1996. The ferritins: Molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275:161-203.
    • (1996) Biochim. Biophys. Acta , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 12
    • 0042330459 scopus 로고    scopus 로고
    • Synthesis of biotinylated heme and its application to panning heme-binding proteins
    • Ishida, M., N. Dohmae, Y. Shiro, and Y. Isogai. 2003. Synthesis of biotinylated heme and its application to panning heme-binding proteins. Anal. Biochem. 321:138-141.
    • (2003) Anal. Biochem , vol.321 , pp. 138-141
    • Ishida, M.1    Dohmae, N.2    Shiro, Y.3    Isogai, Y.4
  • 13
    • 33645220567 scopus 로고    scopus 로고
    • Hemin-mediated regulation of an antioxidantresponsive element of the human ferritin H gene and role of Ref-1 during erythroid differentiation of K562 cells
    • Iwasaki, K., E. L. MacKenzie, K. Hailemariam, K. Sakamoto, and Y. Tsuji. 2006. Hemin-mediated regulation of an antioxidantresponsive element of the human ferritin H gene and role of Ref-1 during erythroid differentiation of K562 cells. Mol. Cell. Biol. 26:2845-2856.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 2845-2856
    • Iwasaki, K.1    Mackenzie, E.L.2    Hailemariam, K.3    Sakamoto, K.4    Tsuji, Y.5
  • 14
    • 0030722015 scopus 로고    scopus 로고
    • 4 and 2,2'-azobis-2-amidino-propane hydrochloride (ABAP)
    • Juang, Y. D., K. O. Chay, D. U. Song, J. S. Moon, S. Y. Yang, M. W. Lee, and B. W. Ahn. 1997. Hemin inhibits lipid peroxidation induced by ascorbate/FeSO4 and 2,2'-azobis-2-amidino-propane hydrochloride (ABAP). Exp. Mol. Med. 29:171-175.
    • (1997) Exp. Mol. Med , vol.29 , pp. 171-175
    • Juang, Y.D.1    Chay, K.O.2    Song, D.U.3    Moon, J.S.4    Yang, S.Y.5    Lee, M.W.6    Ahn, B.W.7
  • 15
    • 0026519144 scopus 로고
    • Haem binding to horse ferritin and its effect on the rate of iron release
    • Kadir, F. H. A., F. K. Al-Massada, and G. R. Moore. 1992. Haem binding to horse ferritin and its effect on the rate of iron release. Biochem. J. 282:867-870.
    • (1992) Biochem. J , vol.282 , pp. 867-870
    • Kadir, F.H.A.1    Al-Massada, F.K.2    Moore, G.R.3
  • 16
    • 0025116036 scopus 로고
    • Bacterial ferritin contains 24 haem groups
    • Kadir, F. H. A., and G. R. Moore. 1990a. Bacterial ferritin contains 24 haem groups. FEBS Lett. 271:141-143.
    • (1990) FEBS Lett , vol.271 , pp. 141-143
    • Kadir, F.H.A.1    Moore, G.R.2
  • 17
    • 0025605616 scopus 로고
    • Haem binding to horse spleen ferritin
    • Kadir, F. H. A., and G. R. Moore. 1990b. Haem binding to horse spleen ferritin. FEBS Lett. 276:81-84.
    • (1990) FEBS Lett , vol.276 , pp. 81-84
    • Kadir, F.H.A.1    Moore, G.R.2
  • 18
    • 0000541806 scopus 로고
    • Ferritin in turkey tissue: A source of catalytic iron ions for lipid peroxidation
    • Kanner, J., and L. Doll. 1991. Ferritin in turkey tissue: A source of catalytic iron ions for lipid peroxidation. J. Agric. Food Chem. 39:247-249.
    • (1991) J. Agric. Food Chem , vol.39 , pp. 247-249
    • Kanner, J.1    Doll, L.2
  • 21
    • 1642443200 scopus 로고    scopus 로고
    • Iron metabolism in mynah birds (Gracula religiosa) resembles human hereditary haemachromatosis
    • Mete, A., H. G. Hendriks, P. H. M. Klaren, G. M. Dorrestein, J. E. van Dijk, and J. J. M. Marx. 2003. Iron metabolism in mynah birds (Gracula religiosa) resembles human hereditary haemachromatosis. Avian Pathol. 32:625-632.
    • (2003) Avian Pathol , vol.32 , pp. 625-632
    • Mete, A.1    Hendriks, H.G.2    Klaren, P.H.M.3    Dorrestein, G.M.4    van Dijk, J.E.5    Marx, J.J.M.6
  • 22
    • 26644441656 scopus 로고    scopus 로고
    • Partial purification and characterization of ferritin from the liver and intestinal mucosa of chickens, turtledoves and mynahs
    • Mete, A., Y. R. A. van Zeeland, A. B. Vaandrager, J. E. van Dijk, J. J. M. Marx, and G. M. Dorrestein. 2005. Partial purification and characterization of ferritin from the liver and intestinal mucosa of chickens, turtledoves and mynahs. Avian Pathol. 34:430-434.
    • (2005) Avian Pathol , vol.34 , pp. 430-434
    • Mete, A.1    van Zeeland, Y.R.A.2    Vaandrager, A.B.3    van Dijk, J.E.4    Marx, J.J.M.5    Dorrestein, G.M.6
  • 23
    • 79953291120 scopus 로고    scopus 로고
    • Binding of mammalian and avian ferritins with biotinylated hemin: Demonstration of preferential binding of the H subunit to heme
    • Nakai, M., N. Murata, T. Yoda, Y. Yoshikawa, K. Watanabe, and K. Orino. 2011. Binding of mammalian and avian ferritins with biotinylated hemin: Demonstration of preferential binding of the H subunit to heme. J. Vet. Med. Sci. 73:313-318.
    • (2011) J. Vet. Med. Sci , vol.73 , pp. 313-318
    • Nakai, M.1    Murata, N.2    Yoda, T.3    Yoshikawa, Y.4    Watanabe, K.5    Orino, K.6
  • 25
    • 1642525702 scopus 로고    scopus 로고
    • Kinetic analysis of bovine spleen apoferritin and recombinant H and L chain homopolymers: Iron uptake suggests early stage H chain ferroxidase activity and second stage L chain cooperation
    • Orino, K., S. Harada, M. Natsuhori, K. Takehara, and K. Watanabe. 2004. Kinetic analysis of bovine spleen apoferritin and recombinant H and L chain homopolymers: Iron uptake suggests early stage H chain ferroxidase activity and second stage L chain cooperation. Biometals 17:129-134.
    • (2004) Biometals , vol.17 , pp. 129-134
    • Orino, K.1    Harada, S.2    Natsuhori, M.3    Takehara, K.4    Watanabe, K.5
  • 27
    • 54449085184 scopus 로고    scopus 로고
    • Molecular, physiological and clinical aspects of the iron storage protein ferritin
    • Orino, K., and K. Watanabe. 2008. Molecular, physiological and clinical aspects of the iron storage protein ferritin. Vet. J. 178:191-201.
    • (2008) Vet. J , vol.178 , pp. 191-201
    • Orino, K.1    Watanabe, K.2
  • 28
    • 0024505403 scopus 로고
    • Purification of chicken liver ferritin by two novel methods and structural comparison with horse spleen ferritin
    • Passaniti, A., and T. F. Roth. 1989. Purification of chicken liver ferritin by two novel methods and structural comparison with horse spleen ferritin. Biochem. J. 258:413-419.
    • (1989) Biochem. J , vol.258 , pp. 413-419
    • Passaniti, A.1    Roth, T.F.2
  • 31
    • 0020690055 scopus 로고
    • Isolation, purification and characterization of spleen ferritin of Gallus domesticus L
    • Santos Benito, F. F., and M. C. Martin Mateo. 1983. Isolation, purification and characterization of spleen ferritin of Gallus domesticus L. Comp. Biochem. Physiol. B 74:643-645.
    • (1983) Comp. Biochem. Physiol. B , vol.74 , pp. 643-645
    • Santos Benito, F.F.1    Martin Mateo, M.C.2
  • 32
    • 4544220638 scopus 로고    scopus 로고
    • Why heme needs to be degraded to iron, biliverdin IXα, and carbon monoxide?
    • Sassa, S. 2004. Why heme needs to be degraded to iron, biliverdin IXα, and carbon monoxide? Antioxid. Redox Signal. 6:819-824.
    • (2004) Antioxid. Redox Signal , vol.6 , pp. 819-824
    • Sassa, S.1
  • 33
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the rage from 1 to 100 kDa
    • Schagger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the rage from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 34
    • 38649132607 scopus 로고    scopus 로고
    • Apolipoprotein B binds ferritin by hemin-mediated binding: Evidence of direct binding of apolipoprotein B and ferritin to hemin
    • Seki, T., T. Kunichika, K. Watanabe, and K. Orino. 2008. Apolipoprotein B binds ferritin by hemin-mediated binding: Evidence of direct binding of apolipoprotein B and ferritin to hemin. Biometals 21:61-69.
    • (2008) Biometals , vol.21 , pp. 61-69
    • Seki, T.1    Kunichika, T.2    Watanabe, K.3    Orino, K.4
  • 35
    • 0023337433 scopus 로고
    • Structure and expression of the chicken ferritin H subunit gene
    • Stevens, P. W., J. B. Dodgson, and J. D. Engel. 1987. Structure and expression of the chicken ferritin H subunit gene. Mol. Cell. Biol. 7:1751-1758.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 1751-1758
    • Stevens, P.W.1    Dodgson, J.B.2    Engel, J.D.3
  • 36
    • 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
  • 37
    • 0033853838 scopus 로고    scopus 로고
    • Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress
    • Tsuji, Y., H. Ayaki, S. P. Whitman, C. S. Morrow, S. V. Torti, and F. M. Torti. 2000. Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress. Mol. Cell. Biol. 20:5818-5827.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.