메뉴 건너뛰기




Volumn 40, Issue 1, 2014, Pages 288-295

Identification and characterization of a Macrobrachium nipponense ferritin subunit regulated by iron ion and pathogen challenge

Author keywords

CDNA cloning; Ferritin; Gene expression; Iron; Macrobrachium nipponense

Indexed keywords

ARTHROPOD PROTEIN; COMPLEMENTARY DNA; FERRITIN; IRON; PROTEIN SUBUNIT;

EID: 84904905555     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2014.07.002     Document Type: Article
Times cited : (12)

References (47)
  • 1
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison P.M., Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1996, 1275:161-203.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 2
    • 54449085184 scopus 로고    scopus 로고
    • Molecular, physiological and clinical aspects of the iron storage protein ferritin
    • Orino K., Watanabe K. Molecular, physiological and clinical aspects of the iron storage protein ferritin. Vet J 2008, 178:191-201.
    • (2008) Vet J , vol.178 , pp. 191-201
    • Orino, K.1    Watanabe, K.2
  • 3
    • 0025112529 scopus 로고
    • The ferritin family of iron storage proteins
    • Theil E.C. The ferritin family of iron storage proteins. Adv Enzymol Relat Areas Mol Biol 1990, 63:421-449.
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63 , pp. 421-449
    • Theil, E.C.1
  • 4
    • 0034949363 scopus 로고    scopus 로고
    • Iron metabolism, free radicals, and oxidative injury
    • Emerit J., Beaumont C., Trivin F. Iron metabolism, free radicals, and oxidative injury. Biomed Pharmacother 2001, 55:333-339.
    • (2001) Biomed Pharmacother , vol.55 , pp. 333-339
    • Emerit, J.1    Beaumont, C.2    Trivin, F.3
  • 5
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti F.M., Torti S.V. Regulation of ferritin genes and protein. Blood 2002, 99:3505-3516.
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 7
    • 0030060705 scopus 로고    scopus 로고
    • Overexpression of the ferritin H subunit in cultured erythroid cells changes the intracellular iron distribution
    • Picard V., Renaudie F., Porcher C., Hentze M.W., Grandchamp B., Beaumont C. Overexpression of the ferritin H subunit in cultured erythroid cells changes the intracellular iron distribution. Blood 1996, 87:2057-2064.
    • (1996) Blood , vol.87 , pp. 2057-2064
    • Picard, V.1    Renaudie, F.2    Porcher, C.3    Hentze, M.W.4    Grandchamp, B.5    Beaumont, C.6
  • 8
    • 0035366598 scopus 로고    scopus 로고
    • Repression of the heavy ferritin chain increases the labile iron pool of human K562 cells
    • Kakhlon O., Gruenbaum Y., Cabantchik Z.I. Repression of the heavy ferritin chain increases the labile iron pool of human K562 cells. Biochem J 2001, 356:311-316.
    • (2001) Biochem J , vol.356 , pp. 311-316
    • Kakhlon, O.1    Gruenbaum, Y.2    Cabantchik, Z.I.3
  • 10
    • 77953812085 scopus 로고    scopus 로고
    • Nuclear ferritin: a new role for ferritin in cell biology
    • Alkhateeb A.A., Connor J.R. Nuclear ferritin: a new role for ferritin in cell biology. Biochim Biophys Acta 2010, 1800:793-797.
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 793-797
    • Alkhateeb, A.A.1    Connor, J.R.2
  • 12
    • 0036646141 scopus 로고    scopus 로고
    • Ferritin binds to light chain of human Hkininogen and inhibits kallikrein-mediated bradykinin release
    • Parthasarathy N., Torti S.V., Torti F.M. Ferritin binds to light chain of human Hkininogen and inhibits kallikrein-mediated bradykinin release. Biochem J 2002, 365:279-286.
    • (2002) Biochem J , vol.365 , pp. 279-286
    • Parthasarathy, N.1    Torti, S.V.2    Torti, F.M.3
  • 13
    • 33645048994 scopus 로고    scopus 로고
    • Cellular regulation and molecular interactions of the ferritins
    • Hintze K.J., Theil E.C. Cellular regulation and molecular interactions of the ferritins. Cell Mol Life Sci 2006, 63:591-600.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 591-600
    • Hintze, K.J.1    Theil, E.C.2
  • 14
    • 0037462675 scopus 로고    scopus 로고
    • Nrf2 mediates the induction of ferritin H in response to xenobiotics and cancer chemopreventive dithiolethiones
    • Pietsch E.C., Chan J.Y., Torti F.M., Torti S.V. Nrf2 mediates the induction of ferritin H in response to xenobiotics and cancer chemopreventive dithiolethiones. JBiol Chem 2003, 278:2361-2369.
    • (2003) JBiol Chem , vol.278 , pp. 2361-2369
    • Pietsch, E.C.1    Chan, J.Y.2    Torti, F.M.3    Torti, S.V.4
  • 15
    • 0034731457 scopus 로고    scopus 로고
    • Combinatorial mRNA regulation: iron regulatory proteins and iso-iron-responsive elements (Iso-IREs)
    • Theil E.C., Eisenstein R.S. Combinatorial mRNA regulation: iron regulatory proteins and iso-iron-responsive elements (Iso-IREs). JBiol Chem 2000, 275:40659-40662.
    • (2000) JBiol Chem , vol.275 , pp. 40659-40662
    • Theil, E.C.1    Eisenstein, R.S.2
  • 16
    • 0029803246 scopus 로고    scopus 로고
    • Ferritin mRNAs in Schistosoma mansoni do not have iron-responsive elements for posttranscriptional regulation
    • Schussler P., Potters E., Winnen R., Michel A., Bottke W., Kunz W. Ferritin mRNAs in Schistosoma mansoni do not have iron-responsive elements for posttranscriptional regulation. Eur J Biochem 1996, 241:64-69.
    • (1996) Eur J Biochem , vol.241 , pp. 64-69
    • Schussler, P.1    Potters, E.2    Winnen, R.3    Michel, A.4    Bottke, W.5    Kunz, W.6
  • 17
    • 0031758919 scopus 로고    scopus 로고
    • Drosophila ferritin mRNA: alternative RNA splicing regulates the presence of the iron-responsive element
    • Lind M.I., Ekengren S., Melefors O., Soderhall K. Drosophila ferritin mRNA: alternative RNA splicing regulates the presence of the iron-responsive element. FEBS Lett 1998, 436:476-482.
    • (1998) FEBS Lett , vol.436 , pp. 476-482
    • Lind, M.I.1    Ekengren, S.2    Melefors, O.3    Soderhall, K.4
  • 18
    • 0033019925 scopus 로고    scopus 로고
    • Iron availability dramatically alters the distribution of ferritin subunit messages in Drosophila melanogaster
    • Georgieva T., Dunkov B.C., Harizanova N., Ralchev K., Law J.H. Iron availability dramatically alters the distribution of ferritin subunit messages in Drosophila melanogaster. Proc Natl Acad Sci U S A 1999, 96:2716-2721.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2716-2721
    • Georgieva, T.1    Dunkov, B.C.2    Harizanova, N.3    Ralchev, K.4    Law, J.H.5
  • 19
    • 44249086113 scopus 로고    scopus 로고
    • Transcriptional regulation of ferritin mRNA levels by iron in the freshwater giant prawn, Macrobrachium rosenbergii
    • Qiu G.F., Zheng L., Liu P. Transcriptional regulation of ferritin mRNA levels by iron in the freshwater giant prawn, Macrobrachium rosenbergii. Comp Biochem Physiol B Biochem Mol Biol 2008, 150:320-325.
    • (2008) Comp Biochem Physiol B Biochem Mol Biol , vol.150 , pp. 320-325
    • Qiu, G.F.1    Zheng, L.2    Liu, P.3
  • 21
    • 84893444135 scopus 로고    scopus 로고
    • Identification of two secreted ferritin subunits involved in immune defense of Yesso scallop Patinopecten yessoensis
    • Sun Y., Zhang Y., Fu X., Zhang R., Zou J., Wang S., et al. Identification of two secreted ferritin subunits involved in immune defense of Yesso scallop Patinopecten yessoensis. Fish Shellfish Immunol 2014, 37:53-59.
    • (2014) Fish Shellfish Immunol , vol.37 , pp. 53-59
    • Sun, Y.1    Zhang, Y.2    Fu, X.3    Zhang, R.4    Zou, J.5    Wang, S.6
  • 22
    • 84859865647 scopus 로고    scopus 로고
    • Fisheries economic statistics
    • Bureau of Fishery, Ministry of Agriculture, P.R.C, China Agricultural Press, Beijing
    • Bureau of Fishery, Ministry of Agriculture, P.R.C Fisheries economic statistics. China fishery yearbook 2009, 236. China Agricultural Press, Beijing.
    • (2009) China fishery yearbook , pp. 236
  • 23
    • 84902470573 scopus 로고    scopus 로고
    • Identification and biological characteristics of the pathogen causing Macrobrachium nipponense soft-shell syndrome
    • [in Chinese with English abstract]
    • Pan X.Y., Shen J.Y., Li J.Y., He B.X., Yin W.L., Hao G.J., et al. Identification and biological characteristics of the pathogen causing Macrobrachium nipponense soft-shell syndrome. Microbiol China 2009, 36:1571-1576. [in Chinese with English abstract].
    • (2009) Microbiol China , vol.36 , pp. 1571-1576
    • Pan, X.Y.1    Shen, J.Y.2    Li, J.Y.3    He, B.X.4    Yin, W.L.5    Hao, G.J.6
  • 24
    • 84901759583 scopus 로고    scopus 로고
    • Studies on the pathogens of bacterial diseases of Macrobrachium nipponense
    • [in Chinese with English abstract]
    • Shen J.Y., Qian D., Liu W., Yin W.L., Shen Z.H., Cao Z., et al. Studies on the pathogens of bacterial diseases of Macrobrachium nipponense. JZhejiang Ocean Univ (Nat Sci) 2000, 19:222-224. [in Chinese with English abstract].
    • (2000) JZhejiang Ocean Univ (Nat Sci) , vol.19 , pp. 222-224
    • Shen, J.Y.1    Qian, D.2    Liu, W.3    Yin, W.L.4    Shen, Z.H.5    Cao, Z.6
  • 25
    • 0029875555 scopus 로고    scopus 로고
    • Purification and cDNA cloning of ferritin from the hepatopancreas of the freshwater crayfish Pacifastacus leniusculus
    • Huang T.S., Law J.H., Soderhall K. Purification and cDNA cloning of ferritin from the hepatopancreas of the freshwater crayfish Pacifastacus leniusculus. Eur J Biochem 1996, 236:450-456.
    • (1996) Eur J Biochem , vol.236 , pp. 450-456
    • Huang, T.S.1    Law, J.H.2    Soderhall, K.3
  • 26
    • 0033038467 scopus 로고    scopus 로고
    • An atypical iron-responsive element (IRE) within crayfish ferritin mRNA and an iron regulatory protein 1 (IRP1)-like protein from crayfish hepatopancreas
    • Huang T.S., Melefors O., Lind M.I., Soderhall K. An atypical iron-responsive element (IRE) within crayfish ferritin mRNA and an iron regulatory protein 1 (IRP1)-like protein from crayfish hepatopancreas. Insect Biochem Mol Biol 1999, 29:1-9.
    • (1999) Insect Biochem Mol Biol , vol.29 , pp. 1-9
    • Huang, T.S.1    Melefors, O.2    Lind, M.I.3    Soderhall, K.4
  • 27
    • 74649083213 scopus 로고    scopus 로고
    • CDNA cloning and expression of Ubc9 in the developing embryo and ovary of oriental river prawn, Macrobrachium nipponense
    • Zhang F.Y., Chen L.Q., Wu P., Zhao W.H., Li E.R., Qin J.Q. cDNA cloning and expression of Ubc9 in the developing embryo and ovary of oriental river prawn, Macrobrachium nipponense. Comp Biochem Physiol B Biochem Mol Biol 2010, 155:288-293.
    • (2010) Comp Biochem Physiol B Biochem Mol Biol , vol.155 , pp. 288-293
    • Zhang, F.Y.1    Chen, L.Q.2    Wu, P.3    Zhao, W.H.4    Li, E.R.5    Qin, J.Q.6
  • 29
    • 34447344092 scopus 로고    scopus 로고
    • Two ferritin subunits from disk abalone (Haliotis discus discus): cloning, characterization and expression analysis
    • De Zoysa M., Lee J. Two ferritin subunits from disk abalone (Haliotis discus discus): cloning, characterization and expression analysis. Fish Shellfish Immunol 2007, 23:624-635.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 624-635
    • De Zoysa, M.1    Lee, J.2
  • 30
    • 27644444230 scopus 로고    scopus 로고
    • The response of ferritin to LPS and acute phase of Pseudomonas infection
    • Ong D.S., Wang L., Zhu Y., Ho B., Ding J.L. The response of ferritin to LPS and acute phase of Pseudomonas infection. JEndotoxin Res 2005, 11:267-280.
    • (2005) JEndotoxin Res , vol.11 , pp. 267-280
    • Ong, D.S.1    Wang, L.2    Zhu, Y.3    Ho, B.4    Ding, J.L.5
  • 31
    • 0036027763 scopus 로고    scopus 로고
    • Evolution of the acute phase response: iron release by echinoderm (Asterias forbesi) coelomocytes, and cloning of an echinoderm ferritin molecule
    • Beck G., Ellis T.W., Habicht G.S., Schluter S.F., Marchalonis J.J. Evolution of the acute phase response: iron release by echinoderm (Asterias forbesi) coelomocytes, and cloning of an echinoderm ferritin molecule. Dev Comp Immunol 2002, 26:11-26.
    • (2002) Dev Comp Immunol , vol.26 , pp. 11-26
    • Beck, G.1    Ellis, T.W.2    Habicht, G.S.3    Schluter, S.F.4    Marchalonis, J.J.5
  • 33
    • 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 U S A 1996, 93:8175-8182.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 34
    • 0023067301 scopus 로고
    • Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms
    • Theil E.C. Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms. Annu Rev Biochem 1987, 56:289-315.
    • (1987) Annu Rev Biochem , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 35
    • 0025230751 scopus 로고
    • The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution
    • Rothenberger S., Mullner E.W., Kuhn L.C. The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution. Nucleic Acids Res 1990, 18:1175-1179.
    • (1990) Nucleic Acids Res , vol.18 , pp. 1175-1179
    • Rothenberger, S.1    Mullner, E.W.2    Kuhn, L.C.3
  • 37
    • 0036489168 scopus 로고    scopus 로고
    • Drosophila melanogaster ferritin: cDNA encoding a light chain homologue, temporal and tissue specific expression of both subunit types
    • Georgieva T., Dunkov B.C., Dimov S., Ralchev K., Law J.H. Drosophila melanogaster ferritin: cDNA encoding a light chain homologue, temporal and tissue specific expression of both subunit types. Insect Biochem Mol Biol 2002, 32:295-302.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 295-302
    • Georgieva, T.1    Dunkov, B.C.2    Dimov, S.3    Ralchev, K.4    Law, J.H.5
  • 38
    • 33646759977 scopus 로고    scopus 로고
    • Molecular cloning and tissue distribution of ferritin in Pacific white shrimp (Litopenaeus vannamei)
    • Hsieh S.L., Chiu Y.C., Kuo C.M. Molecular cloning and tissue distribution of ferritin in Pacific white shrimp (Litopenaeus vannamei). Fish Shellfish Immunol 2006, 21:279-283.
    • (2006) Fish Shellfish Immunol , vol.21 , pp. 279-283
    • Hsieh, S.L.1    Chiu, Y.C.2    Kuo, C.M.3
  • 39
    • 79953667726 scopus 로고    scopus 로고
    • Isolation and characterization of a ferritin cDNA from the mud crab Scylla paramamosain
    • Zhang D., Jiang K.J., Zhang F.Y., Ma C.Y., Shi Y.H., Qiao Z.G., et al. Isolation and characterization of a ferritin cDNA from the mud crab Scylla paramamosain. JCrustac Biol 2011, 31:345-351.
    • (2011) JCrustac Biol , vol.31 , pp. 345-351
    • Zhang, D.1    Jiang, K.J.2    Zhang, F.Y.3    Ma, C.Y.4    Shi, Y.H.5    Qiao, Z.G.6
  • 40
    • 0032878232 scopus 로고    scopus 로고
    • Iron-regulatory proteins, iron responsive elements and ferritin mRNA translation
    • Thomson A.M., Rogers J.T., Leedman P.J. Iron-regulatory proteins, iron responsive elements and ferritin mRNA translation. Int J Biochem Cell Biol 1999, 31:1139-1152.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1139-1152
    • Thomson, A.M.1    Rogers, J.T.2    Leedman, P.J.3
  • 41
    • 77951995410 scopus 로고    scopus 로고
    • New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants
    • Briat J.F., Ravet K., Arnaud N., Duc C., Boucherez J., Touraine B., et al. New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants. Ann Bot 2010, 105:811-822.
    • (2010) Ann Bot , vol.105 , pp. 811-822
    • Briat, J.F.1    Ravet, K.2    Arnaud, N.3    Duc, C.4    Boucherez, J.5    Touraine, B.6
  • 42
    • 34247279096 scopus 로고    scopus 로고
    • The unique regulation of Aedes aegypti larval cell ferritin by iron
    • Geiser D.L., Mayo J.J., Winzerling J.J. The unique regulation of Aedes aegypti larval cell ferritin by iron. Insect Biochem Mol Biol 2007, 37:418-429.
    • (2007) Insect Biochem Mol Biol , vol.37 , pp. 418-429
    • Geiser, D.L.1    Mayo, J.J.2    Winzerling, J.J.3
  • 43
    • 33646363763 scopus 로고    scopus 로고
    • Iron-withholding strategy in innate immunity
    • Ong S.T., Ho J.Z.S., Ho B., Ding J.L. Iron-withholding strategy in innate immunity. Immunobiology 2006, 211:295-314.
    • (2006) Immunobiology , vol.211 , pp. 295-314
    • Ong, S.T.1    Ho, J.Z.S.2    Ho, B.3    Ding, J.L.4
  • 44
    • 79953311152 scopus 로고    scopus 로고
    • Identification and characterization of a clam ferritin from Sinonovacula constricta
    • Li C.H., Li H., Su X.R., Li T.W. Identification and characterization of a clam ferritin from Sinonovacula constricta. Fish Shellfish Immunol 2011, 30:1147-1151.
    • (2011) Fish Shellfish Immunol , vol.30 , pp. 1147-1151
    • Li, C.H.1    Li, H.2    Su, X.R.3    Li, T.W.4
  • 45
    • 84875804111 scopus 로고    scopus 로고
    • Identification and characterization of four ferritin subunits involved in immune defense of the Yesso scallop (Patinopecten yessoensis)
    • Zhang Y., Zhang R., Zou J., Hu X., Wang S., Zhang L., et al. Identification and characterization of four ferritin subunits involved in immune defense of the Yesso scallop (Patinopecten yessoensis). Fish Shellfish Immunol 2013, 34:1178-1187.
    • (2013) Fish Shellfish Immunol , vol.34 , pp. 1178-1187
    • Zhang, Y.1    Zhang, R.2    Zou, J.3    Hu, X.4    Wang, S.5    Zhang, L.6
  • 46
    • 77949915061 scopus 로고    scopus 로고
    • Two novel secreted ferritins involved in immune defense of Chinese mitten crab Eriocheir sinensis
    • Kong P., Wang L., Zhang H., Zhou Z., Qiu L., Gai Y., et al. Two novel secreted ferritins involved in immune defense of Chinese mitten crab Eriocheir sinensis. Fish Shellfish Immunol 2010, 28:604-612.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 604-612
    • Kong, P.1    Wang, L.2    Zhang, H.3    Zhou, Z.4    Qiu, L.5    Gai, Y.6
  • 47
    • 77956344975 scopus 로고    scopus 로고
    • Transcriptional upregulation of a novel ferritin homolog in abalone Haliotis discus hannai ino by dietary iron
    • Wu C.L., Zhang W.B., Mai K.S., Xu W., Wang X.J., Ma H.M., et al. Transcriptional upregulation of a novel ferritin homolog in abalone Haliotis discus hannai ino by dietary iron. Comp Biochem Physiol C Toxicol Pharmacol 2010, 152:424-432.
    • (2010) Comp Biochem Physiol C Toxicol Pharmacol , vol.152 , pp. 424-432
    • Wu, C.L.1    Zhang, W.B.2    Mai, K.S.3    Xu, W.4    Wang, X.J.5    Ma, H.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.