메뉴 건너뛰기




Volumn 34, Issue 2, 2013, Pages 471-485

Deciphering of the Dual oxidase (Nox family) gene from kuruma shrimp, Marsupenaeus japonicus: Full-length cDNA cloning and characterization

Author keywords

Duox; Expression analysis; Gene knockdown; Kuruma shrimp; Nox family

Indexed keywords

CRUSTACEA; DECAPODA (CRUSTACEA); HEXAPODA; MARSUPENAEUS JAPONICUS; SHRIMP WHITE SPOT SYNDROME VIRUS; TRIBOLIUM CASTANEUM; VERTEBRATA;

EID: 84872601805     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2012.11.026     Document Type: Article
Times cited : (20)

References (31)
  • 1
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Dröge W. Free radicals in the physiological control of cell function. Physiol Rev 2002, 82:47-95.
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Dröge, W.1
  • 2
    • 0030457649 scopus 로고    scopus 로고
    • Antibacterial effects of hydrogen peroxide and methods for its detection and quantitation
    • Juven B.J., Pierson M.D. Antibacterial effects of hydrogen peroxide and methods for its detection and quantitation. J Food Prot 1996, 59:1233-1241.
    • (1996) J Food Prot , vol.59 , pp. 1233-1241
    • Juven, B.J.1    Pierson, M.D.2
  • 3
    • 0032254389 scopus 로고    scopus 로고
    • Possible role of reactive oxygen species in antiviral defense
    • Skulachev V.P. Possible role of reactive oxygen species in antiviral defense. Biochemistry (Mosc) 1998, 63:1438-1440.
    • (1998) Biochemistry (Mosc) , vol.63 , pp. 1438-1440
    • Skulachev, V.P.1
  • 4
    • 65349172964 scopus 로고    scopus 로고
    • Duox maturation factors form cell surface complexes with Duox affecting the specificity of reactive oxygen species generation
    • Morand S., Ueyama T., Tsujibe S., Saito N., Korzeniowska A., Leto T.L. Duox maturation factors form cell surface complexes with Duox affecting the specificity of reactive oxygen species generation. FASEB J 2009, 23:1205-1218.
    • (2009) FASEB J , vol.23 , pp. 1205-1218
    • Morand, S.1    Ueyama, T.2    Tsujibe, S.3    Saito, N.4    Korzeniowska, A.5    Leto, T.L.6
  • 5
    • 0033601327 scopus 로고    scopus 로고
    • Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs
    • Dupuy C., Ohayon R., Valent A., Noël-Hudson M.S., Dème D., Virion A. Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs. J Biol Chem 1999, 274:37265-37269.
    • (1999) J Biol Chem , vol.274 , pp. 37265-37269
    • Dupuy, C.1    Ohayon, R.2    Valent, A.3    Noël-Hudson, M.S.4    Dème, D.5    Virion, A.6
  • 6
    • 0034725643 scopus 로고    scopus 로고
    • Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family
    • De Deken X., Wang D., Many M.C., Costagliola S., Libert F., Vassart G., et al. Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. J Biol Chem 2000, 275:23227-23233.
    • (2000) J Biol Chem , vol.275 , pp. 23227-23233
    • De Deken, X.1    Wang, D.2    Many, M.C.3    Costagliola, S.4    Libert, F.5    Vassart, G.6
  • 7
    • 0035921417 scopus 로고    scopus 로고
    • Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox
    • Edens W.A., Sharling L., Cheng G., Shapira R., Kinkade J.M., Lee T., et al. Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox. J Cell Biol 2001, 154:879-891.
    • (2001) J Cell Biol , vol.154 , pp. 879-891
    • Edens, W.A.1    Sharling, L.2    Cheng, G.3    Shapira, R.4    Kinkade, J.M.5    Lee, T.6
  • 9
    • 27544443327 scopus 로고    scopus 로고
    • Molecular composition and regulation of the Nox family NAD(P)H oxidases
    • Sumimoto H., Miyano K., Takeya R. Molecular composition and regulation of the Nox family NAD(P)H oxidases. Biochem Biophys Res Commun 2005, 338:677-686.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 677-686
    • Sumimoto, H.1    Miyano, K.2    Takeya, R.3
  • 10
    • 67650917886 scopus 로고    scopus 로고
    • Expression of NADPH oxidase homologues and accessory genes in human cancer cell lines, tumours and adjacent normal tissues
    • Juhasz A., Ge Y., Markel S., Chiu A., Matsumoto L., van Balgooy J., et al. Expression of NADPH oxidase homologues and accessory genes in human cancer cell lines, tumours and adjacent normal tissues. Free Radic Res 2009, 43:523-532.
    • (2009) Free Radic Res , vol.43 , pp. 523-532
    • Juhasz, A.1    Ge, Y.2    Markel, S.3    Chiu, A.4    Matsumoto, L.5    van Balgooy, J.6
  • 11
    • 77951636607 scopus 로고    scopus 로고
    • Dual oxidase, hydrogen peroxide and thyroid diseases
    • Ohye H., Sugawara M. Dual oxidase, hydrogen peroxide and thyroid diseases. Exp Biol Med 2010, 235:424-433.
    • (2010) Exp Biol Med , vol.235 , pp. 424-433
    • Ohye, H.1    Sugawara, M.2
  • 14
    • 24044451233 scopus 로고    scopus 로고
    • Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium
    • Harper R.W., Xu C., Eiserich J.P., Chen Y., Kao C.Y., Thai P., et al. Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium. FEBS Lett 2005, 579:4911-4917.
    • (2005) FEBS Lett , vol.579 , pp. 4911-4917
    • Harper, R.W.1    Xu, C.2    Eiserich, J.P.3    Chen, Y.4    Kao, C.Y.5    Thai, P.6
  • 15
    • 27644498442 scopus 로고    scopus 로고
    • A direct role for dual oxidase in Drosophila gut immunity
    • Ha E.M., Oh C.T., Bae Y.S., Lee W.J. A direct role for dual oxidase in Drosophila gut immunity. Science 2005, 310:847-850.
    • (2005) Science , vol.310 , pp. 847-850
    • Ha, E.M.1    Oh, C.T.2    Bae, Y.S.3    Lee, W.J.4
  • 16
    • 77949593677 scopus 로고    scopus 로고
    • Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases
    • Leto T.L., Morand S., Hurt D., Ueyama T. Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases. Antioxid Redox Signal 2009, 11:2607-2619.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2607-2619
    • Leto, T.L.1    Morand, S.2    Hurt, D.3    Ueyama, T.4
  • 17
    • 77950234253 scopus 로고    scopus 로고
    • A peroxidase/dual oxidase system modulates midgut epithelial immunity in Anopheles gambiae
    • Kumar S., Molina-Cruz A., Gupta L., Rodrigues J., Barillas-Mury C. A peroxidase/dual oxidase system modulates midgut epithelial immunity in Anopheles gambiae. Science 2010, 327:1644-1648.
    • (2010) Science , vol.327 , pp. 1644-1648
    • Kumar, S.1    Molina-Cruz, A.2    Gupta, L.3    Rodrigues, J.4    Barillas-Mury, C.5
  • 18
    • 0034694381 scopus 로고    scopus 로고
    • Measurement of reactive oxygen intermediate production in haemocytes of the penaeid shrimp, Penaeus vannamei
    • Muñoz M., Cedeño R., Rodríguez J., Van Der Knaap W.P.W., Mialhe E., Bachère E. Measurement of reactive oxygen intermediate production in haemocytes of the penaeid shrimp, Penaeus vannamei. Aquaculture 2000, 191:89-107.
    • (2000) Aquaculture , vol.191 , pp. 89-107
    • Muñoz, M.1    Cedeño, R.2    Rodríguez, J.3    Van Der Knaap, W.P.W.4    Mialhe, E.5    Bachère, E.6
  • 20
    • 34447559438 scopus 로고    scopus 로고
    • In vitro generation of superoxide anion by the hemocytes of Macrobrachium rosenbergii: possible mechanism and pathways
    • Vidya N., Thiagarajan R., Arumugam M. In vitro generation of superoxide anion by the hemocytes of Macrobrachium rosenbergii: possible mechanism and pathways. J Exp Zool Part A 2007, 307:383-396.
    • (2007) J Exp Zool Part A , vol.307 , pp. 383-396
    • Vidya, N.1    Thiagarajan, R.2    Arumugam, M.3
  • 21
    • 84855945418 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the NADPH oxidase from the kuruma shrimp, Marsupenaeus japonicus: early gene up-regulation after Vibrio penaeicida and poly(I: C) stimulations in vitro
    • Inada M., Sudhakaran R., Kihara K., Nishi J., Yoshimine M., Mekata T., et al. Molecular cloning and characterization of the NADPH oxidase from the kuruma shrimp, Marsupenaeus japonicus: early gene up-regulation after Vibrio penaeicida and poly(I: C) stimulations in vitro. Mol Cell Probes 2012, 26:29-41.
    • (2012) Mol Cell Probes , vol.26 , pp. 29-41
    • Inada, M.1    Sudhakaran, R.2    Kihara, K.3    Nishi, J.4    Yoshimine, M.5    Mekata, T.6
  • 22
    • 84855959051 scopus 로고    scopus 로고
    • Superoxide and nitric oxide production of kuruma prawn (Marsupenaeus japonicus) hemocytes
    • Itami T., Ohno Y., Suzuki N., Doi K., Kondo M., Takahashi Y., et al. Superoxide and nitric oxide production of kuruma prawn (Marsupenaeus japonicus) hemocytes. Fish Sci 2002, 68:1119-1122.
    • (2002) Fish Sci , vol.68 , pp. 1119-1122
    • Itami, T.1    Ohno, Y.2    Suzuki, N.3    Doi, K.4    Kondo, M.5    Takahashi, Y.6
  • 23
    • 77949888065 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the nitric oxide synthase gene from kuruma shrimp, Marsupenaeus japonicus
    • Inada M., Mekata T., Sudhakaran R., Okugawa S., Kono T., El Asely A.M., et al. Molecular cloning and characterization of the nitric oxide synthase gene from kuruma shrimp, Marsupenaeus japonicus. Fish Shellfish Immunol 2010, 28:701-711.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 701-711
    • Inada, M.1    Mekata, T.2    Sudhakaran, R.3    Okugawa, S.4    Kono, T.5    El Asely, A.M.6
  • 24
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: recent updates to the protein domain annotation resource
    • Letunic I., Doerks T., Bork P. SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res 2011, 10.1093/nar/gkr931.
    • (2011) Nucleic Acids Res
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 25
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 1999, 41:95-98.
    • (1999) Nucleic Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 26
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 2011, 28:2731-2739.
    • (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
  • 27
    • 44949106317 scopus 로고    scopus 로고
    • Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species
    • Sumimoto H. Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species. FEBS J 2008, 275:3249-3277.
    • (2008) FEBS J , vol.275 , pp. 3249-3277
    • Sumimoto, H.1
  • 28
    • 22544464980 scopus 로고    scopus 로고
    • Diseases of cultured kuruma shrimp in Japan: a review
    • Momoyama K., Muroga K. Diseases of cultured kuruma shrimp in Japan: a review. Fish Pathol 2005, 40:1-14.
    • (2005) Fish Pathol , vol.40 , pp. 1-14
    • Momoyama, K.1    Muroga, K.2
  • 29
    • 84872604650 scopus 로고    scopus 로고
    • A model for apoptotic interaction between white spot syndrome virus and shrimp
    • Fish Shellfish Immunol, [Epub ahead of print].
    • Leu JH, Lin SJ, Huang JY, Chen TC, Lo CF. A model for apoptotic interaction between white spot syndrome virus and shrimp. Fish Shellfish Immunol, [Epub ahead of print].
    • Leu, J.H.1    Lin, S.J.2    Huang, J.Y.3    Chen, T.C.4    Lo, C.F.5
  • 30
    • 22144471938 scopus 로고    scopus 로고
    • Silencing of yellow head virus replication in penaeid shrimp cells by dsRNA
    • Tirasophon W., Roshorm Y., Panyim S. Silencing of yellow head virus replication in penaeid shrimp cells by dsRNA. Biochem Biophys Res Commun 2005, 334:102-107.
    • (2005) Biochem Biophys Res Commun , vol.334 , pp. 102-107
    • Tirasophon, W.1    Roshorm, Y.2    Panyim, S.3
  • 31
    • 4544368487 scopus 로고    scopus 로고
    • Induction of antiviral immunity by double-stranded RNA in a marine invertebrate
    • Robalino J., Browdy C.L., Prior S., Metz A., Parnell P., Gross P., et al. Induction of antiviral immunity by double-stranded RNA in a marine invertebrate. J Virol 2004, 78:10442-10448.
    • (2004) J Virol , vol.78 , pp. 10442-10448
    • Robalino, J.1    Browdy, C.L.2    Prior, S.3    Metz, A.4    Parnell, P.5    Gross, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.