메뉴 건너뛰기




Volumn 29, Issue 3, 2010, Pages 544-549

Identification of upregulated immune-related genes in Vibrio harveyi challenged Penaeus monodon postlarvae

Author keywords

EST; Penaeus monodon; QPCR; Shrimp diseases; SSH; Vibrio harveyi

Indexed keywords

CRUSTACEA; DECAPODA (CRUSTACEA); PENAEUS MONODON; VIBRIO HARVEYI;

EID: 77954536931     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2010.05.010     Document Type: Article
Times cited : (49)

References (38)
  • 1
    • 0037413982 scopus 로고    scopus 로고
    • Phenotypic diversity among Vibrio isolates from marine aquaculture systems
    • Vandenberghe J., Thompson F.L., Gomez-Gill B., Swings J. Phenotypic diversity among Vibrio isolates from marine aquaculture systems. Aquaculture 2003, 219:9-20.
    • (2003) Aquaculture , vol.219 , pp. 9-20
    • Vandenberghe, J.1    Thompson, F.L.2    Gomez-Gill, B.3    Swings, J.4
  • 2
    • 0034694377 scopus 로고    scopus 로고
    • Experimental infection models for shrimp Vibriosis studies: a review
    • Saulnier D., Haffner P., Goarant C., Levy P., Ansquer D. Experimental infection models for shrimp Vibriosis studies: a review. Aquaculture 2000, 191:133-144.
    • (2000) Aquaculture , vol.191 , pp. 133-144
    • Saulnier, D.1    Haffner, P.2    Goarant, C.3    Levy, P.4    Ansquer, D.5
  • 3
  • 4
    • 15844428981 scopus 로고    scopus 로고
    • Suppression subtractive hybridization: a method for generating differentially regulated or tissue-specific cDNA probes and libraries
    • Ditchenko L., Lau Y.F., Campbell A.P., Chenchik A., Moqadam F., Huang B., et al. Suppression subtractive hybridization: a method for generating differentially regulated or tissue-specific cDNA probes and libraries. Proc Natl Acad Sci USA 1996, 93:6025-6030.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6025-6030
    • Ditchenko, L.1    Lau, Y.F.2    Campbell, A.P.3    Chenchik, A.4    Moqadam, F.5    Huang, B.6
  • 5
    • 2442702902 scopus 로고    scopus 로고
    • Comparing gene discovery from Affymetrix GeneChip microarrays and Clontech PCR-select cDNA subtraction: a case study
    • Cao W., Epstein C., Liu H., De Loughery C., Ge N., Lin J., et al. Comparing gene discovery from Affymetrix GeneChip microarrays and Clontech PCR-select cDNA subtraction: a case study. BMC Genomics 2004, 5(1):26.
    • (2004) BMC Genomics , vol.5 , Issue.1 , pp. 26
    • Cao, W.1    Epstein, C.2    Liu, H.3    De Loughery, C.4    Ge, N.5    Lin, J.6
  • 6
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using Real-time quantitative PCR and the 2-ΔΔ CT method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using Real-time quantitative PCR and the 2-ΔΔ CT method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 7
    • 0000839322 scopus 로고
    • Experimental infections of crustaceans with luminous bacteria related to Photobacterium and Vibrio - effect of salinity and pH on infectiosity
    • Prayitno S.B., Latchford J.W. Experimental infections of crustaceans with luminous bacteria related to Photobacterium and Vibrio - effect of salinity and pH on infectiosity. Aquaculture 1995, 132:105-112.
    • (1995) Aquaculture , vol.132 , pp. 105-112
    • Prayitno, S.B.1    Latchford, J.W.2
  • 9
    • 33750965196 scopus 로고    scopus 로고
    • Penaeus monodon gene discovery project: the generation of an EST collection and establishment of a database
    • Tassanakajona A., Klinbungab S., Paunglarpb N., Rimphanitchayakita V., Udomkitd A., Jitrapakdee S., et al. Penaeus monodon gene discovery project: the generation of an EST collection and establishment of a database. Gene 2006, 384:104-112.
    • (2006) Gene , vol.384 , pp. 104-112
    • Tassanakajona, A.1    Klinbungab, S.2    Paunglarpb, N.3    Rimphanitchayakita, V.4    Udomkitd, A.5    Jitrapakdee, S.6
  • 10
    • 33746871180 scopus 로고    scopus 로고
    • Cloning, expression and identification of ferritin from Chinese shrimp, Fenneropenaeus chinensis
    • Zhang J., Li F., Wang Z., Zhang X., Zhou Q., Xiang J. Cloning, expression and identification of ferritin from Chinese shrimp, Fenneropenaeus chinensis. J Biotechnol 2006, 125:173-184.
    • (2006) J Biotechnol , vol.125 , pp. 173-184
    • Zhang, J.1    Li, F.2    Wang, Z.3    Zhang, X.4    Zhou, Q.5    Xiang, J.6
  • 11
    • 4644229512 scopus 로고    scopus 로고
    • Differential gene expression profile in hepatopancreas of WSSV-resistant shrimp (Penaeus japonicus) by suppression subtractive hybridization
    • Pan D., He N., Yang Z., Liu H., Xu X. Differential gene expression profile in hepatopancreas of WSSV-resistant shrimp (Penaeus japonicus) by suppression subtractive hybridization. Dev Comp Immunol 2005, 29:103-112.
    • (2005) Dev Comp Immunol , vol.29 , pp. 103-112
    • Pan, D.1    He, N.2    Yang, Z.3    Liu, H.4    Xu, X.5
  • 12
    • 3743076659 scopus 로고
    • Interactions between bacteria and iron binding proteins
    • Marcelis J.H. Interactions between bacteria and iron binding proteins. Vet Res Commun 1980, 4:151-164.
    • (1980) Vet Res Commun , vol.4 , pp. 151-164
    • Marcelis, J.H.1
  • 14
    • 0029162593 scopus 로고
    • In vivo, in vitro and cell-free synthesis of hemocyanin in the shrimp Penaeus semisulcatus (de Haan)
    • Khayat M., Funkenstein B., Tietz A., Lubzens E. In vivo, in vitro and cell-free synthesis of hemocyanin in the shrimp Penaeus semisulcatus (de Haan). Comp Biochem Physiol B 1995, 112:31-38.
    • (1995) Comp Biochem Physiol B , vol.112 , pp. 31-38
    • Khayat, M.1    Funkenstein, B.2    Tietz, A.3    Lubzens, E.4
  • 15
    • 0035861645 scopus 로고    scopus 로고
    • Crustacean immunity, Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge
    • Destoumieux-Garzòn D., Saulnier D., Garnier J., Jouffrey C., Bulet P., Bachère E. Crustacean immunity, Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge. J Biol Chem 2001, 276:47070-47077.
    • (2001) J Biol Chem , vol.276 , pp. 47070-47077
    • Destoumieux-Garzòn, D.1    Saulnier, D.2    Garnier, J.3    Jouffrey, C.4    Bulet, P.5    Bachère, E.6
  • 16
    • 0032476016 scopus 로고    scopus 로고
    • Tarantula hemocyanin shows phenoloxidase activity
    • Decker H., Rimke T. Tarantula hemocyanin shows phenoloxidase activity. J Biol Chem 1998, 273:25889-25892.
    • (1998) J Biol Chem , vol.273 , pp. 25889-25892
    • Decker, H.1    Rimke, T.2
  • 17
    • 0344736987 scopus 로고    scopus 로고
    • Antiviral properties of hemocyanin isolated from shrimp Penaeus monodon
    • Zhang X., Huang C., Qin Q. Antiviral properties of hemocyanin isolated from shrimp Penaeus monodon. Antiviral Res 2004, 61:93-99.
    • (2004) Antiviral Res , vol.61 , pp. 93-99
    • Zhang, X.1    Huang, C.2    Qin, Q.3
  • 18
    • 0035007921 scopus 로고    scopus 로고
    • Peroxinectin, a cell adhesion protein associated with the proPOsystem from the black tiger shrimp, Penaeus monodon
    • Sritunyalucksana K., Wongsuebsantati K., Johansson M.W., Soderhall K. Peroxinectin, a cell adhesion protein associated with the proPOsystem from the black tiger shrimp, Penaeus monodon. Dev Comp Immunol 2001, 25:353-363.
    • (2001) Dev Comp Immunol , vol.25 , pp. 353-363
    • Sritunyalucksana, K.1    Wongsuebsantati, K.2    Johansson, M.W.3    Soderhall, K.4
  • 21
    • 38249006800 scopus 로고
    • Antioxidant enzymes associated with the blood cells and haemolymph of the mussel Mytilus edulis
    • Pipe R.K., Porte C., Livingstone D.R. Antioxidant enzymes associated with the blood cells and haemolymph of the mussel Mytilus edulis. Fish Shellfish Immunol 1993, 3:221-233.
    • (1993) Fish Shellfish Immunol , vol.3 , pp. 221-233
    • Pipe, R.K.1    Porte, C.2    Livingstone, D.R.3
  • 22
    • 0027669291 scopus 로고
    • Antioxidants, immune response and animal function. Physiological role of antioxidants in the immune system
    • Bendich A. Antioxidants, immune response and animal function. Physiological role of antioxidants in the immune system. J Dairy Sci 1993, 76:2789-2794.
    • (1993) J Dairy Sci , vol.76 , pp. 2789-2794
    • Bendich, A.1
  • 23
    • 27644551262 scopus 로고    scopus 로고
    • Molecular cloning and characterization of cytosolic manganese superoxide dismutase (cytMn-SOD) from the giant freshwater prawn Macrobrachium rosenbergii
    • Cheng W., Tung Y.S., Liu C.H., Chen J.C. Molecular cloning and characterization of cytosolic manganese superoxide dismutase (cytMn-SOD) from the giant freshwater prawn Macrobrachium rosenbergii. Fish Shellfish Immunol 2006, 20:438-449.
    • (2006) Fish Shellfish Immunol , vol.20 , pp. 438-449
    • Cheng, W.1    Tung, Y.S.2    Liu, C.H.3    Chen, J.C.4
  • 24
    • 1542284717 scopus 로고    scopus 로고
    • Molecular cloning and expression of a mammalian homologue of a translationally controlled tumor protein (TCTP) gene from Peneaus monodon shrimp
    • Bangrak P., Graidist P., Chotigeat W., Phongdara A. Molecular cloning and expression of a mammalian homologue of a translationally controlled tumor protein (TCTP) gene from Peneaus monodon shrimp. J Biotechnol 2004, 108:219-226.
    • (2004) J Biotechnol , vol.108 , pp. 219-226
    • Bangrak, P.1    Graidist, P.2    Chotigeat, W.3    Phongdara, A.4
  • 25
    • 0028982775 scopus 로고
    • Molecular identification of an IgE-dependent histamine-releasing factor
    • MacDonald S.M., Rafnar T., Langdon J., Lichtenstein L.M. Molecular identification of an IgE-dependent histamine-releasing factor. Science 1995, 269:688-690.
    • (1995) Science , vol.269 , pp. 688-690
    • MacDonald, S.M.1    Rafnar, T.2    Langdon, J.3    Lichtenstein, L.M.4
  • 26
    • 0034665666 scopus 로고    scopus 로고
    • Human recombinant histamine-releasing factor activates human eosinophils and the eosinophilic cell line
    • Bheekha-Escura R., MacGlashan D.W., Langdon J.M., MacDonald S.M. Human recombinant histamine-releasing factor activates human eosinophils and the eosinophilic cell line. Blood 2000, 96:2191-2198.
    • (2000) Blood , vol.96 , pp. 2191-2198
    • Bheekha-Escura, R.1    MacGlashan, D.W.2    Langdon, J.M.3    MacDonald, S.M.4
  • 27
    • 0343337581 scopus 로고    scopus 로고
    • Molecular identification of IgE-dependent histamine-releasing factor as a B cell growth factor
    • Kang H.S., Lee M.J., Song H., Han S.H., Kim Y.M., Im J.Y., et al. Molecular identification of IgE-dependent histamine-releasing factor as a B cell growth factor. J Immunol 2001, 166:6545-6554.
    • (2001) J Immunol , vol.166 , pp. 6545-6554
    • Kang, H.S.1    Lee, M.J.2    Song, H.3    Han, S.H.4    Kim, Y.M.5    Im, J.Y.6
  • 28
    • 0019165508 scopus 로고
    • Organization of actin gene sequences in the sea urchin: molecular cloning of an intron-containing DNA sequence coding for a cytoplasmic actin
    • Urica D.S., Schloss J.A., Crain W.R. Organization of actin gene sequences in the sea urchin: molecular cloning of an intron-containing DNA sequence coding for a cytoplasmic actin. Proc Natl Acad Sci USA 1980, 77:5683-5687.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 5683-5687
    • Urica, D.S.1    Schloss, J.A.2    Crain, W.R.3
  • 29
    • 33746275536 scopus 로고    scopus 로고
    • Molecular characterization of the sarcoplasmic calcium-binding protein(SCP) from crayish Procambarus clarkii
    • Gao Y., Gillen C.M., Wheatly M.G. Molecular characterization of the sarcoplasmic calcium-binding protein(SCP) from crayish Procambarus clarkii. Comp Biochem Physiol B 2006, 144:478-487.
    • (2006) Comp Biochem Physiol B , vol.144 , pp. 478-487
    • Gao, Y.1    Gillen, C.M.2    Wheatly, M.G.3
  • 30
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - a splendid molecular machine
    • Boyer P.D. The ATP synthase - a splendid molecular machine. Annu Rev Biochem 1997, 66:717-749.
    • (1997) Annu Rev Biochem , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 31
    • 34250015780 scopus 로고    scopus 로고
    • Comparative analysis of differentially expressed genes in normal and white spot syndrome virus infected Penaeus monodon
    • Leu J.H., Chang C.C., Wu J.L., Hsu C.W., Hirono I., Aoki T., et al. Comparative analysis of differentially expressed genes in normal and white spot syndrome virus infected Penaeus monodon. BMC Genomics 2007, 8:120-134.
    • (2007) BMC Genomics , vol.8 , pp. 120-134
    • Leu, J.H.1    Chang, C.C.2    Wu, J.L.3    Hsu, C.W.4    Hirono, I.5    Aoki, T.6
  • 32
    • 0037162487 scopus 로고    scopus 로고
    • The molecular basis of the coloration mechanism in lobster shell: β-crustacyanin at 3.2-Å resolution
    • Cianci M., Rizkallah P.J., Olczak A., Raftery J., Chayen N.E., Zagalsky P.F., et al. The molecular basis of the coloration mechanism in lobster shell: β-crustacyanin at 3.2-Å resolution. Proc Natl Acad Sci USA 2002, 99:9795-9800.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9795-9800
    • Cianci, M.1    Rizkallah, P.J.2    Olczak, A.3    Raftery, J.4    Chayen, N.E.5    Zagalsky, P.F.6
  • 33
    • 20544473945 scopus 로고    scopus 로고
    • Esterified astaxanthin levels in lobster epithelia correlate with shell colour intensity: potential role in crustacean shell colour formation
    • Wade N., Goulter K.C., Wilson K.J., Hall M.R., Degnan B.M. Esterified astaxanthin levels in lobster epithelia correlate with shell colour intensity: potential role in crustacean shell colour formation. Comp Biochem Physiol B 2005, 141:307-313.
    • (2005) Comp Biochem Physiol B , vol.141 , pp. 307-313
    • Wade, N.1    Goulter, K.C.2    Wilson, K.J.3    Hall, M.R.4    Degnan, B.M.5
  • 34
    • 0021686359 scopus 로고
    • The covalent protein structure of insecticyanin, a blue biliprotein from the hemolymph of the tobacco hornworm Manduca sexta
    • Riley C.T., Barbeau B.K., Keim P.S., Kezdy F.J., Heinrikson R.L., Law J.H. The covalent protein structure of insecticyanin, a blue biliprotein from the hemolymph of the tobacco hornworm Manduca sexta. J Biol Chem 1984, 259:13159-13165.
    • (1984) J Biol Chem , vol.259 , pp. 13159-13165
    • Riley, C.T.1    Barbeau, B.K.2    Keim, P.S.3    Kezdy, F.J.4    Heinrikson, R.L.5    Law, J.H.6
  • 35
    • 0024537390 scopus 로고
    • Distribution and functions of lecithin:cholesterol acyltransferase and cholesteryl ester transfer protein in plasma lipoproteins. Evidence for a functional unit containing these activities together with apolipoproteins A-I and D that catalyzes the esterification and transfer of cell-derived cholesterol
    • Francone O.L., Gurakar A., Fielding C. Distribution and functions of lecithin:cholesterol acyltransferase and cholesteryl ester transfer protein in plasma lipoproteins. Evidence for a functional unit containing these activities together with apolipoproteins A-I and D that catalyzes the esterification and transfer of cell-derived cholesterol. J Biol Chem 1989, 264:7066-7072.
    • (1989) J Biol Chem , vol.264 , pp. 7066-7072
    • Francone, O.L.1    Gurakar, A.2    Fielding, C.3
  • 36
    • 0024205195 scopus 로고
    • Developmentally regulated synthesis of a low molecular weight protein (Ch 21) by differentiating chondrocytes
    • Cancedda F.D., Manduca P., Tacchetti C., Fossa P., Quarto R., Cancedda R. Developmentally regulated synthesis of a low molecular weight protein (Ch 21) by differentiating chondrocytes. J Cell Biol 1988, 107:2455-2463.
    • (1988) J Cell Biol , vol.107 , pp. 2455-2463
    • Cancedda, F.D.1    Manduca, P.2    Tacchetti, C.3    Fossa, P.4    Quarto, R.5    Cancedda, R.6
  • 38
    • 40849124354 scopus 로고    scopus 로고
    • Difference between hemocyanin subunits from shrimp Penaeus japonicus in anti-WSSV defense
    • Lei K., Li F., Zhang M., Yang H., Luo T., Xu X. Difference between hemocyanin subunits from shrimp Penaeus japonicus in anti-WSSV defense. Dev Comp Immunol 2008, 32:808-813.
    • (2008) Dev Comp Immunol , vol.32 , pp. 808-813
    • Lei, K.1    Li, F.2    Zhang, M.3    Yang, H.4    Luo, T.5    Xu, X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.