메뉴 건너뛰기




Volumn 26, Issue 3, 2009, Pages 459-466

Identification and cloning of the α2-macroglobulin of giant freshwater prawn Macrobrachium rosenbergii and its expression in relation with the molt stage and bacteria injection

Author keywords

Crustacean; Giant freshwater prawn; Macrobrachium rosenbergii; Molecular cloning; Molt cycle; Protease inhibitor; Real time PCR; 2 Macroglobulin

Indexed keywords

ARTHROPODA; BACTERIA (MICROORGANISMS); CRUSTACEA; LACTOCOCCUS; LACTOCOCCUS GARVIEAE; LITOPENAEUS VANNAMEI; MACROBRACHIUM ROSENBERGII; MARSUPENAEUS JAPONICUS; PENAEUS MONODON; SCYLLA SERRATA; VIBRIO ALGINOLYTICUS;

EID: 62749198593     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2009.01.007     Document Type: Article
Times cited : (36)

References (46)
  • 1
    • 0002939376 scopus 로고
    • Studies on yeast infection in cultured giant freshwater prawn (Macrobrachium rosenbergii)
    • Hsu J.P., and Liu C.I. Studies on yeast infection in cultured giant freshwater prawn (Macrobrachium rosenbergii). Fish Dis Res 5 (1994) 55-68
    • (1994) Fish Dis Res , vol.5 , pp. 55-68
    • Hsu, J.P.1    Liu, C.I.2
  • 2
    • 0032497628 scopus 로고    scopus 로고
    • Isolation and characterization of an enterococcus-like bacterium causing muscle necrosis and mortality in Macrobrachium rosenbergii in Taiwan
    • Cheng W., and Chen J.C. Isolation and characterization of an enterococcus-like bacterium causing muscle necrosis and mortality in Macrobrachium rosenbergii in Taiwan. Dis Aquat Org 34 (1998) 93-101
    • (1998) Dis Aquat Org , vol.34 , pp. 93-101
    • Cheng, W.1    Chen, J.C.2
  • 3
    • 0034694378 scopus 로고    scopus 로고
    • Shrimp immunity and disease control
    • Bachere E. Shrimp immunity and disease control. Aquaculture 191 (2000) 3-11
    • (2000) Aquaculture , vol.191 , pp. 3-11
    • Bachere, E.1
  • 4
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase-activating system in invertebrate immunity
    • Söderhäll K., and Cerenius L. Role of the prophenoloxidase-activating system in invertebrate immunity. Curr Opin Immunol 10 (1998) 23-28
    • (1998) Curr Opin Immunol , vol.10 , pp. 23-28
    • Söderhäll, K.1    Cerenius, L.2
  • 5
    • 0033141885 scopus 로고    scopus 로고
    • Editorial: invertebrate immunity
    • Söderhäll K. Editorial: invertebrate immunity. Dev Comp Immunol 23 (1999) 263-266
    • (1999) Dev Comp Immunol , vol.23 , pp. 263-266
    • Söderhäll, K.1
  • 6
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • Kanost M.R. Serine proteinase inhibitors in arthropod immunity. Dev Comp Immunol 23 (1999) 291-301
    • (1999) Dev Comp Immunol , vol.23 , pp. 291-301
    • Kanost, M.R.1
  • 7
    • 0026573162 scopus 로고
    • Alpha 2-macroglobulin: a protein at the interface of fibrinolysis and cellular growth regulation
    • Gonias S.L. Alpha 2-macroglobulin: a protein at the interface of fibrinolysis and cellular growth regulation. Exp Hematol 20 (1992) 302-311
    • (1992) Exp Hematol , vol.20 , pp. 302-311
    • Gonias, S.L.1
  • 8
    • 0027180969 scopus 로고
    • Alpha 2-macroglobulin is a binding protein of inhibin and activin
    • Vaughan J.M., and Vale W.W. Alpha 2-macroglobulin is a binding protein of inhibin and activin. Endocrinology 132 (1993) 2038-2050
    • (1993) Endocrinology , vol.132 , pp. 2038-2050
    • Vaughan, J.M.1    Vale, W.W.2
  • 9
    • 0020023831 scopus 로고
    • Functional modifications of alpha2-macroglobulin by primary amines: kinetics of inactivation of alpha 2-macroglobulin by methylamine, and formation of anomalous complexes with trypsin
    • Van Leuven F., Cassiman J.J., and van den Berghe H. Functional modifications of alpha2-macroglobulin by primary amines: kinetics of inactivation of alpha 2-macroglobulin by methylamine, and formation of anomalous complexes with trypsin. Biochem J 201 (1982) 119-128
    • (1982) Biochem J , vol.201 , pp. 119-128
    • Van Leuven, F.1    Cassiman, J.J.2    van den Berghe, H.3
  • 10
    • 0015896128 scopus 로고
    • The interaction of alpha 2-macroglobulin with proteinases: characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism
    • Barrett A.J., and Starkey P.M. The interaction of alpha 2-macroglobulin with proteinases: characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism. Biochem J 133 (1973) 709-724
    • (1973) Biochem J , vol.133 , pp. 709-724
    • Barrett, A.J.1    Starkey, P.M.2
  • 11
    • 0020134193 scopus 로고
    • Relation of internal thioesters to conformational change and receptor-recognition site in alpha2-macroglobulin complexes
    • Van Leuven F., Marynen P., Cassiman J.J., and van den Berghe H. Relation of internal thioesters to conformational change and receptor-recognition site in alpha2-macroglobulin complexes. Biochem J 203 (1982) 405-411
    • (1982) Biochem J , vol.203 , pp. 405-411
    • Van Leuven, F.1    Marynen, P.2    Cassiman, J.J.3    van den Berghe, H.4
  • 12
    • 33750038289 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of a thioester-containing alpha 2-macroglobulin (alpha 2-M) from the haemocytes of mud crab Scylla serrata
    • Vaseeharan B., Lin Y.C., Ko C.F., Chiou T.T., and Chen J.C. Molecular cloning and characterisation of a thioester-containing alpha 2-macroglobulin (alpha 2-M) from the haemocytes of mud crab Scylla serrata. Fish Shellfish Immunol 22 (2007) 115-130
    • (2007) Fish Shellfish Immunol , vol.22 , pp. 115-130
    • Vaseeharan, B.1    Lin, Y.C.2    Ko, C.F.3    Chiou, T.T.4    Chen, J.C.5
  • 13
    • 2442454655 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of alpha(2)-macroglobulin in the Kuruma shrimp, Marsupenaeus japonicus
    • Rattanachai A., Hirono I., Ohira T., Takahashi Y., and Aoki T. Molecular cloning and expression analysis of alpha(2)-macroglobulin in the Kuruma shrimp, Marsupenaeus japonicus. Fish Shellfish Immunol 16 (2004) 599-611
    • (2004) Fish Shellfish Immunol , vol.16 , pp. 599-611
    • Rattanachai, A.1    Hirono, I.2    Ohira, T.3    Takahashi, Y.4    Aoki, T.5
  • 14
    • 33748758437 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of a proteinase inhibitor, alpha 2-macroglobulin (alpha 2-M) from the haemocytes of tiger shrimp Penaeus monodon
    • Lin Y.C., Vaseeharan B., Ko C.F., Chiou T.T., and Chen J.C. Molecular cloning and characterisation of a proteinase inhibitor, alpha 2-macroglobulin (alpha 2-M) from the haemocytes of tiger shrimp Penaeus monodon. Mol Immunol 44 (2007) 1065-1074
    • (2007) Mol Immunol , vol.44 , pp. 1065-1074
    • Lin, Y.C.1    Vaseeharan, B.2    Ko, C.F.3    Chiou, T.T.4    Chen, J.C.5
  • 15
    • 37349103963 scopus 로고    scopus 로고
    • Molecular cloning and phylogenetic analysis on alpha2-macroglobulin (alpha2-M) of white shrimp Litopenaeus vannamei
    • Lin Y.C., Vaseeharan B., and Chen J.C. Molecular cloning and phylogenetic analysis on alpha2-macroglobulin (alpha2-M) of white shrimp Litopenaeus vannamei. Dev Comp Immunol 32 (2008) 317-329
    • (2008) Dev Comp Immunol , vol.32 , pp. 317-329
    • Lin, Y.C.1    Vaseeharan, B.2    Chen, J.C.3
  • 17
    • 0035796814 scopus 로고    scopus 로고
    • Hemolymph oxyhemocyanin, protein, osmolality and electrolyte levels of Macrobrachium rosenbergii in relation to size and molt stage
    • Cheng W., Liu C.H., Cheng C.H., and Chen J.C. Hemolymph oxyhemocyanin, protein, osmolality and electrolyte levels of Macrobrachium rosenbergii in relation to size and molt stage. Aquaculture 198 (2001) 387-400
    • (2001) Aquaculture , vol.198 , pp. 387-400
    • Cheng, W.1    Liu, C.H.2    Cheng, C.H.3    Chen, J.C.4
  • 18
    • 0037162874 scopus 로고    scopus 로고
    • Hemolymph oxyhemocyanin, protein, osmolality and electrolyte levels of whiteleg shrimp Litopenaeus vannamei in relation to size and molt stage
    • Cheng W., Liu C.H., Yan D.F., and Chen J.C. Hemolymph oxyhemocyanin, protein, osmolality and electrolyte levels of whiteleg shrimp Litopenaeus vannamei in relation to size and molt stage. Aquaculture 211 (2002) 325-339
    • (2002) Aquaculture , vol.211 , pp. 325-339
    • Cheng, W.1    Liu, C.H.2    Yan, D.F.3    Chen, J.C.4
  • 19
    • 0035234069 scopus 로고    scopus 로고
    • Effects of intrinsic and extrinsic factors on the haemocyte profile of the prawn, Macrobrachium rosenbergii
    • Cheng W., and Chen J.C. Effects of intrinsic and extrinsic factors on the haemocyte profile of the prawn, Macrobrachium rosenbergii. Fish Shellfish Immunol 11 (2001) 53-63
    • (2001) Fish Shellfish Immunol , vol.11 , pp. 53-63
    • Cheng, W.1    Chen, J.C.2
  • 20
    • 0037469011 scopus 로고    scopus 로고
    • The immune response of the giant freshwater prawn Macrobrachium rosenbergii and its susceptibility to Lactococcus garvieae in relation to the moult stage
    • Cheng W., Juang F.M., Li J.T., Lin M.C., Liu C.H., and Chen J.C. The immune response of the giant freshwater prawn Macrobrachium rosenbergii and its susceptibility to Lactococcus garvieae in relation to the moult stage. Aquaculture 218 (2003) 33-45
    • (2003) Aquaculture , vol.218 , pp. 33-45
    • Cheng, W.1    Juang, F.M.2    Li, J.T.3    Lin, M.C.4    Liu, C.H.5    Chen, J.C.6
  • 21
    • 33644998405 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of prophenoloxidase cDNA from haemocytes of the giant freshwater prawn, Macrobrachium rosenbergii, and its transcription in relation with the moult stage
    • Liu C.H., Tseng D.Y., Lai C.Y., Cheng W., and Kuo C.M. Molecular cloning and characterisation of prophenoloxidase cDNA from haemocytes of the giant freshwater prawn, Macrobrachium rosenbergii, and its transcription in relation with the moult stage. Fish Shellfish Immunol 21 (2006) 60-69
    • (2006) Fish Shellfish Immunol , vol.21 , pp. 60-69
    • Liu, C.H.1    Tseng, D.Y.2    Lai, C.Y.3    Cheng, W.4    Kuo, C.M.5
  • 22
    • 33845667800 scopus 로고    scopus 로고
    • Peroxinectin gene transcription of the giant freshwater prawn Macrobrachium rosenbergii under intrinsic, immunostimulant, and chemotherapeutant influences
    • Liu C.H., Yeh S.P., Hsu P.Y., and Cheng W. Peroxinectin gene transcription of the giant freshwater prawn Macrobrachium rosenbergii under intrinsic, immunostimulant, and chemotherapeutant influences. Fish Shellfish Immunol 22 (2007) 408-417
    • (2007) Fish Shellfish Immunol , vol.22 , pp. 408-417
    • Liu, C.H.1    Yeh, S.P.2    Hsu, P.Y.3    Cheng, W.4
  • 23
    • 0001151788 scopus 로고
    • A rapid technique for molt staging in live Macrobrachium rosenbergii
    • Peebles J.B. A rapid technique for molt staging in live Macrobrachium rosenbergii. Aquaculture 12 (1977) 173-180
    • (1977) Aquaculture , vol.12 , pp. 173-180
    • Peebles, J.B.1
  • 24
    • 33644994056 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of peroxinectin, a cell adhesion molecule, from the giant freshwater prawn Macrobrachium rosenbergii
    • Hsu P.I., Liu C.H., Tseng D.Y., Lee P.P., and Cheng W. Molecular cloning and characterisation of peroxinectin, a cell adhesion molecule, from the giant freshwater prawn Macrobrachium rosenbergii. Fish Shellfish Immunol 21 (2006) 1-10
    • (2006) Fish Shellfish Immunol , vol.21 , pp. 1-10
    • Hsu, P.I.1    Liu, C.H.2    Tseng, D.Y.3    Lee, P.P.4    Cheng, W.5
  • 26
    • 0019797407 scopus 로고
    • Evolutionary trees from DNA sequences: a maximum likelihood approach
    • Felsenstein J. Evolutionary trees from DNA sequences: a maximum likelihood approach. J Mol Evol 17 (1981) 368-376
    • (1981) J Mol Evol , vol.17 , pp. 368-376
    • Felsenstein, J.1
  • 27
    • 15944365891 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of prophenoloxidase from haemocytes of the white shrimp, Litopenaeus vannamei
    • Lai C.Y., Cheng W., and Kuo C.M. Molecular cloning and characterisation of prophenoloxidase from haemocytes of the white shrimp, Litopenaeus vannamei. Fish Shellfish Immunol 18 (2005) 417-430
    • (2005) Fish Shellfish Immunol , vol.18 , pp. 417-430
    • Lai, C.Y.1    Cheng, W.2    Kuo, C.M.3
  • 28
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak K.J., and Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25 (2001) 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 29
    • 0031817835 scopus 로고    scopus 로고
    • The inhibition of extracellular proteinases from Aphanomyces spp. by three different proteinase inhibitors from crayfish blood
    • Dieguez-Uribeondo J., and Cerenius L. The inhibition of extracellular proteinases from Aphanomyces spp. by three different proteinase inhibitors from crayfish blood. Mycol Res 102 (1998) 820-824
    • (1998) Mycol Res , vol.102 , pp. 820-824
    • Dieguez-Uribeondo, J.1    Cerenius, L.2
  • 30
    • 0025572540 scopus 로고
    • The proPO-system and associated proteins; role in cellular communication in arthropods
    • Söderhäll K., Aspan A., and Duvic B. The proPO-system and associated proteins; role in cellular communication in arthropods. Res Immunol 141 (1990) 896-907
    • (1990) Res Immunol , vol.141 , pp. 896-907
    • Söderhäll, K.1    Aspan, A.2    Duvic, B.3
  • 31
    • 0036076660 scopus 로고    scopus 로고
    • Early events in crustacean innate immunity
    • Lee S.Y., and Söderhäll K. Early events in crustacean innate immunity. Fish Shellfish Immunol 12 (2002) 421-437
    • (2002) Fish Shellfish Immunol , vol.12 , pp. 421-437
    • Lee, S.Y.1    Söderhäll, K.2
  • 34
    • 0024333351 scopus 로고
    • Alpha-macroglobulins: structure, shape, and mechanism of proteinase complex formation
    • Sottrup-Jensen L. Alpha-macroglobulins: structure, shape, and mechanism of proteinase complex formation. J Biol Chem 264 (1989) 11539-11542
    • (1989) J Biol Chem , vol.264 , pp. 11539-11542
    • Sottrup-Jensen, L.1
  • 35
    • 0024439479 scopus 로고
    • The alpha-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian alpha-macroglobulins
    • Sottrup-Jensen L., Sand O., Kristensen L., and Fey G.H. The alpha-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian alpha-macroglobulins. J Biol Chem 264 (1989) 15781-15789
    • (1989) J Biol Chem , vol.264 , pp. 15781-15789
    • Sottrup-Jensen, L.1    Sand, O.2    Kristensen, L.3    Fey, G.H.4
  • 36
    • 0034924843 scopus 로고    scopus 로고
    • The contribution of proteinase inhibitors to immune defense
    • Armstrong P.B. The contribution of proteinase inhibitors to immune defense. Trends Immunol 22 (2001) 47-52
    • (2001) Trends Immunol , vol.22 , pp. 47-52
    • Armstrong, P.B.1
  • 38
    • 0024980237 scopus 로고
    • Amino acid sequence around the thiolester of alpha 2-macroglobulin from plasma of the crayfish, Pacifastacus leniusculus
    • Hall M., Söderhäll K., and Sottrup-Jensen L. Amino acid sequence around the thiolester of alpha 2-macroglobulin from plasma of the crayfish, Pacifastacus leniusculus. FEBS Lett 254 (1989) 111-114
    • (1989) FEBS Lett , vol.254 , pp. 111-114
    • Hall, M.1    Söderhäll, K.2    Sottrup-Jensen, L.3
  • 39
    • 0033956456 scopus 로고    scopus 로고
    • Origin and evolution of the complement system
    • Nonaka M. Origin and evolution of the complement system. Curr Top Microbiol Immunol 248 (2000) 37-50
    • (2000) Curr Top Microbiol Immunol , vol.248 , pp. 37-50
    • Nonaka, M.1
  • 40
    • 0023002185 scopus 로고
    • The receptor-binding domain of human alpha 2-macroglobulin: isolation after limited proteolysis with a bacterial proteinase
    • Van Leuven F., Marynen P., Sottrup-Jensen L., Cassiman J.J., and van den Berghe H. The receptor-binding domain of human alpha 2-macroglobulin: isolation after limited proteolysis with a bacterial proteinase. J Biol Chem 261 (1986) 11369-11373
    • (1986) J Biol Chem , vol.261 , pp. 11369-11373
    • Van Leuven, F.1    Marynen, P.2    Sottrup-Jensen, L.3    Cassiman, J.J.4    van den Berghe, H.5
  • 41
    • 0031673224 scopus 로고    scopus 로고
    • Localization of basic residues required for receptor binding to the single alpha-helix of the receptor binding domain of human alpha2-macroglobulin
    • Huang W., Dolmer K., Liao X., and Gettins P.G. Localization of basic residues required for receptor binding to the single alpha-helix of the receptor binding domain of human alpha2-macroglobulin. Protein Sci 7 (1998) 2602-2612
    • (1998) Protein Sci , vol.7 , pp. 2602-2612
    • Huang, W.1    Dolmer, K.2    Liao, X.3    Gettins, P.G.4
  • 42
    • 38249007916 scopus 로고
    • Crayfish alpha-macroglobulin and 76 kDa protein; their biosynthesis and subcellular localization of the 76 kDa protein
    • Liang Z., Lindblad P., Beauvais A., Johansson M.W., Latge J.P., Hall M., et al. Crayfish alpha-macroglobulin and 76 kDa protein; their biosynthesis and subcellular localization of the 76 kDa protein. J Insect Physiol 38 (1992) 987-995
    • (1992) J Insect Physiol , vol.38 , pp. 987-995
    • Liang, Z.1    Lindblad, P.2    Beauvais, A.3    Johansson, M.W.4    Latge, J.P.5    Hall, M.6
  • 43
    • 0031142206 scopus 로고    scopus 로고
    • Haematological and phenoloxidase activity changes in the shrimp Penaeus stylirostris in relation with the moult cycle
    • Le Moullac G., Le Groumellec M., Ansquer D., Froissard S., Levy P., and Aquacop. Haematological and phenoloxidase activity changes in the shrimp Penaeus stylirostris in relation with the moult cycle. Fish Shellfish Immunol 7 (1997) 227-234
    • (1997) Fish Shellfish Immunol , vol.7 , pp. 227-234
    • Le Moullac, G.1    Le Groumellec, M.2    Ansquer, D.3    Froissard, S.4    Levy, P.5    Aquacop6
  • 44
    • 0037297165 scopus 로고    scopus 로고
    • Stimulation of peripheral blood mononuclear cells with lipopolysaccharide induces expression of the plasma protein alpha(2)-macroglobulin
    • Gunnarsson M., Frangsmyr L., Stigbrand T., and Jensen P.E.H. Stimulation of peripheral blood mononuclear cells with lipopolysaccharide induces expression of the plasma protein alpha(2)-macroglobulin. Protein Expr Purif 27 (2003) 238-243
    • (2003) Protein Expr Purif , vol.27 , pp. 238-243
    • Gunnarsson, M.1    Frangsmyr, L.2    Stigbrand, T.3    Jensen, P.E.H.4
  • 45
    • 0028979353 scopus 로고
    • Alpha 2-macroglobulin-mediated clearance of proteases from the plasma of the American horseshoe crab, Limulus polyphemus
    • Melchior R., Quigley J.P., and Armstrong P.B. Alpha 2-macroglobulin-mediated clearance of proteases from the plasma of the American horseshoe crab, Limulus polyphemus. J Biol Chem 270 (1995) 13496-13502
    • (1995) J Biol Chem , vol.270 , pp. 13496-13502
    • Melchior, R.1    Quigley, J.P.2    Armstrong, P.B.3
  • 46
    • 0032254201 scopus 로고    scopus 로고
    • Insect cell stimulation by LPS requires the activity of cell-released proteases
    • Wittwer D., and Wiesner A. Insect cell stimulation by LPS requires the activity of cell-released proteases. Arch Insect Biochem Physiol 39 (1998) 91-97
    • (1998) Arch Insect Biochem Physiol , vol.39 , pp. 91-97
    • Wittwer, D.1    Wiesner, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.