메뉴 건너뛰기




Volumn 23, Issue 6, 2007, Pages 1196-1208

Induction of phenoloxidase and other immunological activities in Sydney rock oysters challenged with microbial pathogen-associate molecular patterns

Author keywords

LPS; Phagocytosis; Phenoloxidase; Sydney rock oyster (Saccostrea glomerata); Zymosan

Indexed keywords

OSTREIDAE; SACCOSTREA GLOMERATA;

EID: 35648986570     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2007.05.003     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 27644578820 scopus 로고    scopus 로고
    • Cellular encapsulation and melanization are enhanced by immulectins, pattern recognition receptors from the tobacco hornworm Manduca sexta
    • Ling E., and Yu X.-Q. Cellular encapsulation and melanization are enhanced by immulectins, pattern recognition receptors from the tobacco hornworm Manduca sexta. Dev Comp Immunol 30 (2006) 289-299
    • (2006) Dev Comp Immunol , vol.30 , pp. 289-299
    • Ling, E.1    Yu, X.-Q.2
  • 2
    • 5144220046 scopus 로고    scopus 로고
    • Infectious non-self recognition in invertebrates: lessons from Drosophila and other insect models
    • Royet J. Infectious non-self recognition in invertebrates: lessons from Drosophila and other insect models. Mol Immunol 41 (2004) 1063-1075
    • (2004) Mol Immunol , vol.41 , pp. 1063-1075
    • Royet, J.1
  • 3
    • 0033046061 scopus 로고    scopus 로고
    • An 86 kDa diapause protein 1-like protein is a component of early-staged encapsulation-relating proteins in coleopteran insect, Tenebrio molitor larvae
    • Cho M.Y., Choi H.W., Moon G.Y., Kim M.H., Kwon T.H., Homma K.I., et al. An 86 kDa diapause protein 1-like protein is a component of early-staged encapsulation-relating proteins in coleopteran insect, Tenebrio molitor larvae. FEBS Lett 451 (1999) 303-307
    • (1999) FEBS Lett , vol.451 , pp. 303-307
    • Cho, M.Y.1    Choi, H.W.2    Moon, G.Y.3    Kim, M.H.4    Kwon, T.H.5    Homma, K.I.6
  • 5
    • 29344443249 scopus 로고    scopus 로고
    • Phagocytosis by Lymnaea stagnalis haemocytes: a potential role for phosphatidylinositol 3-kinase but not protein kinase A
    • Plows L.D., Cook R.T., Davies A.J., and Walker A.J. Phagocytosis by Lymnaea stagnalis haemocytes: a potential role for phosphatidylinositol 3-kinase but not protein kinase A. J Invertebr Pathol 91 (2006) 74-77
    • (2006) J Invertebr Pathol , vol.91 , pp. 74-77
    • Plows, L.D.1    Cook, R.T.2    Davies, A.J.3    Walker, A.J.4
  • 6
    • 0035962034 scopus 로고    scopus 로고
    • Effects of in vivo exposure of Mya arenaria to organic and inorganic mercury on phagocytic activity of hemocytes
    • Fournier M., Pellerin J., Clermont Y., Morin Y., and Brousseau P. Effects of in vivo exposure of Mya arenaria to organic and inorganic mercury on phagocytic activity of hemocytes. Toxicology 161 (2001) 201-211
    • (2001) Toxicology , vol.161 , pp. 201-211
    • Fournier, M.1    Pellerin, J.2    Clermont, Y.3    Morin, Y.4    Brousseau, P.5
  • 7
    • 0001692340 scopus 로고
    • Bivalves
    • Ratcliffe N.A., and Rowley A.F. (Eds), Academic Press, London
    • Cheng T.C. Bivalves. In: Ratcliffe N.A., and Rowley A.F. (Eds). Invertebrate blood cells (1981), Academic Press, London 233-300
    • (1981) Invertebrate blood cells , pp. 233-300
    • Cheng, T.C.1
  • 8
    • 0016670053 scopus 로고
    • A quantitative study of phagocytosis by hemolymph cells of the pelecypods Crassostrea virginica and Mercenaria mercenaria
    • Foley D.A., and Cheng T.C. A quantitative study of phagocytosis by hemolymph cells of the pelecypods Crassostrea virginica and Mercenaria mercenaria. J Invertebr Pathol 25 (1975) 189-197
    • (1975) J Invertebr Pathol , vol.25 , pp. 189-197
    • Foley, D.A.1    Cheng, T.C.2
  • 9
    • 0033862794 scopus 로고    scopus 로고
    • In vitro production of superoxide and nitric oxide (as nitrite and nitrate) by Mytilus galloprovincialis haemocytes upon incubation with PMA or laminarin or during yeast phagocytosis
    • Arumugam M., Romestand B., Torreilles J., and Roch P. In vitro production of superoxide and nitric oxide (as nitrite and nitrate) by Mytilus galloprovincialis haemocytes upon incubation with PMA or laminarin or during yeast phagocytosis. Eur J Cell Biol 79 (2000) 513-519
    • (2000) Eur J Cell Biol , vol.79 , pp. 513-519
    • Arumugam, M.1    Romestand, B.2    Torreilles, J.3    Roch, P.4
  • 10
    • 0033106065 scopus 로고    scopus 로고
    • Defense mechanisms and disease prevention in farmed marine invertebrates
    • Roch P. Defense mechanisms and disease prevention in farmed marine invertebrates. Aquaculture 172 (1999) 125-145
    • (1999) Aquaculture , vol.172 , pp. 125-145
    • Roch, P.1
  • 11
    • 16844374403 scopus 로고    scopus 로고
    • Anticipating innate immunity without a Toll
    • Engelmann P., Cooper E.L., and Nemeth P. Anticipating innate immunity without a Toll. Mol Immunol 42 (2005) 931-942
    • (2005) Mol Immunol , vol.42 , pp. 931-942
    • Engelmann, P.1    Cooper, E.L.2    Nemeth, P.3
  • 12
    • 33646532402 scopus 로고    scopus 로고
    • Host defence peptides from invertebrates - emerging antimicrobial strategies
    • Hancock R.E.W., Brown K.L., and Mookherjee N. Host defence peptides from invertebrates - emerging antimicrobial strategies. Immunobiology 211 (2006) 315-322
    • (2006) Immunobiology , vol.211 , pp. 315-322
    • Hancock, R.E.W.1    Brown, K.L.2    Mookherjee, N.3
  • 13
    • 0343090209 scopus 로고    scopus 로고
    • Activation of the prophenoloxidase system of the brown shrimp Penaeus californiensis Holmes
    • Hernandez-Lopez J., Gollas-Galvan T., and Vargas-Albores F. Activation of the prophenoloxidase system of the brown shrimp Penaeus californiensis Holmes. Comp Biochem Physiol C 113 (1996) 61-66
    • (1996) Comp Biochem Physiol C , vol.113 , pp. 61-66
    • Hernandez-Lopez, J.1    Gollas-Galvan, T.2    Vargas-Albores, F.3
  • 14
    • 0025748686 scopus 로고
    • A comparison of phenoloxidase activity in the blood cells of marine invertebrates
    • Smith V.J., and Söderhäll K. A comparison of phenoloxidase activity in the blood cells of marine invertebrates. Dev Comp Immunol 15 (1991) 251-261
    • (1991) Dev Comp Immunol , vol.15 , pp. 251-261
    • Smith, V.J.1    Söderhäll, K.2
  • 15
    • 48749142242 scopus 로고
    • β-1,3-Glucan induced cellular defence reactions in the shore crab, Carcinus maenas
    • Smith V.J., Söderhäll K., and Hamilton M. β-1,3-Glucan induced cellular defence reactions in the shore crab, Carcinus maenas. Comp Biochem Physiol A 77 (1984) 635-639
    • (1984) Comp Biochem Physiol A , vol.77 , pp. 635-639
    • Smith, V.J.1    Söderhäll, K.2    Hamilton, M.3
  • 16
    • 0026056099 scopus 로고
    • Activation of the prophenoloxidase cascade and initiation of nodule formation in locusts by bacterial lipopolysaccharides
    • Ratcliffe N.A., Brookman J.L., and Rowley A.F. Activation of the prophenoloxidase cascade and initiation of nodule formation in locusts by bacterial lipopolysaccharides. Dev Comp Immunol 15 (1991) 33-39
    • (1991) Dev Comp Immunol , vol.15 , pp. 33-39
    • Ratcliffe, N.A.1    Brookman, J.L.2    Rowley, A.F.3
  • 17
    • 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
  • 18
    • 0021104169 scopus 로고
    • Activation of pro-phenoloxidase by bacterial cell walls or β-1,3-glucans in plasma of the silkworm
    • Ashida M., Ishizaki Y., and Iwahana H. Activation of pro-phenoloxidase by bacterial cell walls or β-1,3-glucans in plasma of the silkworm. Biochem Biophys Res Commun 113 (1983) 562-568
    • (1983) Biochem Biophys Res Commun , vol.113 , pp. 562-568
    • Ashida, M.1    Ishizaki, Y.2    Iwahana, H.3
  • 20
    • 0027463054 scopus 로고
    • In vitro phenoloxidase activity in the blood of Ciona intestinalis and other ascidians
    • Jackson A.D., Smith V.J., and Peddie C.M. In vitro phenoloxidase activity in the blood of Ciona intestinalis and other ascidians. Dev Comp Immunol 17 (1993) 97-108
    • (1993) Dev Comp Immunol , vol.17 , pp. 97-108
    • Jackson, A.D.1    Smith, V.J.2    Peddie, C.M.3
  • 21
    • 0742305683 scopus 로고    scopus 로고
    • From the Cover: a serine protease zymogen functions as a pattern-recognition receptor for lipopolysaccharides
    • Ariki S., Koori K., Osaki T., Motoyama K., Inamori K.I., and Kawabata S.I. From the Cover: a serine protease zymogen functions as a pattern-recognition receptor for lipopolysaccharides. Proc Natl Acad Sci USA 101 (2004) 953-958
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 953-958
    • Ariki, S.1    Koori, K.2    Osaki, T.3    Motoyama, K.4    Inamori, K.I.5    Kawabata, S.I.6
  • 22
    • 0034694375 scopus 로고    scopus 로고
    • The proPO and clotting system in crustaceans
    • Sritunyalucksana K., and Söderhäll K. The proPO and clotting system in crustaceans. Aquaculture 191 (2000) 53-69
    • (2000) Aquaculture , vol.191 , pp. 53-69
    • Sritunyalucksana, K.1    Söderhäll, K.2
  • 23
    • 0001261788 scopus 로고
    • Biochemistry of the prophenoloxidase system in insects with special reference to its activation
    • Onishi E., and Ishizaki H. (Eds), Science Society Press, Tokyo
    • Ashida M., and Yamazaki H.I. Biochemistry of the prophenoloxidase system in insects with special reference to its activation. In: Onishi E., and Ishizaki H. (Eds). Moulting and metamorphosis (1990), Science Society Press, Tokyo 239-265
    • (1990) Moulting and metamorphosis , pp. 239-265
    • Ashida, M.1    Yamazaki, H.I.2
  • 24
    • 20444377685 scopus 로고    scopus 로고
    • MAP kinases mediate phagocytosis and melanization via prophenoloxidase activation in medfly hemocytes
    • Mavrouli M.D., Tsakas S., Theodorou G.L., Lampropoulou M., and Marmaras V.J. MAP kinases mediate phagocytosis and melanization via prophenoloxidase activation in medfly hemocytes. Biochim Biophys Acta 1744 (2005) 145-156
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 145-156
    • Mavrouli, M.D.1    Tsakas, S.2    Theodorou, G.L.3    Lampropoulou, M.4    Marmaras, V.J.5
  • 25
    • 0029686049 scopus 로고    scopus 로고
    • Immune response in insects: the role of phenoloxidase in defense reactions in relation to melanization and sclerotization
    • Marmaras V.J., Charalambidis N.D., and Zervas C.G. Immune response in insects: the role of phenoloxidase in defense reactions in relation to melanization and sclerotization. Arch Insect Biochem Physiol 31 (1996) 119-133
    • (1996) Arch Insect Biochem Physiol , vol.31 , pp. 119-133
    • Marmaras, V.J.1    Charalambidis, N.D.2    Zervas, C.G.3
  • 26
    • 17844370578 scopus 로고    scopus 로고
    • Manduca sexta prophenoloxidase activating proteinase-1 (PAP-1) gene: organization, expression, and regulation by immune and hormonal signals
    • Zou Z., Wang Y., and Jiang H. Manduca sexta prophenoloxidase activating proteinase-1 (PAP-1) gene: organization, expression, and regulation by immune and hormonal signals. Insect Biochem Mol Biol 35 (2005) 627-636
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 627-636
    • Zou, Z.1    Wang, Y.2    Jiang, H.3
  • 27
    • 0002723111 scopus 로고    scopus 로고
    • Roles of the insect cuticle in immunity
    • Söderhäll K., Iwanga S., and Vasta G. (Eds), SOS Publications, Fair Haven, FL
    • Sugumaran M. Roles of the insect cuticle in immunity. In: Söderhäll K., Iwanga S., and Vasta G. (Eds). New directions in invertebrate immunology (1996), SOS Publications, Fair Haven, FL 355-374
    • (1996) New directions in invertebrate immunology , pp. 355-374
    • Sugumaran, M.1
  • 29
    • 0032125335 scopus 로고    scopus 로고
    • Functional analysis of plasma prophenoloxidase system in the marine mussel Perna viridis
    • Asokan R., Arumugam M., and Mullainadhan P. Functional analysis of plasma prophenoloxidase system in the marine mussel Perna viridis. Comp Biochem Physiol A 120 (1998) 753-762
    • (1998) Comp Biochem Physiol A , vol.120 , pp. 753-762
    • Asokan, R.1    Arumugam, M.2    Mullainadhan, P.3
  • 30
    • 33747196988 scopus 로고    scopus 로고
    • Location of intrinsic and inducible phenoloxidase activity in molluscan hemocyanin
    • Siddiqui N.I., Akosung R.F., and Gielens C. Location of intrinsic and inducible phenoloxidase activity in molluscan hemocyanin. Biochem Biophys Res Commun 348 (2006) 1138-1144
    • (2006) Biochem Biophys Res Commun , vol.348 , pp. 1138-1144
    • Siddiqui, N.I.1    Akosung, R.F.2    Gielens, C.3
  • 32
    • 0028618906 scopus 로고
    • Phagocytosis in the colonial ascidian Botryllus schlosseri
    • Ballarin L., Cima F., and Sabbadin A. Phagocytosis in the colonial ascidian Botryllus schlosseri. Dev Comp Immunol 18 (1994) 467-481
    • (1994) Dev Comp Immunol , vol.18 , pp. 467-481
    • Ballarin, L.1    Cima, F.2    Sabbadin, A.3
  • 33
    • 0002821345 scopus 로고
    • Lipopolysaccharide-induced activation of prophenoloxidase activating system in crayfish haemocyte lysate
    • Söderhäll K., and Hall L. Lipopolysaccharide-induced activation of prophenoloxidase activating system in crayfish haemocyte lysate. Biochim Biophys Acta 797 (1984) 99-104
    • (1984) Biochim Biophys Acta , vol.797 , pp. 99-104
    • Söderhäll, K.1    Hall, L.2
  • 34
    • 3342960004 scopus 로고    scopus 로고
    • Flow cytometric analysis of crayfish haemocytes activated by lipopolysaccharides
    • Cardenas W., Dankert J.R., and Jenkins J.A. Flow cytometric analysis of crayfish haemocytes activated by lipopolysaccharides. Fish Shellfish Immunol 17 (2004) 223-233
    • (2004) Fish Shellfish Immunol , vol.17 , pp. 223-233
    • Cardenas, W.1    Dankert, J.R.2    Jenkins, J.A.3
  • 35
    • 0030812370 scopus 로고    scopus 로고
    • Activation of prophenoloxidase in the plasma and haemocytes of the marine mussel, Perna viridis Linnaeus
    • Asokan R., Arumugam M., and Mullainadhan P. Activation of prophenoloxidase in the plasma and haemocytes of the marine mussel, Perna viridis Linnaeus. Dev Comp Immunol 21 (1997) 1-12
    • (1997) Dev Comp Immunol , vol.21 , pp. 1-12
    • Asokan, R.1    Arumugam, M.2    Mullainadhan, P.3
  • 36
    • 0001580238 scopus 로고
    • Phenoloxidase activity in the haemolymph and haemocytes of the marine mussel Mytilus edulis
    • Coles J.A., and Pipe R.K. Phenoloxidase activity in the haemolymph and haemocytes of the marine mussel Mytilus edulis. Fish Shellfish Immunol 4 (1994) 337-352
    • (1994) Fish Shellfish Immunol , vol.4 , pp. 337-352
    • Coles, J.A.1    Pipe, R.K.2
  • 37
    • 0031184815 scopus 로고    scopus 로고
    • Phenoloxidase specific activity in the red swamp crayfish Procambarus clarkii
    • Cardenas W., and Dankert J.R. Phenoloxidase specific activity in the red swamp crayfish Procambarus clarkii. Fish Shellfish Immunol 7 (1997) 283-295
    • (1997) Fish Shellfish Immunol , vol.7 , pp. 283-295
    • Cardenas, W.1    Dankert, J.R.2
  • 38
    • 0033597134 scopus 로고    scopus 로고
    • A pattern recognition protein for peptidoglycan: cloning the cDNA and the gene of the silkworm, Bombyx mori
    • Ochiai M., and Ashida M. A pattern recognition protein for peptidoglycan: cloning the cDNA and the gene of the silkworm, Bombyx mori. J Biol Chem 274 (1999) 11854-11858
    • (1999) J Biol Chem , vol.274 , pp. 11854-11858
    • Ochiai, M.1    Ashida, M.2
  • 39
    • 33748761934 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a lipopolysaccharide and β-1,3-glucan binding protein from fleshy prawn (Fenneropenaeus chinensis)
    • Du X.-J., Zhao X.-F., and Wang J.-X. Molecular cloning and characterization of a lipopolysaccharide and β-1,3-glucan binding protein from fleshy prawn (Fenneropenaeus chinensis). Mol Immunol 44 (2007) 1085-1094
    • (2007) Mol Immunol , vol.44 , pp. 1085-1094
    • Du, X.-J.1    Zhao, X.-F.2    Wang, J.-X.3
  • 40
    • 0343415656 scopus 로고    scopus 로고
    • A Lipopolysaccharide- and β -1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus. purification, characterization, and cDNA cloning
    • Lee S.Y., Wang R., and Söderhäll K. A Lipopolysaccharide- and β -1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus. purification, characterization, and cDNA cloning. J Biol Chem 275 (2000) 1337-1343
    • (2000) J Biol Chem , vol.275 , pp. 1337-1343
    • Lee, S.Y.1    Wang, R.2    Söderhäll, K.3
  • 41
    • 0030835326 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding proteins and their involvement in the bacterial clearance from the hemolymph of the silkworm Bombyx mori
    • Koizumi N., Morozumi A., Imamura M., Tanaka E., Iwahana H., and Sato R. Lipopolysaccharide-binding proteins and their involvement in the bacterial clearance from the hemolymph of the silkworm Bombyx mori. Eur J Biochem 248 (1997) 217-224
    • (1997) Eur J Biochem , vol.248 , pp. 217-224
    • Koizumi, N.1    Morozumi, A.2    Imamura, M.3    Tanaka, E.4    Iwahana, H.5    Sato, R.6
  • 42
    • 0032516658 scopus 로고    scopus 로고
    • Crystal Structure of hemolin: a horseshoe shape with implications for homophilic adhesion
    • Su X.-D., Gastinel L.N., Vaughn D.E., Faye I., Poon P., and Bjorkman P.J. Crystal Structure of hemolin: a horseshoe shape with implications for homophilic adhesion. Science 281 (1998) 991-995
    • (1998) Science , vol.281 , pp. 991-995
    • Su, X.-D.1    Gastinel, L.N.2    Vaughn, D.E.3    Faye, I.4    Poon, P.5    Bjorkman, P.J.6
  • 43
    • 0033524926 scopus 로고    scopus 로고
    • A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes specific O-antigens of bacterial lipopolysaccharides
    • Inamori K.I., Saito T., Iwaki D., Nagira T., Iwanaga S., Arisaka F., et al. A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes specific O-antigens of bacterial lipopolysaccharides. J Biol Chem 274 (1999) 3272-3278
    • (1999) J Biol Chem , vol.274 , pp. 3272-3278
    • Inamori, K.I.1    Saito, T.2    Iwaki, D.3    Nagira, T.4    Iwanaga, S.5    Arisaka, F.6
  • 44
    • 0034019343 scopus 로고    scopus 로고
    • Cytotoxicity and cytotoxic molecules in invertebrates
    • Nappi A.J., and Ottaviani E. Cytotoxicity and cytotoxic molecules in invertebrates. BioEssays 22 (2000) 469-480
    • (2000) BioEssays , vol.22 , pp. 469-480
    • Nappi, A.J.1    Ottaviani, E.2
  • 45
    • 0029981365 scopus 로고    scopus 로고
    • The o-diphenol oxidase activity of arthropod hemocyanin
    • Zlateva T., Di Muro P., Salvato B., and Beltramini M. The o-diphenol oxidase activity of arthropod hemocyanin. FEBS Lett 384 (1996) 251-254
    • (1996) FEBS Lett , vol.384 , pp. 251-254
    • Zlateva, T.1    Di Muro, P.2    Salvato, B.3    Beltramini, M.4
  • 46
    • 0032491185 scopus 로고    scopus 로고
    • The enzymatic properties of Octopus vulgaris hemocyanin: o-diphenol oxidase activity
    • Salvato B., Santamaria M., Beltramini M., Alzuet G., and Casella L. The enzymatic properties of Octopus vulgaris hemocyanin: o-diphenol oxidase activity. Biochemistry 37 (1998) 14065-14077
    • (1998) Biochemistry , vol.37 , pp. 14065-14077
    • Salvato, B.1    Santamaria, M.2    Beltramini, M.3    Alzuet, G.4    Casella, L.5
  • 47
    • 33646162208 scopus 로고    scopus 로고
    • Effects of infection of EGFP-expressing Escherichia coli on haemocytes in Ciona intestinalis
    • Liu L., Wu C., Chen T., Zhang X., Li F., Luo W., et al. Effects of infection of EGFP-expressing Escherichia coli on haemocytes in Ciona intestinalis. J Exp Mar Biol Ecol 332 (2006) 121-134
    • (2006) J Exp Mar Biol Ecol , vol.332 , pp. 121-134
    • Liu, L.1    Wu, C.2    Chen, T.3    Zhang, X.4    Li, F.5    Luo, W.6
  • 50
    • 34547842131 scopus 로고    scopus 로고
    • Sydney rock oyster (Saccostrea glomerata) hemocytes: morphology and function
    • 10.1016/j.jip.2007.02.011
    • Aladaileh S., Nair S.V., Birch D., and Raftos D.A. Sydney rock oyster (Saccostrea glomerata) hemocytes: morphology and function. J Invertebr Pathol (2007) 10.1016/j.jip.2007.02.011
    • (2007) J Invertebr Pathol
    • Aladaileh, S.1    Nair, S.V.2    Birch, D.3    Raftos, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.