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Volumn 38, Issue 1, 2008, Pages 99-112

Eicosanoids mediate prophenoloxidase release from oenocytoids in the beet armyworm Spodoptera exigua

Author keywords

Eicosanoids; Oenocytoids; PLA2; Prophenoloxidase; Spodoptera exigua; Xenorhabdus nematophila

Indexed keywords

CATECHOL OXIDASE; DEXAMETHASONE; ENZYME PRECURSOR; ICOSANOID; MONOPHENOL MONOOXYGENASE; PHOSPHOLIPASE A2; PRO PHENOLOXIDASE; PRO-PHENOLOXIDASE; UNCLASSIFIED DRUG;

EID: 36749076932     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2007.09.013     Document Type: Article
Times cited : (120)

References (71)
  • 1
    • 0001304960 scopus 로고
    • Morphological and functional dimorphism in Xenorhabdus spp., bacteria symbiotically associated with the insect pathogenic nematodes Neoaplectana and Heterorhabditis
    • Akhurst R.J. Morphological and functional dimorphism in Xenorhabdus spp., bacteria symbiotically associated with the insect pathogenic nematodes Neoaplectana and Heterorhabditis. J. Gen. Microbiol. 121 (1980) 303-309
    • (1980) J. Gen. Microbiol. , vol.121 , pp. 303-309
    • Akhurst, R.J.1
  • 2
    • 0000926038 scopus 로고    scopus 로고
    • Recent advances on the research of the insect prophenoloxidase cascade
    • Brey P.T., and Hultmark D. (Eds), Chapman & Hall, London
    • Ashida M., and Brey P.T. Recent advances on the research of the insect prophenoloxidase cascade. In: Brey P.T., and Hultmark D. (Eds). Molecular Mechanisms of Immune Responses in Insects (1998), Chapman & Hall, London 135-172
    • (1998) Molecular Mechanisms of Immune Responses in Insects , pp. 135-172
    • Ashida, M.1    Brey, P.T.2
  • 3
    • 0025361114 scopus 로고
    • Studies on prophenol oxidase activation in the mosquito Aedes aegypti L
    • Ashida M., Kinoshita K., and Brey P.T. Studies on prophenol oxidase activation in the mosquito Aedes aegypti L. Eur. J. Biochem. 188 (1990) 507-515
    • (1990) Eur. J. Biochem. , vol.188 , pp. 507-515
    • Ashida, M.1    Kinoshita, K.2    Brey, P.T.3
  • 4
    • 0002657568 scopus 로고
    • Characterization of haemolymph protyrosinase and a cuticular activator from Manduca sexta
    • Aso Y., Kramer K.J., Hopkins T.L., and Lookhart G.L. Characterization of haemolymph protyrosinase and a cuticular activator from Manduca sexta. Insect Biochem 15 (1985) 9-17
    • (1985) Insect Biochem , vol.15 , pp. 9-17
    • Aso, Y.1    Kramer, K.J.2    Hopkins, T.L.3    Lookhart, G.L.4
  • 5
    • 0028853375 scopus 로고
    • cDNA cloning of prophenol oxidase from the freshwater crayfish Pacifasticus leniusculus and its activation
    • Aspan A., Huang T.S., Cerenius L., and Söderhäll K. cDNA cloning of prophenol oxidase from the freshwater crayfish Pacifasticus leniusculus and its activation. Proc. Natl. Acad. Sci. USA 92 (1995) 939-943
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 939-943
    • Aspan, A.1    Huang, T.S.2    Cerenius, L.3    Söderhäll, K.4
  • 6
    • 34248216101 scopus 로고    scopus 로고
    • Crystal cell rupture after injury in Drosophila requires the JNK pathway, small GTPases and the TNF homolog Eiger
    • Bidla G., Dushay M.S., and Theopold U. Crystal cell rupture after injury in Drosophila requires the JNK pathway, small GTPases and the TNF homolog Eiger. J. Cell Sci. 120 (2007) 1209-1215
    • (2007) J. Cell Sci. , vol.120 , pp. 1209-1215
    • Bidla, G.1    Dushay, M.S.2    Theopold, U.3
  • 7
    • 33845913239 scopus 로고    scopus 로고
    • Eicosanoids mediate Galleria mellonella cellular immune response to viral infection
    • Büyükgüzel E., Tunaz H., Stanley D., and Büyükgüzel K. Eicosanoids mediate Galleria mellonella cellular immune response to viral infection. J. Insect Physiol. 53 (2007) 99-105
    • (2007) J. Insect Physiol. , vol.53 , pp. 99-105
    • Büyükgüzel, E.1    Tunaz, H.2    Stanley, D.3    Büyükgüzel, K.4
  • 8
    • 0036246370 scopus 로고    scopus 로고
    • Dexamethasone inhibition of the cellular immune response of Drosophila melanogaster against a parasitoid
    • Carton Y., Frey F., Stanley D.W., Vass E., and Nappi A.J. Dexamethasone inhibition of the cellular immune response of Drosophila melanogaster against a parasitoid. J. Parasitol. 88 (2002) 405-407
    • (2002) J. Parasitol. , vol.88 , pp. 405-407
    • Carton, Y.1    Frey, F.2    Stanley, D.W.3    Vass, E.4    Nappi, A.J.5
  • 9
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • Cerenius L., and Söderhäll K. The prophenoloxidase-activating system in invertebrates. Immunol. Rev. 198 (2004) 116-126
    • (2004) Immunol. Rev. , vol.198 , pp. 116-126
    • Cerenius, L.1    Söderhäll, K.2
  • 10
    • 0037066464 scopus 로고    scopus 로고
    • Requirement for a peptidoglycan recognition protein (PGRP) in relish activation and antibacterial immune responses in Drosophila
    • Choe K.-M., Werner T., Stöven S., Hultmark D., and Anderson K.V. Requirement for a peptidoglycan recognition protein (PGRP) in relish activation and antibacterial immune responses in Drosophila. Science 296 (2002) 359-362
    • (2002) Science , vol.296 , pp. 359-362
    • Choe, K.-M.1    Werner, T.2    Stöven, S.3    Hultmark, D.4    Anderson, K.V.5
  • 11
    • 0018829656 scopus 로고
    • Chemical and enzymatic syntheses of 5-HPETE, a key biological precursor of slow-reacting substances of anaphylaxis (SRS) and 5-HETE
    • Corey E.J., Albright J.O., Barton A.E., and Hashimoto S. Chemical and enzymatic syntheses of 5-HPETE, a key biological precursor of slow-reacting substances of anaphylaxis (SRS) and 5-HETE. J. Am. Chem. Soc. 102 (1980) 1435-1436
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 1435-1436
    • Corey, E.J.1    Albright, J.O.2    Barton, A.E.3    Hashimoto, S.4
  • 12
    • 0035983790 scopus 로고    scopus 로고
    • Modulation by eicosanoid biosynthesis inhibitors of immune responses by the insect Manduca sexta to the pathogenic fungus Metarhizium aniopliae
    • Dean P., Gadsden J.C., Richards E.H., Edwards J.P., Charnley A.K., and Reynolds S.E. Modulation by eicosanoid biosynthesis inhibitors of immune responses by the insect Manduca sexta to the pathogenic fungus Metarhizium aniopliae. J. Invertebr. Pathol. 79 (2002) 93-101
    • (2002) J. Invertebr. Pathol. , vol.79 , pp. 93-101
    • Dean, P.1    Gadsden, J.C.2    Richards, E.H.3    Edwards, J.P.4    Charnley, A.K.5    Reynolds, S.E.6
  • 13
    • 0000496402 scopus 로고
    • Lipopolysaccharides of Xenorhabdus nematophilus (Enterobacteriaceae) and their haemocyte toxicity in non-immune Galleria mellonella (Insecta: Lepidoptera) larvae
    • Dunphy G.B., and Webster J.M. Lipopolysaccharides of Xenorhabdus nematophilus (Enterobacteriaceae) and their haemocyte toxicity in non-immune Galleria mellonella (Insecta: Lepidoptera) larvae. J. Gen. Microbiol. 134 (1988) 1017-1028
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1017-1028
    • Dunphy, G.B.1    Webster, J.M.2
  • 16
    • 1542350675 scopus 로고    scopus 로고
    • Effects of eicosanoid biosynthesis inhibitors on the prophenoloxidase-activating system and microaggregation reactions in the hemolymph of Rhodnius prolixus infected with Trypanosoma rangeli
    • Garcia E.S., Machado E.M.M., and Azambuja P. Effects of eicosanoid biosynthesis inhibitors on the prophenoloxidase-activating system and microaggregation reactions in the hemolymph of Rhodnius prolixus infected with Trypanosoma rangeli. J. Insect Physiol. 50 (2004) 157-165
    • (2004) J. Insect Physiol. , vol.50 , pp. 157-165
    • Garcia, E.S.1    Machado, E.M.M.2    Azambuja, P.3
  • 17
    • 0032894442 scopus 로고    scopus 로고
    • Monoclonal antibodies bind distinct classes of hemocytes in the moth, Pseudoplusia includens
    • Gardiner E.M.M., and Strand M.R. Monoclonal antibodies bind distinct classes of hemocytes in the moth, Pseudoplusia includens. J. Insect Physiol. 45 (1999) 113-126
    • (1999) J. Insect Physiol. , vol.45 , pp. 113-126
    • Gardiner, E.M.M.1    Strand, M.R.2
  • 18
    • 0003072571 scopus 로고
    • Simple mass-rearing of beet armyworm, Spodoptera exigua (Hübner) (Lepidoptera: Noctuidae), on an artificial diet
    • Gho H.G., Lee S.G., Lee B.P., Choi K.M., and Kim J.H. Simple mass-rearing of beet armyworm, Spodoptera exigua (Hübner) (Lepidoptera: Noctuidae), on an artificial diet. Kor. J. Appl. Entomol. 29 (1990) 180-183
    • (1990) Kor. J. Appl. Entomol. , vol.29 , pp. 180-183
    • Gho, H.G.1    Lee, S.G.2    Lee, B.P.3    Choi, K.M.4    Kim, J.H.5
  • 19
    • 0043131983 scopus 로고    scopus 로고
    • Adipokinetic hormone enhances nodule formation and phenoloxidase activation in adult locusts injected with bacterial lipopolysaccharide
    • Goldsworthy G., Chandrakant S., and Opoku-Ware K. Adipokinetic hormone enhances nodule formation and phenoloxidase activation in adult locusts injected with bacterial lipopolysaccharide. J. Insect Physiol. 49 (2003) 795-803
    • (2003) J. Insect Physiol. , vol.49 , pp. 795-803
    • Goldsworthy, G.1    Chandrakant, S.2    Opoku-Ware, K.3
  • 20
    • 0037061450 scopus 로고    scopus 로고
    • The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein
    • Gottar M., Gobert V., Michel T., Belvin M., Duyk G., Hoffman J.A., Ferrandon D., and Royet J. The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature 416 (2002) 640-644
    • (2002) Nature , vol.416 , pp. 640-644
    • Gottar, M.1    Gobert, V.2    Michel, T.3    Belvin, M.4    Duyk, G.5    Hoffman, J.A.6    Ferrandon, D.7    Royet, J.8
  • 21
    • 0029112663 scopus 로고
    • Prophenol oxidase of the hawkmoth Manduca sexta. Purification, activation, substrate specificity of the active enzyme, and molecular cloning
    • Hall M., Scott T., Sugumaran M., Söderhäll K., and Law J. Prophenol oxidase of the hawkmoth Manduca sexta. Purification, activation, substrate specificity of the active enzyme, and molecular cloning. Proc. Natl. Acad. Sci. USA 92 (1995) 7764-7768
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7764-7768
    • Hall, M.1    Scott, T.2    Sugumaran, M.3    Söderhäll, K.4    Law, J.5
  • 22
    • 0003123713 scopus 로고    scopus 로고
    • Phenoloxidase activity in hemolymph of naïve and Beauveria bassiana-infected Spodoptera exigua larvae
    • Hung S.Y., and Boucias D.G. Phenoloxidase activity in hemolymph of naïve and Beauveria bassiana-infected Spodoptera exigua larvae. J. Invertebr. Pathol. 67 (1996) 35-40
    • (1996) J. Invertebr. Pathol. , vol.67 , pp. 35-40
    • Hung, S.Y.1    Boucias, D.G.2
  • 23
    • 0001310380 scopus 로고
    • Biosynthesis of prophenoloxidase in hemocytes of larval hemolymph of the silkworm, Bombyx mori
    • Iwama R., and Ashida M. Biosynthesis of prophenoloxidase in hemocytes of larval hemolymph of the silkworm, Bombyx mori. Insect Biochem 16 (1986) 547-555
    • (1986) Insect Biochem , vol.16 , pp. 547-555
    • Iwama, R.1    Ashida, M.2
  • 24
    • 2942569114 scopus 로고    scopus 로고
    • An entomopathogenic bacterium, Xenorhabdus nematophila, inhibits the expression of an antibacterial peptide, cecropin, of the beet armyworm, Spodoptera exigua
    • Ji D., and Kim Y. An entomopathogenic bacterium, Xenorhabdus nematophila, inhibits the expression of an antibacterial peptide, cecropin, of the beet armyworm, Spodoptera exigua. J. Insect Physiol. 50 (2004) 489-496
    • (2004) J. Insect Physiol. , vol.50 , pp. 489-496
    • Ji, D.1    Kim, Y.2
  • 25
    • 0033953792 scopus 로고    scopus 로고
    • The clip-domain family of serine proteinases in arthropods
    • Jiang H., and Kanost M.R. The clip-domain family of serine proteinases in arthropods. Insect Biochem. Mol. Biol. 30 (2000) 95-105
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 95-105
    • Jiang, H.1    Kanost, M.R.2
  • 26
    • 0031251981 scopus 로고    scopus 로고
    • Subunit composition of pro-phenol oxidase from Manduca sexta: molecular cloning of subunit proPO-P1
    • Jiang H., Wang Y., Ma C., and Kanost M.R. Subunit composition of pro-phenol oxidase from Manduca sexta: molecular cloning of subunit proPO-P1. Insect Biochem. Mol. Biol. 27 (1997) 835-850
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 835-850
    • Jiang, H.1    Wang, Y.2    Ma, C.3    Kanost, M.R.4
  • 27
    • 0032514618 scopus 로고    scopus 로고
    • Pro-phenol oxidase activating proteinase from an insect, Manduca sexta: a bacteria-inducible protein similar to Drosophila easter
    • Jiang H., Wang Y., and Kanost M.R. Pro-phenol oxidase activating proteinase from an insect, Manduca sexta: a bacteria-inducible protein similar to Drosophila easter. Proc. Natl. Acad. Sci. USA 95 (1998) 12220-12225
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12220-12225
    • Jiang, H.1    Wang, Y.2    Kanost, M.R.3
  • 28
    • 0037423271 scopus 로고    scopus 로고
    • Prophenoloxidase-activating proteinase-2 (PAP-2) from hemolymph of Manduca sexta: a bacteria-inducible serine proteinase containing two clip domains
    • Jiang H., Wang Y., Yu X.Q., and Kanost M.R. Prophenoloxidase-activating proteinase-2 (PAP-2) from hemolymph of Manduca sexta: a bacteria-inducible serine proteinase containing two clip domains. J. Biol. Chem. 278 (2003) 3552-3561
    • (2003) J. Biol. Chem. , vol.278 , pp. 3552-3561
    • Jiang, H.1    Wang, Y.2    Yu, X.Q.3    Kanost, M.R.4
  • 29
    • 0141924388 scopus 로고    scopus 로고
    • Prophenoloxidase-activating proteinase-3 (PAP-3) from Manduca sexta hemolymph: a clip-domain serine proteinase regulated by serpin-1J and serine proteinase homologs
    • Jiang H., Wang Y., Yu X.Q., Zhu Y., and Kanost M.R. Prophenoloxidase-activating proteinase-3 (PAP-3) from Manduca sexta hemolymph: a clip-domain serine proteinase regulated by serpin-1J and serine proteinase homologs. Insect Biochem. Mol. Biol. 33 (2003) 1049-1060
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 1049-1060
    • Jiang, H.1    Wang, Y.2    Yu, X.Q.3    Zhu, Y.4    Kanost, M.R.5
  • 31
    • 1642504737 scopus 로고    scopus 로고
    • Innate immune responses of a lepidopteran insects, Manduca sexta
    • Kanost M.R., Jiang H., and Yu X. Innate immune responses of a lepidopteran insects, Manduca sexta. Immunol. Rev. 198 (2004) 97-105
    • (2004) Immunol. Rev. , vol.198 , pp. 97-105
    • Kanost, M.R.1    Jiang, H.2    Yu, X.3
  • 32
    • 0029162812 scopus 로고
    • Molecular cloning of insect pro-phenol oxidase: a copper-containing protein homologous to arthropod hemocyanin
    • Kawabata T., Yasuhara Y., Ochiai M., Matsuura S., and Ashida M. Molecular cloning of insect pro-phenol oxidase: a copper-containing protein homologous to arthropod hemocyanin. Proc. Natl. Acad. Sci. USA 92 (1995) 7774-7778
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7774-7778
    • Kawabata, T.1    Yasuhara, Y.2    Ochiai, M.3    Matsuura, S.4    Ashida, M.5
  • 34
    • 0029556818 scopus 로고
    • The prophenoloxidase from the wax moth Galleria mellonella: purification and characterization of the proenzyme
    • Kopácek P., Weise C., and Götz P. The prophenoloxidase from the wax moth Galleria mellonella: purification and characterization of the proenzyme. Insect Biochem. Mol. Biol. 25 (1995) 1081-1091
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 1081-1091
    • Kopácek, P.1    Weise, C.2    Götz, P.3
  • 35
    • 0002728435 scopus 로고    scopus 로고
    • In vitro activation of pro-phenol-oxidase by two kinds of pro-phenol-oxidase-activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae
    • Lee S.Y., Kwon T.H., Hyun J.H., Choi J.S., Kawabata S., Iwanaga S., and Lee B.L. In vitro activation of pro-phenol-oxidase by two kinds of pro-phenol-oxidase-activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae. Eur. J. Biochem. 254 (1998) 50-57
    • (1998) Eur. J. Biochem. , vol.254 , pp. 50-57
    • Lee, S.Y.1    Kwon, T.H.2    Hyun, J.H.3    Choi, J.S.4    Kawabata, S.5    Iwanaga, S.6    Lee, B.L.7
  • 36
    • 14544306023 scopus 로고    scopus 로고
    • Reexamination of phenoloxidase in larval circulating hemocytes of the silk larva, Bombyx mori
    • Ling E., Shirai K., Kanehatsu R., and Kiguchi K. Reexamination of phenoloxidase in larval circulating hemocytes of the silk larva, Bombyx mori. Tissue Cell 37 (2005) 101-107
    • (2005) Tissue Cell , vol.37 , pp. 101-107
    • Ling, E.1    Shirai, K.2    Kanehatsu, R.3    Kiguchi, K.4
  • 37
    • 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
  • 38
    • 0036730522 scopus 로고    scopus 로고
    • Eicosanoids mediate Manduca sexta cellular response to the fungal pathogen Beauveria bassiana: a role for lipoxygenase pathway
    • Lord J.C., Anderson S., and Stanley D.W. Eicosanoids mediate Manduca sexta cellular response to the fungal pathogen Beauveria bassiana: a role for lipoxygenase pathway. Arch. Insect Biochem. Physiol. 51 (2002) 46-54
    • (2002) Arch. Insect Biochem. Physiol. , vol.51 , pp. 46-54
    • Lord, J.C.1    Anderson, S.2    Stanley, D.W.3
  • 39
    • 35448933979 scopus 로고    scopus 로고
    • Madanagopal, N., Kim, Y., 2007. A putative protein translation inhibitory factor encoded by Cotesia plutellae bracovirus suppresses host hemocyte-spreading behavior. J. Insect Physiol., in press.
  • 40
    • 0030871338 scopus 로고    scopus 로고
    • The effects of eicosanoid biosynthesis inhibitors on prophenoloxidase activation, phagocytosis and cell spreading in Galleria mellonella
    • Mandato G.A., Diehl-Jones L., Moore S.J., and Downer R.G. The effects of eicosanoid biosynthesis inhibitors on prophenoloxidase activation, phagocytosis and cell spreading in Galleria mellonella. J. Insect Physiol. 43 (1997) 1-8
    • (1997) J. Insect Physiol. , vol.43 , pp. 1-8
    • Mandato, G.A.1    Diehl-Jones, L.2    Moore, S.J.3    Downer, R.G.4
  • 41
    • 19644364615 scopus 로고    scopus 로고
    • Eicosanoids influence in vitro elongation of plasmatocytes from the tobacco hornworm, Manduca sexta
    • Miller J.S. Eicosanoids influence in vitro elongation of plasmatocytes from the tobacco hornworm, Manduca sexta. Arch. Insect Biochem. Physiol. 59 (2005) 42-51
    • (2005) Arch. Insect Biochem. Physiol. , vol.59 , pp. 42-51
    • Miller, J.S.1
  • 42
    • 0028604574 scopus 로고
    • Eicosanoids mediate insect nodulation responses to bacterial infections
    • Miller J.S., Nguyen T., and Stanley-Samuelson D.W. Eicosanoids mediate insect nodulation responses to bacterial infections. Proc. Natl. Acad. Sci. USA 91 (1994) 12418-12422
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12418-12422
    • Miller, J.S.1    Nguyen, T.2    Stanley-Samuelson, D.W.3
  • 43
    • 0001818292 scopus 로고    scopus 로고
    • Eicosanoids mediate nodulation responses to bacterial infections in larvae of the tenebrionid beetle, Zophobas atratus
    • Miller J.S., Howard R.W., Nyugen T., and Stanley-Samuelson D.W. Eicosanoids mediate nodulation responses to bacterial infections in larvae of the tenebrionid beetle, Zophobas atratus. J. Insect Physiol. 42 (1996) 3-12
    • (1996) J. Insect Physiol. , vol.42 , pp. 3-12
    • Miller, J.S.1    Howard, R.W.2    Nyugen, T.3    Stanley-Samuelson, D.W.4
  • 44
    • 0031449598 scopus 로고    scopus 로고
    • Eicosanoids mediate induction of immune genes in the fat body of the silkworm, Bombyx mori
    • Morishima I., Yamano Y., Inoue K., and Matsuo N. Eicosanoids mediate induction of immune genes in the fat body of the silkworm, Bombyx mori. FEBS Lett. 419 (1997) 83-86
    • (1997) FEBS Lett. , vol.419 , pp. 83-86
    • Morishima, I.1    Yamano, Y.2    Inoue, K.3    Matsuo, N.4
  • 45
    • 0033833552 scopus 로고    scopus 로고
    • Eicosanoids rescue Spodoptera exigua infected with Xenorhabdus nematophilus, the symbiotic bacteria to the entomopathogenic nematode, Steinernema carpocapsae
    • Park Y., and Kim Y. Eicosanoids rescue Spodoptera exigua infected with Xenorhabdus nematophilus, the symbiotic bacteria to the entomopathogenic nematode, Steinernema carpocapsae. J. Insect Physiol. 46 (2000) 1469-1476
    • (2000) J. Insect Physiol. , vol.46 , pp. 1469-1476
    • Park, Y.1    Kim, Y.2
  • 47
    • 30744432869 scopus 로고    scopus 로고
    • 2 associated with tobacco hornworm hemocyte membrane preparations acts in cellular immune reactions
    • 2 associated with tobacco hornworm hemocyte membrane preparations acts in cellular immune reactions. Arch. Insect Biochem. Physiol. 60 (2005) 105-115
    • (2005) Arch. Insect Biochem. Physiol. , vol.60 , pp. 105-115
    • Park, Y.1    Nor Aliza, A.R.2    Stanley, D.3
  • 48
    • 0028277880 scopus 로고
    • Separation and behavior in vitro of hemocytes from the moth, Pseudoplusia includens
    • Pech L.L., Trudeau D., and Strand M.R. Separation and behavior in vitro of hemocytes from the moth, Pseudoplusia includens. Cell Tissue Res. 277 (1994) 159-167
    • (1994) Cell Tissue Res. , vol.277 , pp. 159-167
    • Pech, L.L.1    Trudeau, D.2    Strand, M.R.3
  • 49
    • 0141790977 scopus 로고    scopus 로고
    • Prostaglandins, not lipoxygenase products, mediate insect microaggregation reactions to bacterial challenge in isolated hemocyte preparations
    • Phelps P.K., Miller J.S., and Stanley D.W. Prostaglandins, not lipoxygenase products, mediate insect microaggregation reactions to bacterial challenge in isolated hemocyte preparations. Comp. Biochem. Physiol. 136A (2003) 409-416
    • (2003) Comp. Biochem. Physiol. , vol.136 A , pp. 409-416
    • Phelps, P.K.1    Miller, J.S.2    Stanley, D.W.3
  • 51
    • 0037061482 scopus 로고    scopus 로고
    • Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli
    • Rämet M., Manfruelli P., Pearson A., Mathey-Preveot B., and Ezekowitz R.A.B. Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature 416 (2002) 644-648
    • (2002) Nature , vol.416 , pp. 644-648
    • Rämet, M.1    Manfruelli, P.2    Pearson, A.3    Mathey-Preveot, B.4    Ezekowitz, R.A.B.5
  • 52
    • 36749012872 scopus 로고    scopus 로고
    • SAS Institute Inc., 1989. SAS/STAT User's Guide, release 6.03 ed. SAS Institute, Cary, NC.
  • 53
    • 0033548626 scopus 로고    scopus 로고
    • Prophenoloxidase-activating enzyme of the silkworm, Bombyx mori: purification, characterization and cDNA cloning
    • Satoh D., Horii A., Ochiai M., and Ashida M. Prophenoloxidase-activating enzyme of the silkworm, Bombyx mori: purification, characterization and cDNA cloning. J. Biol. Chem. 274 (1999) 7441-7453
    • (1999) J. Biol. Chem. , vol.274 , pp. 7441-7453
    • Satoh, D.1    Horii, A.2    Ochiai, M.3    Ashida, M.4
  • 56
    • 36749037654 scopus 로고    scopus 로고
    • Factors affecting the activation of hemolymph prophenoloxidase of Spodoptera exigua (Lepidoptera: Noctuidae)
    • Shrestha S., and Kim Y. Factors affecting the activation of hemolymph prophenoloxidase of Spodoptera exigua (Lepidoptera: Noctuidae). J. Asia-Pac. Entomol. 10 (2007) 131-135
    • (2007) J. Asia-Pac. Entomol. , vol.10 , pp. 131-135
    • Shrestha, S.1    Kim, Y.2
  • 57
    • 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
  • 59
    • 84978426513 scopus 로고    scopus 로고
    • Eicosanoids
    • Gilbert L.I., Iatrou K., and Gill S. (Eds), Elsevier, Oxford, UK
    • Stanley D.W. Eicosanoids. In: Gilbert L.I., Iatrou K., and Gill S. (Eds). Comprehensive Molecular Insect Science vol. 4 (2005), Elsevier, Oxford, UK 307-339
    • (2005) Comprehensive Molecular Insect Science , vol.4 , pp. 307-339
    • Stanley, D.W.1
  • 60
    • 33645098178 scopus 로고    scopus 로고
    • Eicosanoid actions in insect cellular immune functions
    • Stanley D.W., and Miller J.S. Eicosanoid actions in insect cellular immune functions. Entomol. Exp. Appl. 119 (2006) 1-13
    • (2006) Entomol. Exp. Appl. , vol.119 , pp. 1-13
    • Stanley, D.W.1    Miller, J.S.2
  • 62
    • 0002723111 scopus 로고    scopus 로고
    • Roles of the insect cuticle in immunity
    • Söderhäll K., Iwanaga S., and Vasta G.R. (Eds), SOS Publications, Fair Haven, NJ
    • Sugumaran M. Roles of the insect cuticle in immunity. In: Söderhäll K., Iwanaga S., and Vasta G.R. (Eds). New Directions in Invertebrate Immunology (1996), SOS Publications, Fair Haven, NJ 355-374
    • (1996) New Directions in Invertebrate Immunology , pp. 355-374
    • Sugumaran, M.1
  • 63
    • 0032806588 scopus 로고    scopus 로고
    • Eicosanoids mediate nodulation reactions to bacterial infections in adults of two 17-year periodical cicadas, Magicicada spetendecim and M. cassini
    • Tunaz H., Bedick J.C., Miller J.S., Hoback W.W., Rana R.L., and Stanley D.W. Eicosanoids mediate nodulation reactions to bacterial infections in adults of two 17-year periodical cicadas, Magicicada spetendecim and M. cassini. J. Insect Physiol. 45 (1999) 923-931
    • (1999) J. Insect Physiol. , vol.45 , pp. 923-931
    • Tunaz, H.1    Bedick, J.C.2    Miller, J.S.3    Hoback, W.W.4    Rana, R.L.5    Stanley, D.W.6
  • 65
    • 35348897832 scopus 로고    scopus 로고
    • Uhm, J.H., Seo, Y.R., Yoe, S.M., Kang, S.W., Han, S.S., 2007. Analysis of the immune-inducible genes of Plutella xylostella using expressed sequence tags and cDNA microarray. Dev. Comp. Immunol., in press.
  • 67
    • 28844452777 scopus 로고    scopus 로고
    • The roles of two clip domain serine proteases in innate immune responses of the malaria vector Anopheles gambiae
    • Volz J., Osta M.A., Kafatos F.C., and Muller H. The roles of two clip domain serine proteases in innate immune responses of the malaria vector Anopheles gambiae. J. Biol. Chem. 280 (2005) 40161-40168
    • (2005) J. Biol. Chem. , vol.280 , pp. 40161-40168
    • Volz, J.1    Osta, M.A.2    Kafatos, F.C.3    Muller, H.4
  • 68
    • 0035059407 scopus 로고    scopus 로고
    • Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus
    • Wang R., Lee S.Y., Cerenius L., and Söderhäll K. Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus. Eur. J. Biochem. 268 (2001) 895-902
    • (2001) Eur. J. Biochem. , vol.268 , pp. 895-902
    • Wang, R.1    Lee, S.Y.2    Cerenius, L.3    Söderhäll, K.4
  • 69
    • 0037393120 scopus 로고    scopus 로고
    • 2-generated fatty acid cascade and lipopolysachharide-dependent activation of the immune deficiency (imd) pathway in insect immunity
    • 2-generated fatty acid cascade and lipopolysachharide-dependent activation of the immune deficiency (imd) pathway in insect immunity. Biochem. J. 371 (2003) 205-210
    • (2003) Biochem. J. , vol.371 , pp. 205-210
    • Yajima, M.1    Takada, M.2    Takahashi, N.3    Kikuchi, H.4    Natori, S.5    Oshima, Y.6    Kurata, S.7
  • 70
    • 2942617149 scopus 로고    scopus 로고
    • Immulectin-2 a pattern recognition receptor that stimulates hemocyte encapsulation and melanization in the tobacco hornworm Manduca sexta
    • Yu X.Q., and Kanost M.R. Immulectin-2 a pattern recognition receptor that stimulates hemocyte encapsulation and melanization in the tobacco hornworm Manduca sexta. Dev. Comp. Immunol. 28 (2004) 891-900
    • (2004) Dev. Comp. Immunol. , vol.28 , pp. 891-900
    • Yu, X.Q.1    Kanost, M.R.2
  • 71
    • 0037311545 scopus 로고    scopus 로고
    • Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm
    • Yu X.Q., Jiang H., Wang Y., and Kanost M.R. Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm. Insect Biochem. Mol. Biol. 33 (2003) 197-208
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 197-208
    • Yu, X.Q.1    Jiang, H.2    Wang, Y.3    Kanost, M.R.4


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