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Volumn 371, Issue 1, 2003, Pages 205-210

A newly established in vitro culture using transgenic Drosophila reveals functional coupling between the phospholipase A2-generated fatty acid cascade and lipopolysaccharide-dependent activation of the immune deficiency (imd) pathway in insect immunity

Author keywords

Host defence; Innate immunity; Nuclear factor B (NF B); Tumour necrosis factor (TNF)

Indexed keywords

ANTIGENS; FATTY ACIDS; IMMUNIZATION; MICROORGANISMS;

EID: 0037393120     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021603     Document Type: Article
Times cited : (90)

References (33)
  • 2
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway, C. A. (1989) Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harbor Symp. Quant. Biol. 54, 1-13
    • (1989) Cold Spring Harbor Symp. Quant. Biol. , vol.54 , pp. 1-13
    • Janeway, C.A.1
  • 3
    • 0036167107 scopus 로고    scopus 로고
    • Drosophila innate immunity: An evolutionary perspective
    • Hoffmann, J. A. and Reichhart, J. M. (2002) Drosophila innate immunity: an evolutionary perspective. Nat. Immunol. 3, 121-126
    • (2002) Nat. Immunol. , vol.3 , pp. 121-126
    • Hoffmann, J.A.1    Reichhart, J.M.2
  • 4
    • 0032994485 scopus 로고    scopus 로고
    • Induction and regulation of antimicrobial peptides in Drosophila
    • Engström, Y. (1999) Induction and regulation of antimicrobial peptides in Drosophila. Dev. Comp. Immunol. 23, 345-358
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 345-358
    • Engström, Y.1
  • 5
    • 0034913274 scopus 로고    scopus 로고
    • Drosophila immunity: Two paths to NF-κB
    • Khush, R. S., Leulier, F. and Lemaitre, B. (2001) Drosophila immunity: two paths to NF-κB. Trends Immunol 22, 260-264
    • (2001) Trends Immunol. , vol.22 , pp. 260-264
    • Khush, R.S.1    Leulier, F.2    Lemaitre, B.3
  • 6
    • 0035883151 scopus 로고    scopus 로고
    • NF-κB signaling pathways in mammalian and insect innate immunity
    • Silverman, N. and Maniatis, T. (2001) NF-κB signaling pathways in mammalian and insect innate immunity. Genes Dev. 15, 2321-2342
    • (2001) Genes Dev. , vol.15 , pp. 2321-2342
    • Silverman, N.1    Maniatis, T.2
  • 7
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre, B., Nicolas, E., Michaut, L., Reichhart, J.-M. and Hoffmann, J. A. (1996) The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 86, 973-983
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.-M.4    Hoffmann, J.A.5
  • 8
    • 0031446642 scopus 로고    scopus 로고
    • Drosophila host defense: Differential induction of antimicrobial peptide genes after infection by various classes of microorganisms
    • Lemaitre, B., Reichhart, J.-M. and Hoffmann, J. A. (1997) Drosophila host defense: differential induction of antimicrobial peptide genes after infection by various classes of microorganisms Proc. Natl. Acad. Sci. U.S.A. 94, 14614-14619
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 14614-14619
    • Lemaitre, B.1    Reichhart, J.-M.2    Hoffmann, J.A.3
  • 9
    • 0035856990 scopus 로고    scopus 로고
    • Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein
    • Michel, T., Reichhart, J.-M., Hoffmann, J. A. and Royet, J. (2001) Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein. Nature (London) 414, 756-759
    • (2001) Nature (London) , vol.414 , pp. 756-759
    • Michel, T.1    Reichhart, J.-M.2    Hoffmann, J.A.3    Royet, J.4
  • 12
    • 0037108754 scopus 로고    scopus 로고
    • Overexpression of a pattern recognition receptor, peptidoglycan recognition protein-LE, activates imd/relish medicated antibacterial defense and prophenoloxidase cascade in Drosophila larvae
    • Takehana, A., Katsuyama, T., Oshima, Y., Takada, H., Aigaki, T. and Kurata, S. (2002) Overexpression of a pattern recognition receptor, peptidoglycan recognition protein-LE, activates imd/relish medicated antibacterial defense and prophenoloxidase cascade in Drosophila larvae. Proc. Natl. Acad. Sci. U.S.A. 99, 13705-13710
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13705-13710
    • Takehana, A.1    Katsuyama, T.2    Oshima, Y.3    Takada, H.4    Aigaki, T.5    Kurata, S.6
  • 13
    • 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. (2002) Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila. Science 296, 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
  • 14
    • 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., Hoffmann, J. A., Ferrandon, D. and Royet, J. (2002) The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature (London) 416, 640-644
    • (2002) Nature (London) , vol.416 , pp. 640-644
    • Gottar, M.1    Gobert, V.2    Michel, T.3    Belvin, M.4    Duyk, G.5    Hoffmann, J.A.6    Ferrandon, D.7    Royet, J.8
  • 15
    • 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-Prevot, B. and Ezekowitz, R. A. B. (2002) Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature (London) 416, 644-648
    • (2002) Nature (London) , vol.416 , pp. 644-648
    • Rämet, M.1    Manfruelli, P.2    Pearson, A.3    Mathey-Prevot, B.4    Ezekowitz, R.A.B.5
  • 16
    • 0034913684 scopus 로고    scopus 로고
    • Vertebrate innate immunity resembles a mosaic of invertebrate immune responses
    • Salzet, M. (2001) Vertebrate innate immunity resembles a mosaic of invertebrate immune responses. Trends Immunol. 22, 285-288
    • (2001) Trends Immunol. , vol.22 , pp. 285-288
    • Salzet, M.1
  • 17
    • 0037066502 scopus 로고    scopus 로고
    • Decoding the patterns of self and nonself by the innate immune system
    • Medzhitov, R. and Janeway, C. A. (2002) Decoding the patterns of self and nonself by the innate immune system. Science 296, 298-300
    • (2002) Science , vol.296 , pp. 298-300
    • Medzhitov, R.1    Janeway, C.A.2
  • 20
    • 0033118490 scopus 로고    scopus 로고
    • Toll receptor-mediated Drosophila immune response requires Dif, an NF-κB factor
    • Meng, X., Khanuja, B. S. and Ip, Y. T. (1999) Toll receptor-mediated Drosophila immune response requires Dif, an NF-κB factor. Genes Dev. 13, 792-797
    • (1999) Genes Dev. , vol.13 , pp. 792-797
    • Meng, X.1    Khanuja, B.S.2    Ip, Y.T.3
  • 21
    • 0000351955 scopus 로고
    • Dissociation of Sarcophaga peregrina (flesh fly) fat body by pupal haemocytes in vitro
    • Kurata, S., Komano, H. and Natori, S. (1989) Dissociation of Sarcophaga peregrina (flesh fly) fat body by pupal haemocytes in vitro. J. Insect Physiol. 35, 559-565
    • (1989) J. Insect Physiol. , vol.35 , pp. 559-565
    • Kurata, S.1    Komano, H.2    Natori, S.3
  • 22
    • 0020713940 scopus 로고
    • Partial purification and properties of phospholipase A2 from rat liver mitochondria
    • Natori, Y., Karasawa, K., Araki, H., Tamori-Natori, Y. and Nojima, S. (1983) Partial purification and properties of phospholipase A2 from rat liver mitochondria. J. Biochem. (Tokyo) 93, 631-637
    • (1983) J. Biochem. (Tokyo) , vol.93 , pp. 631-637
    • Natori, Y.1    Karasawa, K.2    Araki, H.3    Tamori-Natori, Y.4    Nojima, S.5
  • 23
    • 0023177955 scopus 로고
    • Leukotrienes and lipoxins: Structures, biosynthesis, and biological effects
    • Samuelsson, B., Dahlen, S. E., Lindgren, J. A., Rouzer, C. A. and Serhan, C. N. (1987) Leukotrienes and lipoxins: structures, biosynthesis, and biological effects. Science 237, 1171-1176
    • (1987) Science , vol.237 , pp. 1171-1176
    • Samuelsson, B.1    Dahlen, S.E.2    Lindgren, J.A.3    Rouzer, C.A.4    Serhan, C.N.5
  • 25
  • 26
    • 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. (1997) Eicosanoids mediate induction of immune genes in the fat body of the silkworm, Bombyx mori. FEBS Lett. 419, 83-86
    • (1997) FEBS Lett. , vol.419 , pp. 83-86
    • Morishima, I.1    Yamano, Y.2    Inoue, K.3    Matsuo, N.4
  • 28
    • 0028604574 scopus 로고
    • Eicosanoids mediate insect nodulation responses to bacterial infections
    • Miller, J. S., Nguyen, T. and Stanley-Samuelson, D. W. (1994) Eicosanoids mediate insect nodulation responses to bacterial infections. Proc. Natl. Acad. Sci. U.S.A. 91, 12418-12422
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12418-12422
    • Miller, J.S.1    Nguyen, T.2    Stanley-Samuelson, D.W.3
  • 29
    • 0031391105 scopus 로고    scopus 로고
    • Eicosanoide mediate insect cellular immune reactions to bacterial infections
    • Stanley, D. W. (1997) Eicosanoide mediate insect cellular immune reactions to bacterial infections. Adv. Exp. Med. Biol. 433, 359-362
    • (1997) Adv. Exp. Med. Biol. , vol.433 , pp. 359-362
    • Stanley, D.W.1
  • 30
    • 0001108437 scopus 로고    scopus 로고
    • Prostaglandin production in response to a bacterial infection in true armyworm larvae
    • Jurenka, R. A., Pedibhotla, V. K. and Stanley, D. W. (1999) Prostaglandin production in response to a bacterial infection in true armyworm larvae. Arch. Insect Biochem. Physiol. 41, 225-232
    • (1999) Arch. Insect Biochem. Physiol. , vol.41 , pp. 225-232
    • Jurenka, R.A.1    Pedibhotla, V.K.2    Stanley, D.W.3
  • 31
    • 0026663222 scopus 로고
    • The 29-kDa hemocyte proteinase dissociates fat body at metamorphosis of Sarcophaga
    • Kurata, S., Saito, H. and Natori, S. (1992) The 29-kDa hemocyte proteinase dissociates fat body at metamorphosis of Sarcophaga. Dev. Biol. 153, 115-121
    • (1992) Dev. Biol. , vol.153 , pp. 115-121
    • Kurata, S.1    Saito, H.2    Natori, S.3
  • 32
    • 0032193215 scopus 로고    scopus 로고
    • Selective inhibitors of cytosolic or secretory phospholipase A2 block TNF-induced activation of transcription factor nuclear factor-κB and expression of ICAM-1
    • Thommesen, L., Sjursen, W., Gasvik, K., Hanssen, W., Brekke, O. L., Skattebol, L., Holmeide, A. K., Espevik, T., Johansen, B. and Laegreid, A. (1998) Selective inhibitors of cytosolic or secretory phospholipase A2 block TNF-induced activation of transcription factor nuclear factor-κB and expression of ICAM-1. J. Immunol. 161, 3421-3430
    • (1998) J. Immunol. , vol.161 , pp. 3421-3430
    • Thommesen, L.1    Sjursen, W.2    Gasvik, K.3    Hanssen, W.4    Brekke, O.L.5    Skattebol, L.6    Holmeide, A.K.7    Espevik, T.8    Johansen, B.9    Laegreid, A.10
  • 33
    • 0035839557 scopus 로고    scopus 로고
    • Functional coupling between secretory and cytosolic phospholipase A2 modulates tumor necrosis factor-α- and interleukin-1β-induced NF-κB activation
    • Anthonsen, M. W., Solhaug, A. and Johansen, B. (2001) Functional coupling between secretory and cytosolic phospholipase A2 modulates tumor necrosis factor-α- and interleukin-1β-induced NF-κB activation. J. Biol. Chem. 276, 30527-30536
    • (2001) J. Biol. Chem. , vol.276 , pp. 30527-30536
    • Anthonsen, M.W.1    Solhaug, A.2    Johansen, B.3


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