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Volumn 30, Issue 12, 2006, Pages 1108-1118

Metamorphosis and collagen-IV-fragments stimulate innate immune response in the greater wax moth, Galleria mellonella

Author keywords

Antimicrobial peptides; Collagen fragments; Development; Galleria mellonella; Innate immunity; Metamorphosis

Indexed keywords

COLLAGEN TYPE 4; GALLERIMYCIN; INTERSTITIAL COLLAGENASE; LYSOZYME; MATRIX METALLOPROTEINASE; MESSENGER RNA; METALLOPROTEINASE INHIBITOR; PEPTIDE; TRANSCRIPTION FACTOR REL; UNCLASSIFIED DRUG;

EID: 33746294374     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2006.03.002     Document Type: Article
Times cited : (64)

References (41)
  • 1
    • 11844263877 scopus 로고    scopus 로고
    • Sensing and signaling during infection in Drosophila
    • Royet J., Reichhart J.M., and Hoffmann J.A. Sensing and signaling during infection in Drosophila. Curr Opin Immunol 17 (2005) 11-17
    • (2005) Curr Opin Immunol , vol.17 , pp. 11-17
    • Royet, J.1    Reichhart, J.M.2    Hoffmann, J.A.3
  • 2
    • 0037290892 scopus 로고    scopus 로고
    • Drosophila immunity: paths and pattern
    • Hultmark D. Drosophila immunity: paths and pattern. Curr Opin Immunol 15 (2003) 12-19
    • (2003) Curr Opin Immunol , vol.15 , pp. 12-19
    • Hultmark, D.1
  • 4
    • 0036167107 scopus 로고    scopus 로고
    • Drosophila innate immunity: an evolutionary perspective
    • Hoffman J.A., and Reichhart J.M. Drosophila innate immunity: an evolutionary perspective. Nat Immunol 3 (2002) 121-126
    • (2002) Nat Immunol , vol.3 , pp. 121-126
    • Hoffman, J.A.1    Reichhart, J.M.2
  • 5
    • 0242581687 scopus 로고    scopus 로고
    • The immune response of Drosophila
    • Hoffmann J.A. The immune response of Drosophila. Nature 426 (2003) 33-38
    • (2003) Nature , vol.426 , pp. 33-38
    • Hoffmann, J.A.1
  • 6
    • 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., et al. 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    Hoffmann, J.A.6
  • 7
    • 0032485392 scopus 로고    scopus 로고
    • Regulated nuclear import of Rel proteins in the Drosophila immune response
    • Wu L., and Anderson K. Regulated nuclear import of Rel proteins in the Drosophila immune response. Nature 392 (1998) 93-97
    • (1998) Nature , vol.392 , pp. 93-97
    • Wu, L.1    Anderson, K.2
  • 8
    • 1642504737 scopus 로고    scopus 로고
    • Innate immune response of a lepidopteran insect, Manduca sexta
    • Kanost M.R., Jiang H., and Yu X.Q. Innate immune response of a lepidopteran insect, Manduca sexta. Immunol Rev 198 (2001) 97-105
    • (2001) Immunol Rev , vol.198 , pp. 97-105
    • Kanost, M.R.1    Jiang, H.2    Yu, X.Q.3
  • 9
    • 0037363719 scopus 로고    scopus 로고
    • Identification of immunorelevant genes from greater wax moth (Galleria mellonella) by a subtractive hybridization approach
    • Seitz V., Clermont A., Wedde M., Hummel M., Vilcinskas A., Schlatterer K., et al. Identification of immunorelevant genes from greater wax moth (Galleria mellonella) by a subtractive hybridization approach. Dev Comp Immunol 27 (2003) 207-215
    • (2003) Dev Comp Immunol , vol.27 , pp. 207-215
    • Seitz, V.1    Clermont, A.2    Wedde, M.3    Hummel, M.4    Vilcinskas, A.5    Schlatterer, K.6
  • 10
    • 0032146755 scopus 로고    scopus 로고
    • Purification and characterization of an inducible metalloprotease inhibitor from the hemolymph of greater wax moth larvae, Galleria mellonella
    • Wedde M., Weise C., Kopacek P., Franke P., and Vilcinskas A. Purification and characterization of an inducible metalloprotease inhibitor from the hemolymph of greater wax moth larvae, Galleria mellonella. Eur J Biochem 255 (1998) 535-543
    • (1998) Eur J Biochem , vol.255 , pp. 535-543
    • Wedde, M.1    Weise, C.2    Kopacek, P.3    Franke, P.4    Vilcinskas, A.5
  • 11
    • 0034084470 scopus 로고    scopus 로고
    • Recognition and regulation of metalloproteinase activity in the haemolymph of Galleria mellonella: a new pathway mediating induction of humoral immune responses
    • Griesch J., Wedde M., and Vilcinskas A. Recognition and regulation of metalloproteinase activity in the haemolymph of Galleria mellonella: a new pathway mediating induction of humoral immune responses. Insect Biochem Mol Biol 30 (2000) 461-472
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 461-472
    • Griesch, J.1    Wedde, M.2    Vilcinskas, A.3
  • 12
    • 0036921508 scopus 로고    scopus 로고
    • Insect inhibitors of metalloproteinases
    • Vilcinskas A., and Wedde M. Insect inhibitors of metalloproteinases. IUBMB Life 54 (2002) 339-343
    • (2002) IUBMB Life , vol.54 , pp. 339-343
    • Vilcinskas, A.1    Wedde, M.2
  • 13
    • 12544256496 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H., and Woessner J.F. Matrix metalloproteinases. J Biol Chem 274 (1999) 2191-2194
    • (1999) J Biol Chem , vol.274 , pp. 2191-2194
    • Nagase, H.1    Woessner, J.F.2
  • 14
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases: effectors of development and normal physiology
    • Vu T., and Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev 14 (2000) 2123-2133
    • (2000) Genes Dev , vol.14 , pp. 2123-2133
    • Vu, T.1    Werb, Z.2
  • 15
    • 0037810391 scopus 로고    scopus 로고
    • Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases
    • Bode W., and Maskos K. Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases. Biol Chem 384 (2003) 863-872
    • (2003) Biol Chem , vol.384 , pp. 863-872
    • Bode, W.1    Maskos, K.2
  • 16
    • 0034680919 scopus 로고    scopus 로고
    • Dm1-MMP, a matrix metalloproteinase from Drosophila with a potential role in extracellular matrix remodeling during neural development
    • Llano E., Pendas A., Aza-blanc P., Kornberg T., and Lopez-Otin C. Dm1-MMP, a matrix metalloproteinase from Drosophila with a potential role in extracellular matrix remodeling during neural development. J Biol Chem 275 (2000) 35978-35985
    • (2000) J Biol Chem , vol.275 , pp. 35978-35985
    • Llano, E.1    Pendas, A.2    Aza-blanc, P.3    Kornberg, T.4    Lopez-Otin, C.5
  • 17
    • 0037189532 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of Drosophila Dm-MMP-2, a membrane-bound matrix metalloproteinase with tissue-specific expression
    • Llano E., Adam G., Pendas A., Quesada V., Sanchez L., Santamaria I., et al. Structural and enzymatic characterization of Drosophila Dm-MMP-2, a membrane-bound matrix metalloproteinase with tissue-specific expression. J Biol Chem 277 (2002) 23321-23329
    • (2002) J Biol Chem , vol.277 , pp. 23321-23329
    • Llano, E.1    Adam, G.2    Pendas, A.3    Quesada, V.4    Sanchez, L.5    Santamaria, I.6
  • 18
    • 0002139258 scopus 로고    scopus 로고
    • Antimycotic activity of lysozyme and its contribution to antifungal humoral defence reactions in Galleria mellonella
    • Vilcinskas A., and Matha V. Antimycotic activity of lysozyme and its contribution to antifungal humoral defence reactions in Galleria mellonella. Anim Biol 6 (1997) 19-29
    • (1997) Anim Biol , vol.6 , pp. 19-29
    • Vilcinskas, A.1    Matha, V.2
  • 19
    • 0042970579 scopus 로고    scopus 로고
    • Cloning and expression of gallerimycin, an antifungal peptide expressed in immune response of greater wax moth larvae, Galleria mellonella
    • Schuhmann B., Seitz V., Vilcinskas A., and Podsiadlowski L. Cloning and expression of gallerimycin, an antifungal peptide expressed in immune response of greater wax moth larvae, Galleria mellonella. Arch Insect Biochem Physiol 53 (2003) 125-133
    • (2003) Arch Insect Biochem Physiol , vol.53 , pp. 125-133
    • Schuhmann, B.1    Seitz, V.2    Vilcinskas, A.3    Podsiadlowski, L.4
  • 20
    • 4344590388 scopus 로고    scopus 로고
    • Cloning and expression of an inhibitor of microbial metalloproteinases from insects contributing to innate immunity
    • Clermont A., Wedde M., Seitz V., Podsiadlowski l., Lenze D., Hummel M., et al. Cloning and expression of an inhibitor of microbial metalloproteinases from insects contributing to innate immunity. Biochem J 382 (2004) 315-322
    • (2004) Biochem J , vol.382 , pp. 315-322
    • Clermont, A.1    Wedde, M.2    Seitz, V.3    Podsiadlowski, l.4    Lenze, D.5    Hummel, M.6
  • 22
    • 0001813139 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • Krawetz S., and Misener S. (Eds), Humana Press, Totowa, NJ
    • Rozen S., and Skaletsky H. Primer3 on the WWW for general users and for biologist programmers. In: Krawetz S., and Misener S. (Eds). Bioinformatics methods and protocols: methods in molecular biology (2000), Humana Press, Totowa, NJ
    • (2000) Bioinformatics methods and protocols: methods in molecular biology
    • Rozen, S.1    Skaletsky, H.2
  • 23
    • 0016231216 scopus 로고
    • Insect immunity I. Characteristics of an inducible cell-free antibacterial reaction in hemolymph of Samia cynthia
    • Boman H.G., Nilsson-Faye I., Paul K., and Rasmusen T.J. Insect immunity I. Characteristics of an inducible cell-free antibacterial reaction in hemolymph of Samia cynthia. Infect Immun 10 (1974) 136-145
    • (1974) Infect Immun , vol.10 , pp. 136-145
    • Boman, H.G.1    Nilsson-Faye, I.2    Paul, K.3    Rasmusen, T.J.4
  • 24
    • 0023473676 scopus 로고
    • Cell-free immunity in insects
    • Boman H.G., and Hultmark D. Cell-free immunity in insects. Ann Rev Microbiol 41 (1987) 103-126
    • (1987) Ann Rev Microbiol , vol.41 , pp. 103-126
    • Boman, H.G.1    Hultmark, D.2
  • 25
    • 0021331061 scopus 로고
    • Immunoenzymatic labeling of monoclonal antibodies using immune complexes of alkaline phosphatase and monoclonal anti-alkaline phosphatase (APAAP complexes)
    • Cordell J., Falini B., Erber W., Gosh A., Abdulazis Z., McDonald S., et al. Immunoenzymatic labeling of monoclonal antibodies using immune complexes of alkaline phosphatase and monoclonal anti-alkaline phosphatase (APAAP complexes). J Histochem Cytochem 32 (1984) 219-229
    • (1984) J Histochem Cytochem , vol.32 , pp. 219-229
    • Cordell, J.1    Falini, B.2    Erber, W.3    Gosh, A.4    Abdulazis, Z.5    McDonald, S.6
  • 27
    • 0032485392 scopus 로고    scopus 로고
    • Regulated nuclear import of Rel proteins in the Drosophila immune response
    • Wu A., and Anderson K. Regulated nuclear import of Rel proteins in the Drosophila immune response. Nature 392 (1998) 93-97
    • (1998) Nature , vol.392 , pp. 93-97
    • Wu, A.1    Anderson, K.2
  • 28
    • 0037239819 scopus 로고    scopus 로고
    • Drosophila matrix metalloproteinases are required for tissue remodelling, but not embryonic development
    • Page-McCaw A., Serano J., Sante J., and Rubin G.M. Drosophila matrix metalloproteinases are required for tissue remodelling, but not embryonic development. Dev Cell 4 (2003) 95-106
    • (2003) Dev Cell , vol.4 , pp. 95-106
    • Page-McCaw, A.1    Serano, J.2    Sante, J.3    Rubin, G.M.4
  • 29
    • 24344470024 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression in basal cell carcinoma: relationship between enzyme profile and collagen fragmentation pattern
    • Yucel T., Mutnal A., Fay K., Fligiel S., Wang T., Johnson T., et al. Matrix metalloproteinase expression in basal cell carcinoma: relationship between enzyme profile and collagen fragmentation pattern. Exp Mol Pathol 79 (2005) 151-160
    • (2005) Exp Mol Pathol , vol.79 , pp. 151-160
    • Yucel, T.1    Mutnal, A.2    Fay, K.3    Fligiel, S.4    Wang, T.5    Johnson, T.6
  • 30
    • 0036660865 scopus 로고    scopus 로고
    • Triple-helical peptide analysis of collagenolytic protease activity
    • Lauer-Fields J., and Fields G. Triple-helical peptide analysis of collagenolytic protease activity. Biol Chem 383 (2002) 1095-1105
    • (2002) Biol Chem , vol.383 , pp. 1095-1105
    • Lauer-Fields, J.1    Fields, G.2
  • 31
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • Myllyharju J., and Kivirikko K.I. Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet 20 (2004) 33-43
    • (2004) Trends Genet , vol.20 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 33
    • 18844372795 scopus 로고    scopus 로고
    • Synthesis of prolyl 4-hydroxylase α subunit and type IV collagen in hemocytic granular cells of silkworm, Bombyx mori: involvement of type IV collagen in self-defense reaction and metamorphosis
    • Adachi T., Tomita M., and Yoshizato K. Synthesis of prolyl 4-hydroxylase α subunit and type IV collagen in hemocytic granular cells of silkworm, Bombyx mori: involvement of type IV collagen in self-defense reaction and metamorphosis. Matrix Biol 24 (2005) 136-154
    • (2005) Matrix Biol , vol.24 , pp. 136-154
    • Adachi, T.1    Tomita, M.2    Yoshizato, K.3
  • 34
    • 8344277723 scopus 로고    scopus 로고
    • Hemolymph-dependent and-independent responses in Drosophila immune tissue
    • Bettencourd R., Asha H., Dearolf C., and Ip Y.T. Hemolymph-dependent and-independent responses in Drosophila immune tissue. J Cell Biochem 92 (2004) 849-863
    • (2004) J Cell Biochem , vol.92 , pp. 849-863
    • Bettencourd, R.1    Asha, H.2    Dearolf, C.3    Ip, Y.T.4
  • 35
    • 0035971217 scopus 로고    scopus 로고
    • The extra domain a of fibronectin activates Toll-like receptor 4
    • Okamura Y., Watari M., Jerud E., Young D., Ishizaka S., Rose J., et al. The extra domain a of fibronectin activates Toll-like receptor 4. J Biol Chem 276 (2001) 10229-10233
    • (2001) J Biol Chem , vol.276 , pp. 10229-10233
    • Okamura, Y.1    Watari, M.2    Jerud, E.3    Young, D.4    Ishizaka, S.5    Rose, J.6
  • 36
    • 0026671979 scopus 로고
    • Drosophila PS2 integrin mediates RGD-dependent cell-matrix interactions
    • Bunch T.A., and Brower D.L. Drosophila PS2 integrin mediates RGD-dependent cell-matrix interactions. Development 116 (1992) 239-247
    • (1992) Development , vol.116 , pp. 239-247
    • Bunch, T.A.1    Brower, D.L.2
  • 37
    • 24944516187 scopus 로고    scopus 로고
    • Drosophila sex-peptide stimulates female innate immune system after mating via the Toll and Imd pathways
    • Peng J., Zipperlen P., and Kubli E. Drosophila sex-peptide stimulates female innate immune system after mating via the Toll and Imd pathways. Curr Biol 15 (2005) 1690-1694
    • (2005) Curr Biol , vol.15 , pp. 1690-1694
    • Peng, J.1    Zipperlen, P.2    Kubli, E.3
  • 38
    • 0033525689 scopus 로고    scopus 로고
    • Cloning of the alpha subunit of prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties
    • Annunen P., Koivunen P., and Kivirikko K.I. Cloning of the alpha subunit of prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties. J Biol Chem 274 (1999) 6790-6796
    • (1999) J Biol Chem , vol.274 , pp. 6790-6796
    • Annunen, P.1    Koivunen, P.2    Kivirikko, K.I.3
  • 39
    • 0018846755 scopus 로고
    • Locust collagen: morphological and biochemical characterisation
    • Ashhurst D.E., and Bailey A. Locust collagen: morphological and biochemical characterisation. Eur J Biochem 103 (1980) 75-83
    • (1980) Eur J Biochem , vol.103 , pp. 75-83
    • Ashhurst, D.E.1    Bailey, A.2
  • 40
    • 33746223511 scopus 로고    scopus 로고
    • The genomic response to 20-hydroxyecdysone at the onset of Drosophila metamorphosis
    • Beckstead R., Lam G., and Thummel C. The genomic response to 20-hydroxyecdysone at the onset of Drosophila metamorphosis. Genome Biol 6 (2005) R99
    • (2005) Genome Biol , vol.6
    • Beckstead, R.1    Lam, G.2    Thummel, C.3
  • 41
    • 29744438644 scopus 로고    scopus 로고
    • A spätzle-processing enzyme required for Toll signaling activation in Drosophila innate immunity
    • Jang I.H., Chosa N., Kim S.H., Nam H.J., Lemaitre B., Ochiai M., et al. A spätzle-processing enzyme required for Toll signaling activation in Drosophila innate immunity. Dev Cell 10 (2006) 45-55
    • (2006) Dev Cell , vol.10 , pp. 45-55
    • Jang, I.H.1    Chosa, N.2    Kim, S.H.3    Nam, H.J.4    Lemaitre, B.5    Ochiai, M.6


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