메뉴 건너뛰기




Volumn 34, Issue 1, 2001, Pages 15-20

Activated Phenoloxidase Interacts with a Novel Glycine-rich Protein on the Yeast Two-hybrid System

Author keywords

Defense reaction; Melanin; Phenoloxidase; Prophenoloxidase; Yeast two hybrid

Indexed keywords


EID: 0035581451     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (36)
  • 1
    • 0000926038 scopus 로고    scopus 로고
    • Recent advances in research on the insect pro-phenol oxidases
    • Brey, P E. and Hultmark, D., eds., Chapman & Hall, London
    • Ashida, M. and Brey, P (1998) Recent advances in research on the insect pro-phenol oxidases: in Molecular Mechanisms of Immune Responses in Insects (Brey, P E. and Hultmark, D., eds.), pp. 135-172, Chapman & Hall, London.
    • (1998) Molecular Mechanisms of Immune Responses in Insects , pp. 135-172
    • Ashida, M.1    Brey, P.2
  • 2
    • 0028853375 scopus 로고
    • cDNA cloning of prophenoloxidase from the freshwater crayfish Pacifastacus leniusculus and its activation
    • Aspan, A., Huang, T. S., Cerénius, L. and Söderhäll, K. (1995) cDNA cloning of prophenoloxidase from the freshwater crayfish Pacifastacus leniusculus and its activation. Proc. Natl. Acad. Sci. USA 92, 939-943.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 939-943
    • Aspan, A.1    Huang, T.S.2    Cerénius, L.3    Söderhäll, K.4
  • 3
    • 0025818448 scopus 로고
    • Antibacterial peptides: Key components needed in immunity
    • Boman, H. G. (1991) Antibacterial peptides: key components needed in immunity. Cell 65, 205-207.
    • (1991) Cell , vol.65 , pp. 205-207
    • Boman, H.G.1
  • 4
    • 0033564382 scopus 로고    scopus 로고
    • Molecular cloning and functional properties of two early-stage encapsulation-relating proteins from the coleopteran insect, Tenebrio molitor larvae
    • Cho, M. Y., Lee, H. S., Lee, K. M., Homma, K. I., Natori, S. and Lee, B. L. (1999a) Molecular cloning and functional properties of two early-stage encapsulation-relating proteins from the coleopteran insect, Tenebrio molitor larvae. Eur. J. Biochem. 262, 737-744.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 737-744
    • Cho, M.Y.1    Lee, H.S.2    Lee, K.M.3    Homma, K.I.4    Natori, S.5    Lee, B.L.6
  • 5
    • 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., Moon, G. Y., Kim, M. H., Kwon, T. H., Homma, K., Natori, S. and Lee, B. L. (1999b) 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, 303-307.
    • (1999) FEBS Lett. , vol.451 , pp. 303-307
    • Cho, M.Y.1    Choi, H.2    Moon, G.Y.3    Kim, M.H.4    Kwon, T.H.5    Homma, K.6    Natori, S.7    Lee, B.L.8
  • 6
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 7
    • 0030867913 scopus 로고    scopus 로고
    • Molecular immune responses of the mosquito Anopheles gambiae to bacteria and malaria parasites
    • Dimopoulos, G., Richman, A., Muller, H. M. and Kafatos, F. C. (1997) Molecular immune responses of the mosquito Anopheles gambiae to bacteria and malaria parasites. Proc. Natl. Acad. Sci. USA 94, 11508-11513.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11508-11513
    • Dimopoulos, G.1    Richman, A.2    Muller, H.M.3    Kafatos, F.C.4
  • 8
    • 0029112663 scopus 로고
    • Proenzyme of Manduca sexta phenol oxidase: Purification, activation, substrate specificity of the active enzyme, and molecular cloning
    • Hall, M., Scott, T., Sugumaran, M., Söderhäll, K. and Law, J. H. (1995) Proenzyme of Manduca sexta phenol oxidase: Purification, activation, substrate specificity of the active enzyme, and molecular cloning. Proc. Natl. Acad. Sci. USA 92, 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.H.5
  • 9
    • 0033514933 scopus 로고    scopus 로고
    • The crayfish plasma clotting protein: A vitellogenin-related protein responsible for clot formation in crustacean blood
    • Hall, M., Wang, R., van Antwerpen, R., Sottrup-Jensen, L. and Söderhäll, K. (1999) The crayfish plasma clotting protein: a vitellogenin-related protein responsible for clot formation in crustacean blood. Proc. Natl. Acad. Sci. USA 96, 1965-1970.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1965-1970
    • Hall, M.1    Wang, R.2    Van Antwerpen, R.3    Sottrup-Jensen, L.4    Söderhäll, K.5
  • 11
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • Iwanaga, S., Kawabata, S. and Muta, T. (1998) New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J. Biochem. (Tokyo) 123, 1-15.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 12
    • 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 Harb. Symp. Quant. Biol. 54, 1-13.
    • (1989) Cold Spring Harb. Symp. Quant. Biol. , vol.54 , pp. 1-13
    • Janeway, C.A.1
  • 13
    • 0003661078 scopus 로고
    • Biochemical and molecular characterization of an antifungal protein from Tenebrio molitor larvae
    • Jung, Y. H., Park, B. Y., Lee, D. K., Hahn, Y. S., Chung, J. H., Han, D. M., Moon, H. J., Lee, B. L. and Lee, Y. H. (1995) Biochemical and molecular characterization of an antifungal protein from Tenebrio molitor larvae. Mol Cells 5, 287-292.
    • (1995) Mol Cells , vol.5 , pp. 287-292
    • Jung, Y.H.1    Park, B.Y.2    Lee, D.K.3    Hahn, Y.S.4    Chung, J.H.5    Han, D.M.6    Moon, H.J.7    Lee, B.L.8    Lee, Y.H.9
  • 14
    • 0029162812 scopus 로고
    • Molecular cloning of insect prophenoloxidase: A copper containing protein homologous to arthropod hemocyanin
    • Kawabata, T., Yasuhara, Y., Ochiai, M., Matsuura, S. and Ashida, M. (1995) Molecular cloning of insect prophenoloxidase: A copper containing protein homologous to arthropod hemocyanin, Proc. Natl. Acad. Sci. USA 92, 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
  • 16
    • 0033771124 scopus 로고    scopus 로고
    • A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae
    • Kwon, T. H., Kim, M. S., Choi, H. W., Joo, C. H., Cho, M. Y. and Lee, B. L. (2000) A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae. Eur. J. Biochem. 267, 6188-6196.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6188-6196
    • Kwon, T.H.1    Kim, M.S.2    Choi, H.W.3    Joo, C.H.4    Cho, M.Y.5    Lee, B.L.6
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 49949137301 scopus 로고
    • The repair of wounds in the integument of insects
    • Lai-Fook, J. (1966) The repair of wounds in the integument of insects. J. Insect. Physiol. 12, 195-226.
    • (1966) J. Insect. Physiol. , vol.12 , pp. 195-226
    • Lai-Fook, J.1
  • 19
    • 0033036243 scopus 로고    scopus 로고
    • The pro-phenoloxidase of coleopteran insect, Tenebrio molitor, larvae was activated during cell clump/cell adhesion of insect cellular defense reactions
    • Lee, H. S., Cho, M. Y., Lee, K. M., Kwon, T. H., Homma, K., Natori, S. and Lee, B. L. (1999) The pro-phenoloxidase of coleopteran insect, Tenebrio molitor, larvae was activated during cell clump/cell adhesion of insect cellular defense reactions. FEBS Lett. 444, 255-259.
    • (1999) FEBS Lett. , vol.444 , pp. 255-259
    • Lee, H.S.1    Cho, M.Y.2    Lee, K.M.3    Kwon, T.H.4    Homma, K.5    Natori, S.6    Lee, B.L.7
  • 20
    • 0032528858 scopus 로고    scopus 로고
    • Identification and characterization of the antimicrobial peptide corresponding to C-terminal b-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor
    • Lee, H. Y., Hong, S. U., Oh, J. E., Kwon, M. Y., Yoon, J. H., Lee, J. H., Lee, B. L. and Moon, H. M. (1998a) Identification and characterization of the antimicrobial peptide corresponding to C-terminal b-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor. Biochem. J. 334, 99-105.
    • (1998) Biochem. J. , vol.334 , pp. 99-105
    • Lee, H.Y.1    Hong, S.U.2    Oh, J.E.3    Kwon, M.Y.4    Yoon, J.H.5    Lee, J.H.6    Lee, B.L.7    Moon, H.M.8
  • 21
    • 0033948890 scopus 로고    scopus 로고
    • Activated phenoloxidase from Tenebrio molitor larvae enhances the synthesis of melanin by using a vitellogenin-like protein in the presence of dopamine
    • Lee, K. M, Lee, K. Y, Choi, H. W., Cho, M. Y., Kwon, T. H., Kawabata, S. and Lee, B. L. (2000) Activated phenoloxidase from Tenebrio molitor larvae enhances the synthesis of melanin by using a vitellogenin-like protein in the presence of dopamine. Eur. J. Biochem. 267, 3695-3703.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3695-3703
    • Lee, K.M.1    Lee, K.Y.2    Choi, H.W.3    Cho, M.Y.4    Kwon, T.H.5    Kawabata, S.6    Lee, B.L.7
  • 22
    • 0027953371 scopus 로고
    • Purification and molecular cloning of cDNA for an inducible antibacterial protein of larvae of a coleopteran insect, Holotrichia diomphalia
    • Lee, S. Y., Moon, H. J., Kurata, S., Kurama, T., Natori, S. and Lee, B. L. (1994) Purification and molecular cloning of cDNA for an inducible antibacterial protein of larvae of a coleopteran insect, Holotrichia diomphalia. J. Biochem. (Tokyo), 115, 82-86.
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 82-86
    • Lee, S.Y.1    Moon, H.J.2    Kurata, S.3    Kurama, T.4    Natori, S.5    Lee, B.L.6
  • 23
    • 0029093121 scopus 로고
    • Purification and cDNA cloning of an antifungal protein from the hemolymph of Holotrichia diomphalia larvae
    • Lee, S. Y., Moon, H. J., Kurata, S., Natori, S. and Lee, B. L. (1995) Purification and cDNA cloning of an antifungal protein from the hemolymph of Holotrichia diomphalia larvae. Biol. Pharm. Bull. 18, 1049-1052.
    • (1995) Biol. Pharm. Bull. , vol.18 , pp. 1049-1052
    • Lee, S.Y.1    Moon, H.J.2    Kurata, S.3    Natori, S.4    Lee, B.L.5
  • 24
    • 0002728435 scopus 로고    scopus 로고
    • In vitro activation of pro-phenol-oxidase by two kinds of pro-phenoloxidase-activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae
    • Lee, S. Y., Kwon, T. H., Hyun, J. H., Choi, J. S., Kawabata, S. L, Iwanaga, S. and Lee, B. L. (1998b) In vitro activation of pro-phenol-oxidase by two kinds of pro-phenoloxidase-activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae. Eur. J. Biochem. 254, 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.L.5    Iwanaga, S.6    Lee, B.L.7
  • 25
    • 0000533788 scopus 로고    scopus 로고
    • Molecular cloning of cDNA for pro-phenol-oxidase-activating factor I, a serine protease is induced by lipopolysaccharide or 1,3-beta-glucan in coleopteran insect, Holotrichia diomphalia larvae
    • Lee, S. Y., Cho, M. Y., Hyun, J. H., Lee, K. M., Homma, K., Natori, S., Kawabata, S., Iwanaga, S. and Lee, B. L. (1998c) Molecular cloning of cDNA for pro-phenol-oxidase-activating factor I, a serine protease is induced by lipopolysaccharide or 1,3-beta-glucan in coleopteran insect, Holotrichia diomphalia larvae. Eur. J. Biochem. 257, 615-621.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 615-621
    • Lee, S.Y.1    Cho, M.Y.2    Hyun, J.H.3    Lee, K.M.4    Homma, K.5    Natori, S.6    Kawabata, S.7    Iwanaga, S.8    Lee, B.L.9
  • 26
    • 0343415656 scopus 로고    scopus 로고
    • A lipopolysaccharide and β-1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus
    • Lee, S. Y., Wang, R. and Söderhäll, K. (2000) A lipopolysaccharide and β-1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus. J. Biol. Chem. 275, 1337-1343.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1337-1343
    • Lee, S.Y.1    Wang, R.2    Söderhäll, K.3
  • 27
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtue of a non-clonal system of recognition
    • Medzhitov, R. and Janeway, C, A. (1997a) Innate immunity: the virtue of a non-clonal system of recognition. Cell 91, 295-298.
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway, C.A.2
  • 28
    • 0031050034 scopus 로고    scopus 로고
    • Innate immunity: Impact on the adaptive immune response
    • Medzhitov, R. and Janeway, C, A. (1997b) Innate immunity: impact on the adaptive immune response. Curr. Opin. Immunol. 9, 4-9.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 4-9
    • Medzhitov, R.1    Janeway, C.A.2
  • 29
    • 0028069819 scopus 로고
    • Purification and molecular cloning of cDNA for an inducible antibacterial protein from larvae of the coleopteran, Tenebrio molitor
    • Moon, H. J., Lee, S. Y., Kurata, S., Natori, S. and Lee, B. L. (1994) Purification and molecular cloning of cDNA for an inducible antibacterial protein from larvae of the coleopteran, Tenebrio molitor. J. Biochem. (Tokyo) 116, 53-58.
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 53-58
    • Moon, H.J.1    Lee, S.Y.2    Kurata, S.3    Natori, S.4    Lee, B.L.5
  • 30
    • 0028710016 scopus 로고
    • Function of antimicrobial proteins in insects
    • Natori, S. (1994) Function of antimicrobial proteins in insects. Ciba Found. Symp. 186, 123-132.
    • (1994) Ciba Found. Symp. , vol.186 , pp. 123-132
    • Natori, S.1
  • 31
    • 0024297132 scopus 로고    scopus 로고
    • Purification of a β-1,3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori
    • Ochiai, M. and Ashida, M. (1998) Purification of a β-1,3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori. J. Biol. Chem. 263, 12056-12062.
    • (1998) J. Biol. Chem. , vol.263 , pp. 12056-12062
    • Ochiai, M.1    Ashida, M.2
  • 32
    • 0029865876 scopus 로고    scopus 로고
    • Immunity to eukaryotic parasites in vector insects
    • Richman, A. and Kafatos, F. C. (1996) Immunity to eukaryotic parasites in vector insects. Curr. Opin. Immunol. 8, 14-19.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 14-19
    • Richman, A.1    Kafatos, F.C.2
  • 34
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase-activating system in invertebrate immunity
    • Söderhäll, K. and Cerenius, L. (1998) Role of the prophenoloxidase-activating system in invertebrate immunity. Curr. Opin. Immunol. 10, 23-28.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 23-28
    • Söderhäll, K.1    Cerenius, L.2
  • 35
    • 0026426696 scopus 로고
    • Molecular mechanisms for mammalian melanogenesis: Comparison with insect cuticular sclerotization
    • Sugumaran, M (1991) Molecular mechanisms for mammalian melanogenesis: Comparison with insect cuticular sclerotization. FEBS Lett. 295, 233-239.
    • (1991) FEBS Lett. , vol.295 , pp. 233-239
    • Sugumaran, M.1
  • 36
    • 0019061278 scopus 로고
    • Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose
    • Thomas, P. S. (1980) Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. USA 77, 5201-5205.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5201-5205
    • Thomas, P.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.