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Activated Prophenoloxidase Engaged in the Cell Clump/Cell Adhesion of Coleopteran Insect, Tenebrio Molitor Larvae

  • Hyun Seong Lee
  • Mi Young Cho
  • Bok Luel Lee
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 484)

Abstract

The endogenous defense system is classified into two broad categories, cellular and humoral immune responses. The latter include the synthesis of potent antimicrobial proteins and the activation of the pro-phenoloxidase (pro-PO) cascade (1–5). Previously, we examined the humoral responses of larvae of the coleopteran insects, Tenebrio molitor and Holotrichia diomphalia (1–3) and reported the primary structures of antimicrobial proteins in their hemolymph and pro-PO activating factor (PPAF-I).

Keywords

Copper Binding Site Encapsulation Response Coleopteran Insect Amino Terminal Sequence Adhesion Reaction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Kwon, T. H., Lee, S. Y., Lee, J. H., Choi, J. S., Kawabata, S., Iwanaga S. Lee, B. L. Purification and characterization of pro-phenoloxidase from the hemolymph of coleopteran insect, Holotrichia diomphalia larvae. Mol. Cells 7, 90–97 (1997)PubMedGoogle Scholar
  2. 2.
    Lee, S. Y., Kwon, T. H., Hyun, J. H., Choi, J. S., Kawabata, S., Iwanaga, S., Lee, B. L., In vitro activation of pro-phenoloxidase by two kinds of pro-phenoloxidase activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae. Eur. J. Biochem. 254, 50–57 (1998)CrossRefGoogle Scholar
  3. 3.
    Lee, S. Y., Cho, M. Y., Hyun, J. H., Lee K. M., Homma, K., Natori, S., Kwabata, S., Iwanaga, S., Lee, B. L. Molecular cloning of cDNA for pro-phenoloxidase activating factor I-, a serine protease that induced by lipopolysaccharide or 1,3-beta-glucan in coleopteran insect, Holotrichia diomphalia larvae. Eur, J. Biochem. 257, 615–621 (1998)Google Scholar
  4. 4.
    Aspan, A. and Sderhll, K. Purification of pro-phenol-oxidase from crayfish blood cells and its activation by an endogenous serine protease. Insect. Biochem. 21, 363–373 (1991)CrossRefGoogle Scholar
  5. 5.
    Fujimoto, K., Okino, N., Kawabata, S., Iwanaga, S. and Ohnish, E. Nucleotide sequence of the cDNa encoding pro-phenoloxidase Al of Drosophila melanogaster. Poc. Natl Acad. Sci. USA 92, 7769–7773 (1995)CrossRefGoogle Scholar
  6. 6.
    Cho, M. Y., Lee, H. S., Lee, K. M., Homma, K., Natori, S. and Lee, B. L. Molecular cloning and functional properties of two early-staged encapsulation-relating proteins from the coleopteran insect, Tenebrio molitor larvae. Eur. J. Biochem. 262, 737–744 (1999)CrossRefGoogle Scholar
  7. 7.
    Cho, M. Y., Choi H. W., Moon G.Y., Kim, M. H., Kwon, T. H., Homma, K., Natori, S. and Lee, B. L. An 86kDa diapause protein 1-like protein is a component of early-staged encapsulation relating proteins in coleopteran insect, Tenebrio molitor larvae. FEBS Letters 451, 303–307 (1999)CrossRefGoogle Scholar
  8. 8.
    Tagahashi, H., Azumi, K. and Yokosawa, H. Hemocyte aggregation in the solitary ascidian Halocynthia reretzi: plasma factors, magnesium ion, and Met-Lys-bradykinin induce the aggregation. Biol. Bull. 186, 247–253 (1994)CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Hyun Seong Lee
    • 1
  • Mi Young Cho
    • 1
  • Bok Luel Lee
    • 1
  1. 1.Pusan National UniversityCollege of Pharmacy Jangjeong-DongKorea

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