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Nam, H.J., Jang, I.H., Asano, T., Lee, W.J. (2008). Involvement of pro-phenoloxidase 3 in lamellocyte-mediated spontaneous melanization in Drosophila.  Mol. Cells 26(6): 606--610.
FlyBase ID
FBrf0207487
Publication Type
Research paper
Abstract

Phenoloxidase (PO), a melanin-forming enzyme around the foreign bodies, is an important component of the host defense system in invertebrates. Pro-PO is the enzymatically inactive zymogen form of PO. In the Drosophila genome, three Pro-PO isoforms have been identified to date. These include Pro-PO1 and 2, which are primarily expressed in crystal cells, and Pro-PO3, which is predominantly found in the lamellocytes. In this study, we demonstrated that Drosophila Pro-PO3, but not Pro-PO1 or 2, is enzymatically active in its zymogen form. These findings were evidenced by spectacular melanin forming capacities of various cells and tissues that overexpressed these proenzymes. Furthermore, the melanization phenotype observed in the lamellocyte-enriched hop(Tum-1) mutant was drastically reduced in the absence of PPO3, indicating that PPO3 plays a major role in the lamellocyte-mediated spontaneous melanization process. Taken together, these findings indicate that the biochemical properties, activation mode and in vivo role of Pro-PO3 are likely distinct from those of the other two Pro-PO enzymes involved in Drosophila physiology.

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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Mol. Cells
    Title
    Molecules and Cells
    ISBN/ISSN
    1016-8478
    Data From Reference
    Alleles (14)
    Genes (6)
    Cell Lines (1)
    Natural transposons (1)
    Insertions (3)
    Experimental Tools (4)
    Transgenic Constructs (9)