Evidence for proteins involved in prophenoloxidase cascade Eisenia fetida earthworms
Language English Country Germany Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Invertebrates MeSH
- Hemocyanins MeSH
- Catechol Oxidase immunology metabolism MeSH
- Melanins biosynthesis MeSH
- Oligochaeta immunology MeSH
- Enzyme Precursors immunology metabolism MeSH
- Proteins immunology MeSH
- Signal Transduction immunology MeSH
- Monophenol Monooxygenase biosynthesis metabolism MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Hemocyanins MeSH
- Catechol Oxidase MeSH
- Melanins MeSH
- Enzyme Precursors MeSH
- pro-phenoloxidase MeSH Browser
- Proteins MeSH
- Monophenol Monooxygenase MeSH
The prophenoloxidase cascade represents one of the most important defense mechanisms in many invertebrates. Following the recognition of microbial saccharides by pattern recognition molecules, proteinases cleave inactive prophenoloxidase to its active form, phenoloxidase. Phenoloxidase is a key enzyme responsible for the catalysis of the melanization reaction. Final product melanin is involved in wound healing and immune responses. Prophenoloxidase cascade has been widely described in arthropods; data in other invertebrate groups are less frequent. Here we show detectable phenoloxidase activity in 90-kDa fraction of the coelomic fluid of earthworms Eisenia fetida. Amino acid sequencing of peptides from the active fraction revealed a partial homology with invertebrate phenoloxidases and hemocyanins. Moreover, the level of phenoloxidase activity is lower and the activation slower as compared to other invertebrates.
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Immunol Rev. 2004 Apr;198:116-26 PubMed
Biochemistry. 1998 Oct 6;37(40):14065-77 PubMed
Nature. 1970 Aug 15;227(5259):680-5 PubMed
J Invertebr Pathol. 2004 May-Jun;86(1-2):45-9 PubMed
Biochem Biophys Res Commun. 2004 Sep 17;322(2):490-6 PubMed
Biochem J. 2003 Apr 15;371(Pt 2):515-23 PubMed
Biochemistry. 1999 Feb 16;38(7):2179-88 PubMed
J Biol Chem. 2000 Sep 22;275(38):29264-7 PubMed
Immunol Lett. 2006 Apr 15;104(1-2):18-28 PubMed
J Exp Biol. 2000 Jun;203(Pt 12):1777-82 PubMed
J Biol Chem. 1998 Sep 18;273(38):24948-54 PubMed
Immunogenetics. 2005 Aug;57(7):535-48 PubMed
Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):939-43 PubMed
Immunogenetics. 2002 Mar;53(12):1055-64 PubMed
J Biol Chem. 1998 Oct 2;273(40):25889-92 PubMed
Insect Biochem Mol Biol. 2000 Oct;30(10):953-67 PubMed
J Biochem. 1993 Mar;113(3):285-91 PubMed
Biochim Biophys Acta. 1995 Feb 22;1247(1):1-11 PubMed
FEBS Lett. 1996 Apr 22;384(3):251-4 PubMed
J Biol Chem. 2001 May 25;276(21):17796-9 PubMed
Dev Comp Immunol. 1992 Mar-Jun;16(2-3):95-101 PubMed
Curr Opin Immunol. 1998 Feb;10(1):23-8 PubMed
Dev Comp Immunol. 1999 Jun-Jul;23(4-5):375-90 PubMed
Dev Comp Immunol. 2004 Jun;28(7-8):673-87 PubMed
Ann N Y Acad Sci. 1994 Apr 15;712:155-61 PubMed
Immunol Rev. 1998 Dec;166:15-26 PubMed
EMBO J. 2005 Jan 26;24(2):382-94 PubMed
Dev Comp Immunol. 1991 Fall;15(4):251-61 PubMed
Dev Cell. 2002 Oct;3(4):581-92 PubMed
J Biol Chem. 2001 Dec 7;276(49):45840-7 PubMed
Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6682-7 PubMed
Cell Tissue Res. 1992 Jul;269(1):167-74 PubMed
Proc Natl Acad Sci U S A. 1995 Mar 28;92(7):2964-8 PubMed
Dev Comp Immunol. 1981 Summer;5(3):415-25 PubMed
