Evidence for proteins involved in prophenoloxidase cascade Eisenia fetida earthworms
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- bezobratlí MeSH
- hemokyanin MeSH
- katecholoxidasa imunologie metabolismus MeSH
- melaniny biosyntéza MeSH
- Oligochaeta imunologie MeSH
- prekurzory enzymů imunologie metabolismus MeSH
- proteiny imunologie MeSH
- signální transdukce imunologie MeSH
- tyrosinasa biosyntéza metabolismus MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- hemokyanin MeSH
- katecholoxidasa MeSH
- melaniny MeSH
- prekurzory enzymů MeSH
- pro-phenoloxidase MeSH Prohlížeč
- proteiny MeSH
- tyrosinasa 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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