Eudiplozoon nipponicum (Monogenea): serpins – inhibitors of serine peptidases
| Název česky | Eudiplozoon nipponicum (Monogenea): serpiny - inhibitory serinových peptidáz |
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| Autoři | |
| Rok publikování | 2016 |
| Druh | Další prezentace na konferencích |
| Fakulta / Pracoviště MU | |
| Citace | |
| Popis | Eudiplozoon nipponicum is a platyhelminth, from the class Monogenea, family Diplozoidae. It is oviparous, hematophagous ectoparasite of common carp (Cyprinus carpio). Proteolytic enzymes (peptidases) are functional molecules, which catabolize cleavage of peptide bonds of proteins. According to the process of their action they are divided into several groups (e.g. cysteine, serine, aspartic, metallo- peptidases). Serine peptidases are known as a key factors of many physiological processes of higher organisms, such as complement cascade activation, blood clotting, fibrinolysis, inflammation and programmed apoptosis. Parasites employ the serine peptidases e.g. during invasion and migration of the host tissue and digestion. For each living organisms, the regulation of the activity of peptidases represents the crucial step and it can be mediated also by natural inhibitors, such as serpins – the inhibitors of serine peptidases. In transcriptomes/genomes of various helminth species, we can find high number of genes, coding serpins. In transcriptomic data, obtained on our experimental organism E. nipponicum we identified several sequences corresponding to serpins. Up to now no monogenean serpin has been characterized. The results of our preliminary experiments realized with recombinant serpin protein molecule indicates that function of the serpins could be similar to other blood feeding worms. This means, that eudiplozoon probably adopted similar mechanisms enabling to avoid inflammation, activation of complement and blood clotting. |
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