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Identification et caractérisation partielle d'un nouvelle serpine d'Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea) [Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)]
P. Roudnický, J. Vorel, J. Ilgová, M. Benovics, A. Norek, L. Jedličková, L. Mikeš, D. Potěšil, Z. Zdráhal, J. Dvořák, M. Gelnar, M. Kašný,
Jazyk angličtina Země Francie
Typ dokumentu časopisecké články
NLK
Directory of Open Access Journals
od 2013
Free Medical Journals
od 2005
PubMed Central
od 2011
Europe PubMed Central
od 2011
ProQuest Central
od 2012-02-01
Open Access Digital Library
od 2011-01-01
Open Access Digital Library
od 2013-01-01
Medline Complete (EBSCOhost)
od 2013-01-01
Health & Medicine (ProQuest)
od 2012-02-01
ROAD: Directory of Open Access Scholarly Resources
od 2007
PubMed
30516130
DOI
10.1051/parasite/2018062
Knihovny.cz E-zdroje
- MeSH
- DNA helmintů chemie MeSH
- fylogeneze MeSH
- infekce červy třídy Trematoda parazitologie veterinární MeSH
- inhibitory serinových proteinas chemie genetika izolace a purifikace metabolismus MeSH
- kapři parazitologie MeSH
- nemoci ryb parazitologie MeSH
- počítačová simulace MeSH
- polymerázová řetězová reakce MeSH
- rekombinantní proteiny genetika izolace a purifikace metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvence nukleotidů MeSH
- sekvenční seřazení MeSH
- serpiny chemie genetika izolace a purifikace metabolismus MeSH
- Trematoda chemie klasifikace enzymologie genetika MeSH
- žábry parazitologie MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
BACKGROUND: Serpins are a superfamily of serine peptidase inhibitors that participate in the regulation of many physiological and cell peptidase-mediated processes in all organisms (e.g. in blood clotting, complement activation, fibrinolysis, inflammation, and programmed cell death). It was postulated that in the blood-feeding members of the monogenean family Diplozoidae, serpins could play an important role in the prevention of thrombus formation, activation of complement, inflammation in the host, and/or in the endogenous regulation of protein degradation. RESULTS: In silico analysis showed that the DNA and primary protein structures of serpin from Eudiplozoon nipponicum (EnSerp1) are similar to other members of the serpin superfamily. The inhibitory potential of EnSerp1 on four physiologically-relevant serine peptidases (trypsin, factor Xa, kallikrein, and plasmin) was demonstrated and its presence in the worm's excretory-secretory products (ESPs) was confirmed. CONCLUSION: EnSerp1 influences the activity of peptidases that play a role in blood coagulation, fibrinolysis, and complement activation. This inhibitory potential, together with the serpin's presence in ESPs, suggests that it is likely involved in host-parasite interactions and could be one of the molecules involved in the control of feeding and prevention of inflammatory responses.
Central European Institute of Technology Masaryk University Kamenice 753 5 62500 Brno Czech Republic
Veterinary Research Institute Hudcova 296 70 62100 Brno Czech Republic
Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)
Citace poskytuje Crossref.org
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- $a BACKGROUND: Serpins are a superfamily of serine peptidase inhibitors that participate in the regulation of many physiological and cell peptidase-mediated processes in all organisms (e.g. in blood clotting, complement activation, fibrinolysis, inflammation, and programmed cell death). It was postulated that in the blood-feeding members of the monogenean family Diplozoidae, serpins could play an important role in the prevention of thrombus formation, activation of complement, inflammation in the host, and/or in the endogenous regulation of protein degradation. RESULTS: In silico analysis showed that the DNA and primary protein structures of serpin from Eudiplozoon nipponicum (EnSerp1) are similar to other members of the serpin superfamily. The inhibitory potential of EnSerp1 on four physiologically-relevant serine peptidases (trypsin, factor Xa, kallikrein, and plasmin) was demonstrated and its presence in the worm's excretory-secretory products (ESPs) was confirmed. CONCLUSION: EnSerp1 influences the activity of peptidases that play a role in blood coagulation, fibrinolysis, and complement activation. This inhibitory potential, together with the serpin's presence in ESPs, suggests that it is likely involved in host-parasite interactions and could be one of the molecules involved in the control of feeding and prevention of inflammatory responses.
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- $a Vorel, Jiří $u Department of Botany and Zoology, Faculty of Science, Masaryk University, Kamenice 753/5, 62500 Brno, Czech Republic.
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- $a Dvořák, Jan $u School of Biological Sciences, Medical Biology Centre, Queen's University Belfast, 97 Lisburn Road, Belfast BT9 7BL, United Kingdom - Department of Zoology and Fisheries, Faculty of Agrobiology, Food and Natural Resources, Czech University of Life Sciences in Prague, Kamýcká 129, 16521 Prague, Czech Republic.
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