Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60460709%3A41210%2F18%3A78061" target="_blank" >RIV/60460709:41210/18:78061 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14310/18:00101521 RIV/00216208:11310/18:10388886

Výsledek na webu

<a href="http://dx.doi.org/10.1051/parasite/2018062" target="_blank" >http://dx.doi.org/10.1051/parasite/2018062</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1051/parasite/2018062" target="_blank" >10.1051/parasite/2018062</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)

Popis výsledku v původním jazyce

Serpins are a superfamily of serine peptidase inhibitors that participate in the regulation of many physiological and cell peptidase mediated processes in all organisms. 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, or in the endogenous regulation of protein degradation. 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 excretory secretory products (ESPs) was confirmed. EnSerp1 influences the activity of peptidases that play a role in blood coagulation, fibrinolysis, and complement activation.

Název v anglickém jazyce

Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)

Popis výsledku anglicky

Serpins are a superfamily of serine peptidase inhibitors that participate in the regulation of many physiological and cell peptidase mediated processes in all organisms. 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, or in the endogenous regulation of protein degradation. 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 excretory secretory products (ESPs) was confirmed. EnSerp1 influences the activity of peptidases that play a role in blood coagulation, fibrinolysis, and complement activation.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30310 - Parasitology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2018

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Parasite - Journal de la Societe Francaise de Parasitologie

ISSN

1252-607X

e-ISSN

1252-607X

Svazek periodika

25

Číslo periodika v rámci svazku

61

Stát vydavatele periodika

FR - Francouzská republika

Počet stran výsledku

13

Strana od-do

1-13

Kód UT WoS článku

000452194000001

EID výsledku v databázi Scopus

2-s2.0-85058180856