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

Result code in 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>

Alternative codes found

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

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

30310 - Parasitology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

S - Specificky vyzkum na vysokych skolach

Publication year

2018

Confidentiality

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

Name of the periodical

Parasite - Journal de la Societe Francaise de Parasitologie

ISSN

1252-607X

e-ISSN

1252-607X

Volume of the periodical

25

Issue of the periodical within the volume

61

Country of publishing house

FR - FRANCE

Number of pages

13

Pages from-to

1-13

UT code for WoS article

000452194000001

EID of the result in the Scopus database

2-s2.0-85058180856