Green tea catechins can bind and modify ERp57/PDIA3 activity

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11160%2F13%3A10210413" target="_blank" >RIV/00216208:11160/13:10210413 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/62690094:18470/13:50001868

Výsledek na webu

<a href="http://www.sciencedirect.com/science/article/pii/S0304416512003315" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0304416512003315</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbagen.2012.11.011" target="_blank" >10.1016/j.bbagen.2012.11.011</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Green tea catechins can bind and modify ERp57/PDIA3 activity

Popis výsledku v původním jazyce

Background: Green tea is a rich source of polyphenols, mainly catechins (flavanols), which significantly contribute to the beneficial health effects of green tea in the prevention and treatment of various diseases. In this study the effects of four greentea catechins on protein ERp57, also known as protein disulfide isomerase isoform A3 (PDIA3), have been investigated in an in vitro model. Methods: The interaction of catechins with ERp57 was explored by fluorescence quenching and surface plasmon resonance techniques and their effect on ERp57 activities was investigated. Results: A higher affinity was observed for galloylated cathechins, which bind close to the thioredoxin-like redox-sensitive active sites of the protein, with a preference for the oxidized form. The effects of these catechins on ERp57 properties were also investigated and a moderate inhibition of the reductase activity of ERp57 was observed as well as a strong inhibition of ERp57 DNA binding activity. Conclusions: Cons

Název v anglickém jazyce

Green tea catechins can bind and modify ERp57/PDIA3 activity

Popis výsledku anglicky

Background: Green tea is a rich source of polyphenols, mainly catechins (flavanols), which significantly contribute to the beneficial health effects of green tea in the prevention and treatment of various diseases. In this study the effects of four greentea catechins on protein ERp57, also known as protein disulfide isomerase isoform A3 (PDIA3), have been investigated in an in vitro model. Methods: The interaction of catechins with ERp57 was explored by fluorescence quenching and surface plasmon resonance techniques and their effect on ERp57 activities was investigated. Results: A higher affinity was observed for galloylated cathechins, which bind close to the thioredoxin-like redox-sensitive active sites of the protein, with a preference for the oxidized form. The effects of these catechins on ERp57 properties were also investigated and a moderate inhibition of the reductase activity of ERp57 was observed as well as a strong inhibition of ERp57 DNA binding activity. Conclusions: Cons

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

FR - Farmakologie a lékárnická chemie

OECD FORD obor

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Projekt

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Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Biochimica et Biophysica Acta - General Subjects

ISSN

0304-4165

e-ISSN

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Svazek periodika

1830

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

12

Strana od-do

2671-2682

Kód UT WoS článku

000315307900019

EID výsledku v databázi Scopus

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