Modulation of xenobiotic conjugation enzymes by dihydromyricetin in rats

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F17%3A73582245" target="_blank" >RIV/61989592:15110/17:73582245 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11160/17:10365288 RIV/00216208:11310/17:10365288

Výsledek na webu

<a href="https://link.springer.com/article/10.1007/s00706-017-2007-8" target="_blank" >https://link.springer.com/article/10.1007/s00706-017-2007-8</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00706-017-2007-8" target="_blank" >10.1007/s00706-017-2007-8</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Modulation of xenobiotic conjugation enzymes by dihydromyricetin in rats

Popis výsledku v původním jazyce

Dihydromyricetin, 3,3&apos;,4&apos;,5,5&apos;,7-hexahydroxyflavanone, is a phytochemical occurring in high quantities in tree Hovenia dulcis. This flavanonol is effective in counteracting acute EtOH intoxication and in reducing excessive EtOH consumption. As dihydromyricetin is considered for a potential human use its interactions with biotransformation enzymes should be examined. In general, ingested foreign compounds (xenobiotics) might stimulate expression (induction) of these enzymes and/or inhibit their activities. Usually the metabolism of xenobiotics proceeds via two phases of sequential enzymatic conversion to facilitate their excretion from the body. As xenobiotics biotransformation enzymes of the phase II, sulfo- and N/O-acetyltransferases (SULTs and NATs), are involved in the process of carcinogen activation, their induction/inhibition by dihydromyricetin should be examined. Dihydromyricetin was administered to experimental rats by gastric gavages in three consecutive doses (60 mg/kg body weight/day). The induction of sulfo- and N/O-acetyltransferases was assessed based on the protein levels on Western blots and on their metabolic activity in cytosolic samples of liver, small intestines and colon. Moreover, dihydromyricetin the inhibition of sulfo- and N/O-acetyltransferase mediated activities was examined with recombinant enzymes. Dihydromyricetin induced SULT1A1 activity in all tissues were studied with the exception of small intestines but had no effect on N/O-acetyltransferases. While dihydromyricetin did not affect SULT1A1 specific activity, both NAT1 and NAT2 were effectively inhibited (IC50 &lt; 10 mu mol dm(-3)).

Název v anglickém jazyce

Modulation of xenobiotic conjugation enzymes by dihydromyricetin in rats

Popis výsledku anglicky

Dihydromyricetin, 3,3&apos;,4&apos;,5,5&apos;,7-hexahydroxyflavanone, is a phytochemical occurring in high quantities in tree Hovenia dulcis. This flavanonol is effective in counteracting acute EtOH intoxication and in reducing excessive EtOH consumption. As dihydromyricetin is considered for a potential human use its interactions with biotransformation enzymes should be examined. In general, ingested foreign compounds (xenobiotics) might stimulate expression (induction) of these enzymes and/or inhibit their activities. Usually the metabolism of xenobiotics proceeds via two phases of sequential enzymatic conversion to facilitate their excretion from the body. As xenobiotics biotransformation enzymes of the phase II, sulfo- and N/O-acetyltransferases (SULTs and NATs), are involved in the process of carcinogen activation, their induction/inhibition by dihydromyricetin should be examined. Dihydromyricetin was administered to experimental rats by gastric gavages in three consecutive doses (60 mg/kg body weight/day). The induction of sulfo- and N/O-acetyltransferases was assessed based on the protein levels on Western blots and on their metabolic activity in cytosolic samples of liver, small intestines and colon. Moreover, dihydromyricetin the inhibition of sulfo- and N/O-acetyltransferase mediated activities was examined with recombinant enzymes. Dihydromyricetin induced SULT1A1 activity in all tissues were studied with the exception of small intestines but had no effect on N/O-acetyltransferases. While dihydromyricetin did not affect SULT1A1 specific activity, both NAT1 and NAT2 were effectively inhibited (IC50 &lt; 10 mu mol dm(-3)).

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GBP303%2F12%2FG163" target="_blank" >GBP303/12/G163: Centrum interakcí potravních doplňků s léčivy a nutrigenetiky</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Monatshefte für Chemie

ISSN

0026-9247

e-ISSN

—

Svazek periodika

148

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

AT - Rakouská republika

Počet stran výsledku

7

Strana od-do

2003-2009

Kód UT WoS článku

000413626000014

EID výsledku v databázi Scopus

2-s2.0-85022222907