Modulation of xenobiotic conjugation enzymes by dihydromyricetin in rats

Result code in 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>

Alternative codes found

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

Result on the web

<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>

Result language

angličtina

Original language name

Modulation of xenobiotic conjugation enzymes by dihydromyricetin in rats

Original language description

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)).

Czech name

—

Czech description

—

Type

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

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

<a href="/en/project/GBP303%2F12%2FG163" target="_blank" >GBP303/12/G163: Centre of drug-dietary supplements interactions and nutrigenetics</a><br>

Continuities

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

Publication year

2017

Confidentiality

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

Name of the periodical

Monatshefte für Chemie

ISSN

0026-9247

e-ISSN

—

Volume of the periodical

148

Issue of the periodical within the volume

11

Country of publishing house

AT - AUSTRIA

Number of pages

7

Pages from-to

2003-2009

UT code for WoS article

000413626000014

EID of the result in the Scopus database

2-s2.0-85022222907