The activity of drug-metabolizing enzymes and the biotransformation of selected anthelmintics in the model tapeworm Hymenolepis diminuta
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11160%2F12%3A10124822" target="_blank" >RIV/00216208:11160/12:10124822 - isvavai.cz</a>
Result on the web
<a href="http://journals.cambridge.org/action/displayAbstract?aid=8547427" target="_blank" >http://journals.cambridge.org/action/displayAbstract?aid=8547427</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1017/S0031182011002265" target="_blank" >10.1017/S0031182011002265</a>
Alternative languages
Result language
angličtina
Original language name
The activity of drug-metabolizing enzymes and the biotransformation of selected anthelmintics in the model tapeworm Hymenolepis diminuta
Original language description
The drug-metabolizing enzymes of some helminths can deactivate anthelmintics and therefore partially protect helminths against these drugs' toxic effect. The aim of our study was to assess the activity of the main drug-metabolizing enzymes and evaluate the metabolism of selected anthelmintics (albendazole, flubendazole, mebendazole) in the rat tapeworm Hymenolepis diminuta, a species often used as a model tapeworm. In vitro and ex vivo experiments were performed. Metabolites of the anthelmintics were detected and identified by HPLC with spectrofluorometric or mass-spectrometric detection. The enzymes of H. diminuta are able to reduce the carbonyl group of flubendazole, mebendazole and several other xenobiotics. Although the activity of a number of oxidation enzymes was determined, no oxidative metabolites of albendazole were detected. Regarding conjugation enzymes, a high activity of glutathione S-transferase was observed. A methyl derivative of reduced flubendazole was the only conjug
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GAP502%2F10%2F0217" target="_blank" >GAP502/10/0217: Drug-resistance development in helminths - possible mechanisms and defense</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Parasitology
ISSN
0031-1820
e-ISSN
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Volume of the periodical
139
Issue of the periodical within the volume
6
Country of publishing house
GB - UNITED KINGDOM
Number of pages
10
Pages from-to
809-818
UT code for WoS article
000304008100015
EID of the result in the Scopus database
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