Role of rat cytochromes P450 in the oxidation of 17?-ethinylestradiol

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10283266" target="_blank" >RIV/00216208:11310/14:10283266 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.etap.2014.10.004" target="_blank" >http://dx.doi.org/10.1016/j.etap.2014.10.004</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.etap.2014.10.004" target="_blank" >10.1016/j.etap.2014.10.004</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Role of rat cytochromes P450 in the oxidation of 17?-ethinylestradiol

Popis výsledku v původním jazyce

17?-Ethinylestradiol (EE2) is an endocrine disruptor (ED) used as an ingredient of oral contraceptives. Rat hepatic microsomes metabolize EE2 to three products; two of them are hydroxylated EE2 derivatives. Of the hydroxylation reactions, 2-hydroxylation, is the major reaction. Cytochrome P450 (CYP) plays a major role in EE2 hydroxylation. To resolve which rat CYPs are responsible for EE2 oxidation, three approaches were used: induction of specific CYPs, selective inhibition of CYPs, and recombinant ratCYPs. The results demonstrate that EE2 is hydroxylated by several rat CYPs, among them CYP2C6 and 2C11 are most efficient in 2-hydroxy-EE2 formation, while CYP2A and 3A catalyze EE2 hydroxylation to the second product. EE2 is also an inhibitor of CYP2C-and CYP3A-catalyzed hydroxylation of endogenous EDs progesterone and testosterone. EE2 acts as a reversible inhibitor of CYP3A-mediated progesterone 6?-hydroxylation and inactivates CYP3A- and CYP2C-catalyzed testosterone 6?-hydroxylatio

Název v anglickém jazyce

Role of rat cytochromes P450 in the oxidation of 17?-ethinylestradiol

Popis výsledku anglicky

17?-Ethinylestradiol (EE2) is an endocrine disruptor (ED) used as an ingredient of oral contraceptives. Rat hepatic microsomes metabolize EE2 to three products; two of them are hydroxylated EE2 derivatives. Of the hydroxylation reactions, 2-hydroxylation, is the major reaction. Cytochrome P450 (CYP) plays a major role in EE2 hydroxylation. To resolve which rat CYPs are responsible for EE2 oxidation, three approaches were used: induction of specific CYPs, selective inhibition of CYPs, and recombinant ratCYPs. The results demonstrate that EE2 is hydroxylated by several rat CYPs, among them CYP2C6 and 2C11 are most efficient in 2-hydroxy-EE2 formation, while CYP2A and 3A catalyze EE2 hydroxylation to the second product. EE2 is also an inhibitor of CYP2C-and CYP3A-catalyzed hydroxylation of endogenous EDs progesterone and testosterone. EE2 acts as a reversible inhibitor of CYP3A-mediated progesterone 6?-hydroxylation and inactivates CYP3A- and CYP2C-catalyzed testosterone 6?-hydroxylatio

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA14-18344S" target="_blank" >GA14-18344S: Vývoj nanočástic obsahujících cytostatika a enzymy pro zlepšení chemotherapie lidských neuroblastomů a studium mechanismu jejich působení</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Environmental Toxicology and Pharmacology

ISSN

1382-6689

e-ISSN

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Svazek periodika

38

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

852-860

Kód UT WoS článku

000347512400018

EID výsledku v databázi Scopus

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