Modulation of human cytochrome P450 1A1-mediated oxidation of benzo[a]pyrene by NADPH:cytochrome P450 oxidoreductase and cytochrome b5

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10288693" target="_blank" >RIV/00216208:11310/14:10288693 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11130/14:10288693 RIV/00064203:_____/14:10288693 RIV/62156489:43210/14:43908672 RIV/00216305:26620/14:PU126752

Výsledek na webu

<a href="http://www.nel.edu/archive_issues/o/35_s2/35_s2_Indra--Stiborova_105-113.pdf" target="_blank" >http://www.nel.edu/archive_issues/o/35_s2/35_s2_Indra--Stiborova_105-113.pdf</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Modulation of human cytochrome P450 1A1-mediated oxidation of benzo[a]pyrene by NADPH:cytochrome P450 oxidoreductase and cytochrome b5

Popis výsledku v původním jazyce

OBJECTIVES: Cytochrome P450 (CYP) 1A1 located in the membrane of endoplasmic reticulum is the most important enzyme in both activation and detoxification of carcinogenic benzo[a]pyrene (BaP), in combination with microsomal epoxide hydrolase (mEH). However, it is still not clearly explained how the electron transfer is mediated by NADPH:CYP oxidoreductase (POR), another component of the microsomal enzymatic system, on CYP1A1 during BaP oxidation, and whether microsomal cytochrome b5 might influence thiselectron transfer. METHODS: High performance liquid chromatography (HPLC) was employed for separation of BaP metabolites formed by enzymatic systems containing human CYP1A1. RESULTS: Human CYP1A1 expressed with POR in eukaryotic and prokaryotic expression cellular systems, in microsomes of insect cells (SupersomesTM) and in a membrane fraction of Escherichia coli, respectively, and these enzyme systems reconstituted with purified cytochrome b5 were utilized to study BaP oxidation. Human

Název v anglickém jazyce

Modulation of human cytochrome P450 1A1-mediated oxidation of benzo[a]pyrene by NADPH:cytochrome P450 oxidoreductase and cytochrome b5

Popis výsledku anglicky

OBJECTIVES: Cytochrome P450 (CYP) 1A1 located in the membrane of endoplasmic reticulum is the most important enzyme in both activation and detoxification of carcinogenic benzo[a]pyrene (BaP), in combination with microsomal epoxide hydrolase (mEH). However, it is still not clearly explained how the electron transfer is mediated by NADPH:CYP oxidoreductase (POR), another component of the microsomal enzymatic system, on CYP1A1 during BaP oxidation, and whether microsomal cytochrome b5 might influence thiselectron transfer. METHODS: High performance liquid chromatography (HPLC) was employed for separation of BaP metabolites formed by enzymatic systems containing human CYP1A1. RESULTS: Human CYP1A1 expressed with POR in eukaryotic and prokaryotic expression cellular systems, in microsomes of insect cells (SupersomesTM) and in a membrane fraction of Escherichia coli, respectively, and these enzyme systems reconstituted with purified cytochrome b5 were utilized to study BaP oxidation. Human

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

S - Specificky vyzkum na vysokych skolach<br>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

Neuroendocrinology Letters

ISSN

0172-780X

e-ISSN

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Svazek periodika

35

Číslo periodika v rámci svazku

Suppl. 2

Stát vydavatele periodika

SE - Švédské království

Počet stran výsledku

9

Strana od-do

105-113

Kód UT WoS článku

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EID výsledku v databázi Scopus

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