Effect of melanin on activities of cytochrome P450 1A1 and 1A2
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F25328859%3A_____%2F24%3AN0000041" target="_blank" >RIV/25328859:_____/24:N0000041 - isvavai.cz</a>
Výsledek na webu
—
DOI - Digital Object Identifier
—
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Effect of melanin on activities of cytochrome P450 1A1 and 1A2
Popis výsledku v původním jazyce
Lecture given at the First Joint Conference of Pharmacological Societies 2024, Ostrava 13 - 15 June 2024. The isolation and characterization of melanin from plant matrices using a modified version of the alkaline extraction method is described. Melanin was isolated from barley (Nudimelanocriton variety) and purified by a series of organic solvent treatments, acid hydrolysis and repeated precipitation. Approximately 5 mg of pure melanin was obtained from 12 g of barley grains. The isolated melanin showed its characteristic properties of insolubility in water, acids and organic solvents, while being soluble in alkaline media and precipitating below pH 3. The effect of melanin on cytochrome P450 1A1/2 enzyme activity in HepG2 cells was evaluated by 7-ethoxyresorufin O-dealkylation and high-performance liquid chromatography. Melanin at three concentrations (10 µg/ml, 1 µg/ml and 0.1 µg/ml) did not significantly induce cytochrome P450 1A1/2 enzyme activity (unlike the strong CYP1A1/2 inducer, 2,3,7,8-tetrachlorodibenzodioxin, which results in an almost sixty-fold increase). These findings contribute to the understanding of the physicochemical properties of melanin derived from barley and its interaction with liver enzymes of xenobiotic biotransformation (such as CYP1A1/2).
Název v anglickém jazyce
Effect of melanin on activities of cytochrome P450 1A1 and 1A2
Popis výsledku anglicky
Lecture given at the First Joint Conference of Pharmacological Societies 2024, Ostrava 13 - 15 June 2024. The isolation and characterization of melanin from plant matrices using a modified version of the alkaline extraction method is described. Melanin was isolated from barley (Nudimelanocriton variety) and purified by a series of organic solvent treatments, acid hydrolysis and repeated precipitation. Approximately 5 mg of pure melanin was obtained from 12 g of barley grains. The isolated melanin showed its characteristic properties of insolubility in water, acids and organic solvents, while being soluble in alkaline media and precipitating below pH 3. The effect of melanin on cytochrome P450 1A1/2 enzyme activity in HepG2 cells was evaluated by 7-ethoxyresorufin O-dealkylation and high-performance liquid chromatography. Melanin at three concentrations (10 µg/ml, 1 µg/ml and 0.1 µg/ml) did not significantly induce cytochrome P450 1A1/2 enzyme activity (unlike the strong CYP1A1/2 inducer, 2,3,7,8-tetrachlorodibenzodioxin, which results in an almost sixty-fold increase). These findings contribute to the understanding of the physicochemical properties of melanin derived from barley and its interaction with liver enzymes of xenobiotic biotransformation (such as CYP1A1/2).
Klasifikace
Druh
O - Ostatní výsledky
CEP obor
—
OECD FORD obor
40106 - Agronomy, plant breeding and plant protection; (Agricultural biotechnology to be 4.4)
Návaznosti výsledku
Projekt
<a href="/cs/project/QL24010230" target="_blank" >QL24010230: Barevná pšenice a ječmen – výzva pro budoucnost</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2024
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů