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The Modulation of Phase II Drug-Metabolizing Enzymes in Proliferating and Differentiated CaCo-2 Cells by Hop-Derived Prenylflavonoids
K. Lněničková, M. Šadibolová, P. Matoušková, B. Szotáková, L. Skálová, I. Boušová
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články
Grantová podpora
Research Project SVV 260 550
Univerzita Karlova v Praze
CZ.02.1.01/0.0/0.0/16_019/0000841
Ministerstvo Školství, Mládeže a Tělovýchovy
Free Medical Journals od 2009
PubMed Central od 2009
Europe PubMed Central od 2009
ProQuest Central od 2009-01-01
Open Access Digital Library od 2009-01-01
Open Access Digital Library od 2009-01-01
Health & Medicine (ProQuest) od 2009-01-01
ROAD: Directory of Open Access Scholarly Resources od 2009
Odkazy
PubMed
32708388
DOI
10.3390/nu12072138
Knihovny.cz E-zdroje
- MeSH
- buněčná diferenciace účinky léků genetika MeSH
- Caco-2 buňky MeSH
- exprese genu účinky léků MeSH
- flavonoidy izolace a purifikace farmakologie MeSH
- glukuronosyltransferasa genetika metabolismus MeSH
- glutathiontransferasa genetika metabolismus MeSH
- Humulus chemie MeSH
- katechol-O-methyltransferasa genetika metabolismus MeSH
- lidé MeSH
- neopren izolace a purifikace farmakologie MeSH
- proliferace buněk účinky léků genetika MeSH
- propiofenony izolace a purifikace farmakologie MeSH
- sulfotransferasy genetika metabolismus MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
Prenylflavonoids in the human organism exhibit various health-beneficial activities, although they may interfere with drugs via the modulation of the expression and/or activity of drug-metabolizing enzymes. As intestinal cells are exposed to the highest concentrations of prenylflavonoids, we decided to study the cytotoxicity and modulatory effects of the four main hop-derived prenylflavonoids on the activities and mRNA expression of the main drug-conjugating enzymes in human CaCo-2 cells. Proliferating CaCo-2 cells were used for these purposes as a model of colorectal cancer cells, and differentiated CaCo-2 cells were used as an enterocyte-like model. All the tested prenylflavonoids inhibited the CaCo-2 cells proliferation, with xanthohumol proving the most effective (IC50 8.5 μM). The prenylflavonoids modulated the activities and expressions of the studied enzymes to a greater extent in the differentiated, as opposed to the proliferating, CaCo-2 cells. In the differentiated cells, all the prenylflavonoids caused a marked increase in glutathione S-transferase and catechol-O-methyltransferase activities, while the activity of sulfotransferase was significantly inhibited. Moreover, the prenylflavonoids upregulated the mRNA expression of uridine diphosphate (UDP)-glucuronosyl transferase 1A6 and downregulated that of glutathione S-transferase 1A1/2.
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- $a Prenylflavonoids in the human organism exhibit various health-beneficial activities, although they may interfere with drugs via the modulation of the expression and/or activity of drug-metabolizing enzymes. As intestinal cells are exposed to the highest concentrations of prenylflavonoids, we decided to study the cytotoxicity and modulatory effects of the four main hop-derived prenylflavonoids on the activities and mRNA expression of the main drug-conjugating enzymes in human CaCo-2 cells. Proliferating CaCo-2 cells were used for these purposes as a model of colorectal cancer cells, and differentiated CaCo-2 cells were used as an enterocyte-like model. All the tested prenylflavonoids inhibited the CaCo-2 cells proliferation, with xanthohumol proving the most effective (IC50 8.5 μM). The prenylflavonoids modulated the activities and expressions of the studied enzymes to a greater extent in the differentiated, as opposed to the proliferating, CaCo-2 cells. In the differentiated cells, all the prenylflavonoids caused a marked increase in glutathione S-transferase and catechol-O-methyltransferase activities, while the activity of sulfotransferase was significantly inhibited. Moreover, the prenylflavonoids upregulated the mRNA expression of uridine diphosphate (UDP)-glucuronosyl transferase 1A6 and downregulated that of glutathione S-transferase 1A1/2.
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