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On the Possible Effect of Phytic Acid (Myo-Inositol Hexaphosphoric Acid, IP6) on Cytochromes P450 and Systems of Xenobiotic Metabolism in Different Hepatic Models
V. Frybortova, S. Satka, L. Jourova, I. Zapletalova, M. Srejber, P. Briolotti, M. Daujat-Chavanieu, S. Gerbal-Chaloin, P. Anzenbacher, M. Otyepka, E. Anzenbacherova
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články
Grantová podpora
RVO 61989592
Palacký University, Olomouc
IGA_LF_2024_006
Palacký University, Olomouc
IGA_LF_2024_011
Palacký University, Olomouc
e-INFRA CZ project no. ID:90254
Ministry of Education, Youth and Sports of the Czech Republic
NLK
Free Medical Journals
od 2000
Freely Accessible Science Journals
od 2000
PubMed Central
od 2007
Europe PubMed Central
od 2007
ProQuest Central
od 2000-03-01
Open Access Digital Library
od 2000-01-01
Open Access Digital Library
od 2007-01-01
Health & Medicine (ProQuest)
od 2000-03-01
ROAD: Directory of Open Access Scholarly Resources
od 2000
PubMed
38612422
DOI
10.3390/ijms25073610
Knihovny.cz E-zdroje
- MeSH
- kyselina fytová * MeSH
- lidé MeSH
- messenger RNA MeSH
- savci MeSH
- simulace molekulového dockingu MeSH
- systém (enzymů) cytochromů P-450 MeSH
- xenobiotika * MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
As compounds of natural origin enter human body, it is necessary to investigate their possible interactions with the metabolism of drugs and xenobiotics in general, namely with the cytochrome P450 (CYP) system. Phytic acid (myo-inositol hexaphosphoric acid, IP6) is mainly present in plants but is also an endogenous compound present in mammalian cells and tissues. It has been shown to exhibit protective effect in many pathological conditions. For this paper, its interaction with CYPs was studied using human liver microsomes, primary human hepatocytes, the HepG2 cell line, and molecular docking. Docking experiments and absorption spectra demonstrated the weak ability of IP6 to interact in the heme active site of CYP1A. Molecular docking suggested that IP6 preferentially binds to the protein surface, whereas binding to the active site of CYP1A2 was found to be less probable. Subsequently, we investigated the ability of IP6 to modulate the metabolism of xenobiotics for both the mRNA expression and enzymatic activity of CYP1A enzymes. Our findings revealed that IP6 can slightly modulate the mRNA levels and enzyme activity of CYP1A. However, thanks to the relatively weak interactions of IP6 with CYPs, the chances of the mechanisms of clinically important drug-drug interactions involving IP6 are low.
Citace poskytuje Crossref.org
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