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Investigation of in vitro inhibition of cytochrome P450 1A subfamily enzymes (CYP1A1/2) by polyphenols from coffee
Author(s) -
Bouskela Alice,
Oliveira Ana C.A.X.,
Paumgartten Francisco,
Farah Adriana
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.636.17
Subject(s) - naringin , chemistry , cyp1a2 , polyphenol , cytochrome p450 , biochemistry , quercetin , chlorogenic acid , microsome , pharmacology , enzyme , food science , antioxidant , biology , chromatography
It is suggested that dietary polyphenols play a protective role in the development of chronic diseases. Chlorogenic acids, mainly 5‐ caffeoylquinic acid, are the most abundant polyphenols in coffee, a largely consumed drink worldwide. Despite recent advances in the elucidation of their metabolism, it is still unknown whether they are substrates for the liver enzyme cytochrome P450 system. Knowing that the CYP1A1/2 play an important role in the biotransformation of flavonoids and other polyphenols, the purpose of this study was to investigate the inhibitory effects of 5‐ caffeoylquinic acid and other hydroxycinnamates from coffee on the activity of CYP1A1/2 in rat liver microsomes. Additionally, daidzein, hesperetin, naringin, quercetin and resveratrol, representing the major classes of polyphenols in foods, were tested for comparison purposes. The effects of the tested substances on the activity of ethoxyresorufin‐ O ‐deethylase and methoxyresorufin‐ O ‐demethylase, used as markers of CYP1A1 and CYP1A2, respectively, were determined in hepatic microsomes from Wistar rats treated with β‐naphthoflavone. Results showed that coffee polyphenols did not inhibit CYP1A1/2, which suggests that these substances are not substrates for them. All other polyphenols tested, except for naringin, showed clear inhibition on CYP1A1/2. Quercetin inhibition was particulaly potent (IC 50 = 2.73 and 6.90 μM for CYP1A1 and CYP1A2, respectively), comparable to α‐ naphthoflavone (control).