J 2017

Butyrate alters expression of cytochrome P450 1A1 and metabolism of benzo[a] pyrene via its histone deacetylase activity in colon epithelial cell models

ZAPLETAL, Ondřej, Zuzana TYLICHOVÁ, Jiří NEČA, Jiří KOHOUTEK, Miroslav MACHALA et. al.

Základní údaje

Originální název

Butyrate alters expression of cytochrome P450 1A1 and metabolism of benzo[a] pyrene via its histone deacetylase activity in colon epithelial cell models

Autoři

ZAPLETAL, Ondřej (203 Česká republika, domácí), Zuzana TYLICHOVÁ (203 Česká republika, domácí), Jiří NEČA (203 Česká republika), Jiří KOHOUTEK (203 Česká republika), Miroslav MACHALA (203 Česká republika), A. MILCOVA (203 Česká republika), Michaela POKORNA (203 Česká republika), Jan TOPINKA (203 Česká republika), M.P. MOYER (840 Spojené státy), Jiřina HOFMANOVÁ (203 Česká republika), Alois KOZUBÍK (203 Česká republika) a Jan VONDRÁČEK (203 Česká republika, garant)

Vydání

ARCHIVES OF TOXICOLOGY, HEIDELBERG, SPRINGER HEIDELBERG, 2017, 0340-5761

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10601 Cell biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 5.728

Kód RIV

RIV/00216224:14310/17:00097700

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000399875300008

Klíčová slova anglicky

CYP1A1; Butyrate; Polycyclic aromatic hydrocarbons; DNA adducts; Histone deacetylases; Colon epithelial cells

Štítky

Příznaky

Mezinárodní význam, Recenzováno
Změněno: 29. 3. 2018 15:21, Ing. Nicole Zrilić

Anotace

V originále

Butyrate, a short-chain fatty acid produced by fermentation of dietary fiber, is an important regulator of colonic epithelium homeostasis. In this study, we investigated the impact of this histone deacetylase (HDAC) inhibitor on expression/activity of cytochrome P450 family 1 (CYP1) and on metabolism of carcinogenic polycyclic aromatic hydrocarbon, benzo[a] pyrene (BaP), in colon epithelial cells. Sodium butyrate (NaBt) strongly potentiated the BaP-induced expression of CYP1A1 in human colon carcinoma HCT116 cells. It also co-stimulated the 7-ethoxyresorufin-O-deethylase (EROD) activity induced by the 2,3,7,8-tetrachlorodibenzo-p-dioxin, a prototypical ligand of the aryl hydrocarbon receptor. Up-regulation of CYP1A1 expression/activity corresponded with an enhanced metabolism of BaP and formation of covalent DNA adducts. NaBt significantly potentiated CYP1A1 induction and/or metabolic activation of BaP also in other human colon cell models, colon adenoma AA/C1 cells, colon carcinoma HT-29 cells, or in NCM460D cell line derived from normal colon mucosa. Our results suggest that the effects of NaBt were due to its impact on histone acetylation, because additional HDAC inhibitors (trichostatin A and suberanilohydroxamic acid) likewise increased both the induction of EROD activity and formation of covalent DNA adducts. NaBt-induced acetylation of histone II3 (at Lys14) and histone II4 (at Lys16), two histone modifications modulated during activation of CYP1A1 transcription, and it reduced binding of HDAC1 to the enhancer region of CYP1A1 gene. This in vitro study suggests that butyrate, through modulation of histone acetylation, may potentiate induction of CYP1A1 expression, which might in turn alter the metabolism of BaP within colon epithelial cells.