DNA elements for constitutive androstane receptor- and pregnane X receptor-mediated regulation of bovine CYP3A28 gene.
Animals
Binding Sites
Cattle
Cell Line, Tumor
Cloning, Molecular
/ methods
Constitutive Androstane Receptor
Cytochrome P-450 CYP3A
/ chemistry
Gene Expression Regulation
Hep G2 Cells
Humans
Pregnane X Receptor
/ genetics
Promoter Regions, Genetic
Receptors, Cytoplasmic and Nuclear
/ genetics
Sequence Analysis, DNA
Transcription Factors
/ metabolism
Transfection
Journal
PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081
Informations de publication
Date de publication:
2019
2019
Historique:
received:
13
01
2019
accepted:
11
03
2019
entrez:
26
3
2019
pubmed:
26
3
2019
medline:
18
12
2019
Statut:
epublish
Résumé
The regulation of cytochrome P450 3A (CYP3A) enzymes is established in humans, but molecular mechanisms of its basal and xenobiotic-mediated regulation in cattle are still unknown. Here, ~10 kbp of the bovine CYP3A28 gene promoter were cloned and sequenced, and putative transcription factor binding sites were predicted. The CYP3A28 proximal promoter (PP; -284/+71 bp) contained DNA elements conserved among species. Co-transfection of bovine nuclear receptors (NRs) pregnane X and constitutive androstane receptor (bPXR and bCAR) with various CYP3A28 promoter constructs into hepatoma cell lines identified two main regions, the PP and the distal fragment F3 (-6899/-4937 bp), that were responsive to bPXR (both) and bCAR (F3 fragment only). Site-directed mutagenesis and deletion of NR motif ER6, hepatocyte nuclear factor 1 (HNF-1) and HNF-4 binding sites in the PP suggested either the involvement of ER6 element in bPXR-mediated activation or the cooperation between bPXR and liver-enriched transcription factors (LETFs) in PP transactivation. A putative DR5 element within the F3 fragment was involved in bCAR-mediated PP+F3 transactivation. Although DNA enrichment by anti-human NR antibodies was quite low, ChIP investigations in control and RU486-treated BFH12 cells, suggested that retinoid X receptor α (RXRα) bound to ER6 and DR5 motifs and its recruitment was enhanced by RU486 treatment. The DR5 element seemed to be recognized mainly by bCAR, while no clear-cut results were obtained for bPXR. Present results point to species-differences in CYP3A regulation and the complexity of bovine CYP3A28 regulatory elements, but further confirmatory studies are needed.
Identifiants
pubmed: 30908543
doi: 10.1371/journal.pone.0214338
pii: PONE-D-19-00855
pmc: PMC6433341
doi:
Substances chimiques
Constitutive Androstane Receptor
0
Pregnane X Receptor
0
Receptors, Cytoplasmic and Nuclear
0
Transcription Factors
0
Cytochrome P-450 CYP3A
EC 1.14.14.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0214338Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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