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Journal of Lipid Research, Vol 37, 1831-1841, Copyright © 1996 by Lipid Research, Inc.
DP Wang, D Stroup, M Marrapodi, M Crestani, G Galli and JY Chiang
A stable HepG2 cell line harboring a human cholesterol 7 alpha- hydroxylase
(CYP7A) minigene/luciferase reporter gene construct was selected for
studying transcriptional regulation of CYP7A gene promoter. Insulin and
phorbol 12-myristate-13-acetate (PMA) strongly repressed the promoter
activity as measured with luciferase activity expressed in the cells. The
promoter activity of the 5' progressive deletion/luciferase reporter gene
constructs was studied in a transient transfection assay in HepG2 cells.
PMA represses the promoter activity and the response elements were
localized in the -184/-151 and -134/-81 regions. Insulin also represses the
promoter activity and response element was mapped in the -298/-81 region.
Surprisingly, glucocorticoid receptor (GR) strongly inhibited promoter
activity in the presence of dexamethasone, and response elements were
localized in the -298/-151 and the -150/+24 regions. Thyroid hormone
receptor also repressed promoter activity and response elements were
localized in the -150/+24 and upstream regions. Cotransfection of CYP7A
chimeric constructs with an expression vector carrying liver-enriched
transcription factor HNF3 alpha stimulated the reporter gene activity, but
cotransfection with GR plasmid interfered with the HNF3 alpha-stimulated
activity possibly through competition for binding to overlapping GR/HNF3
binding sites. Thus, human cholesterol 7 alpha-hydroxylase gene promoter is
strongly repressed by insulin, PMA, and steroid/thyroid hormones and
results in the low level of cholesterol 7 alpha-hydroxylase expression in
the human liver.
ARTICLES
Transcriptional regulation of the human cholesterol 7 alpha-hydroxylase gene (CYP7A) in HepG2 cells
Department of Biochemistry and Molecular Pathology, Northeastern Ohio Universities College of Medicine, Rootstown 44272, USA.
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