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Title: The human intestinal fatty acid binding protein (hFABP2) gene is regulated by HNF-4{alpha}

Abstract

The cytosolic human intestinal fatty acid binding protein (hFABP2) is proposed to be involved in intestinal absorption of long-chain fatty acids. The aim of this study was to investigate the regulation of hFABP2 by the endodermal hepatocyte nuclear factor 4{alpha} (HNF-4{alpha}), involved in regulation of genes of fatty acid metabolism and differentiation. Electromobility shift assays demonstrated that HNF-4{alpha} binds at position -324 to -336 within the hFABP2 promoter. Mutation of this HNF-4 binding site abolished the luciferase reporter activity of hFABP2 in postconfluent Caco-2 cells. In HeLa cells, this mutation reduced the activation of the hFABP2 promoter by HNF-4{alpha} by about 50%. Thus, binding element at position -336/-324 essentially determines the transcriptional activity of promoter and may be important in control of hFABP2 expression by dietary lipids and differentiation. Studying genotype interactions of hFABP2 and HNF-4{alpha}, that are both candidate genes for diabetes type 2, may be a powerful approach.

Authors:
 [1];  [2];  [2];  [2]
  1. Molecular Nutrition, Institute of Human Nutrition and Food Science, Christian-Albrechts-University of Kiel, Heinrich-Hecht-Platz 10, D-24118 Kiel (Germany). E-mail: klapper@molnut.uni-kiel.de
  2. Molecular Nutrition, Institute of Human Nutrition and Food Science, Christian-Albrechts-University of Kiel, Heinrich-Hecht-Platz 10, D-24118 Kiel (Germany)
Publication Date:
OSTI Identifier:
20991313
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 356; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2007.02.091; PII: S0006-291X(07)00395-6; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CARBOXYLIC ACIDS; GENE REGULATION; GENES; GENOTYPE; HELA CELLS; INTESTINAL ABSORPTION; LIPIDS; LUCIFERASE; METABOLISM; MUTATIONS; PROMOTERS

Citation Formats

Klapper, Maja, Boehme, Mike, Nitz, Inke, and Doering, Frank. The human intestinal fatty acid binding protein (hFABP2) gene is regulated by HNF-4{alpha}. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.02.091.
Klapper, Maja, Boehme, Mike, Nitz, Inke, & Doering, Frank. The human intestinal fatty acid binding protein (hFABP2) gene is regulated by HNF-4{alpha}. United States. doi:10.1016/j.bbrc.2007.02.091.
Klapper, Maja, Boehme, Mike, Nitz, Inke, and Doering, Frank. Fri . "The human intestinal fatty acid binding protein (hFABP2) gene is regulated by HNF-4{alpha}". United States. doi:10.1016/j.bbrc.2007.02.091.
@article{osti_20991313,
title = {The human intestinal fatty acid binding protein (hFABP2) gene is regulated by HNF-4{alpha}},
author = {Klapper, Maja and Boehme, Mike and Nitz, Inke and Doering, Frank},
abstractNote = {The cytosolic human intestinal fatty acid binding protein (hFABP2) is proposed to be involved in intestinal absorption of long-chain fatty acids. The aim of this study was to investigate the regulation of hFABP2 by the endodermal hepatocyte nuclear factor 4{alpha} (HNF-4{alpha}), involved in regulation of genes of fatty acid metabolism and differentiation. Electromobility shift assays demonstrated that HNF-4{alpha} binds at position -324 to -336 within the hFABP2 promoter. Mutation of this HNF-4 binding site abolished the luciferase reporter activity of hFABP2 in postconfluent Caco-2 cells. In HeLa cells, this mutation reduced the activation of the hFABP2 promoter by HNF-4{alpha} by about 50%. Thus, binding element at position -336/-324 essentially determines the transcriptional activity of promoter and may be important in control of hFABP2 expression by dietary lipids and differentiation. Studying genotype interactions of hFABP2 and HNF-4{alpha}, that are both candidate genes for diabetes type 2, may be a powerful approach.},
doi = {10.1016/j.bbrc.2007.02.091},
journal = {Biochemical and Biophysical Research Communications},
number = 1,
volume = 356,
place = {United States},
year = {Fri Apr 27 00:00:00 EDT 2007},
month = {Fri Apr 27 00:00:00 EDT 2007}
}