The human fatty acid binding protein (FABP2) is involved in intestinal 
absorption and intracellular trafficking of long-chain fatty acids. Here we 
investigate transcriptional regulation of FABP2 by the endodermal hepatic 
nuclear factor 1 alpha (HNF-1alpha). In electromobility shift and supershift 
assays we show the presence of two adjacent HNF-1alpha binding sites within the 
FABP2 promoter regions -185 to -165 and -169 to -149. HNF-1alpha activates an 
FABP2 promoter luciferase construct by 3.5 and 20-fold in Caco-2 and Hela cells, 
respectively. Mutational analysis of HNF-1alpha elements resulted in about 50% 
reduction of basal and HNF-1alpha induced activity of FABP2 promoter constructs, 
predominantly caused by deletion of the -185 to -165 site. Thus, our data 
suggest a major role of HNF-1alpha in control of FABP2 expression in intestine 
via a functional HNF-1alpha recognition element within FABP2 promoter region 
-185 to -165.