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Am J Physiol Gastrointest Liver Physiol (February 3, 2005). doi:10.1152/ajpgi.00312.2004
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Submitted on July 15, 2004
Accepted on January 26, 2005

Role of USF1 and USF2 as potential repressor proteins for human intestinal monocarboxylate transporter 1 (MCT1) promoter

Christos Hadjiagapiou1, Alip Borthakur1, Refka Y. Dahdal1, Ravinder K. Gill1, Jaleh Malakooti1, Krishnamurthy Ramaswamy1, and Pradeep K. Dudeja1*

1 Section of Digestive Diseases and Nutrition, Department of Medicine, University of Illinois at Chicago, Chicago, IL, USA; Jesse Brown VA Medical Center, Chicago, IL, USA

* To whom correspondence should be addressed. E-mail: pkdudeja{at}uic.edu.

Butyrate, a short chain fatty acid, is the major energy fuel for the colonocytes. We have previously reported that monocarboxylate transporter isoform 1 (MCT1) mediates uptake of butyrate by human colonic Caco-2 cells. To better understand the mechanisms of MCT1 expression and regulation in the human intestine, we examined the activity and regulation of MCT1 promoter in Caco-2 cells. The transcription initiation site in the MCT1 promoter was identified as a guanine nucleotide 281 bp upstream from the translation initiation site, and is surrounded by a GC rich area. The promoter was found to be highly active when transfected into Caco-2 cells and its activity decreased with deletions at its 5' end. Gel mobility shift experiments showed binding of the transcription factors USF1 and USF2 to the site -114 to -119 of the MCT1 promoter. Using site directed mutagenesis and promoter activity in Caco-2 cells, the USF proteins appeared to have a repressor role on the MCT1 promoter which was further confirmed by co-transfecting expression vectors encoding USF1 and 2 in Caco-2 cells and determining endogenous MCT1 expression in USF2 overexpressed cells. The two potential SP1 binding sites found in the same region of the promoter were found not to be involved in its regulation.




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