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J. Biol. Chem., Vol. 275, Issue 24, 18358-18365, June 16, 2000
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From the Department of Biochemistry and Molecular Biology and the
Institute of Genetic Science, Yonsei University College of
Medicine, 134 Shinchon-dong, Seodaemun-gu, Seoul 120-752, South
Korea
We investigated transacting factors binding to
the cis-element important in tissue-specific expression of the human
glucose transporter type 2 isoform (GLUT2) gene. By transient
transfection assay, we determined that the 227-base pair fragment
upstream of the ATG start site contained promoter activity and that the region from +87 to +132 (site C) was responsible for tissue-specific expression. DNase I footprinting and electrophoretic mobility shift
assay indicated that site C contained one binding site for hepatocyte
nuclear factor 1 (HNF1) and two binding sites for HNF3. The mutations
at positions +101 and +103, which are considered to be critical in
binding HNF1 and HNF3, resulted in a 53% decrease in promoter
activity, whereas the mutation of the proximal HNF3 binding site (+115
and +117) reduced promoter activity by 28%. The mutations of these
four sites resulted in marked decrease (70%) in promoter activity as
well as diminished bindings of HNF1 and HNF3. A to G mutation, which
causes conversion of the HNF1 and HNF3 binding sequence to the NF-Y
binding site, resulted in a 22% decrease in promoter activity. We
identified that both HNF1 and HNF3 function as transcriptional
activators in GLUT2 gene expression. Coexpression of the pGL+74 (+74 to
+301) construct with the HNF1
Identification of Transacting Factors Responsible for the
Tissue-specific Expression of Human Glucose Transporter Type 2 Isoform Gene
COOPERATIVE ROLE OF HEPATOCYTE NUCLEAR FACTORS 1
AND
3
*
,, and HNF3 expression vectors in NIH
3T3 cells showed the synergistic effect on GLUT2 promoter activity
compared with the expression of HNF1, HNF3, or a combination of
HNF1 and HNF3. These data suggest that HNF1 and HNF3 may be
the most important players in the tissue-specific expression of the
human GLUT2 gene.
*
This work was supported by Korea Science and Engineering
Foundation Grant 96-0403-14-01-3.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of a scholarship from the Brain Korea 21 Project For
Medical Science, Ministry of Education, South Korea.
§
To whom correspondence should be addressed: Dept. of Biochemistry
and Molecular Biology, Yonsei University College of Medicine, 134 Shinchon-dong, Seodaemun-gu, Seoul 120-752, Korea. Tel.:
82-2-361-5187; Fax: 82-2-312-5041; E-mail:
yha111@yumc.yonsei.ac.kr.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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