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J Biol Chem, Vol. 275, Issue 16, 12108-12118, April 21, 2000
From the Department of Molecular Physiology and Biophysics,
Vanderbilt University Medical School, Nashville, Tennessee 37232
In liver and kidney, the terminal step in
gluconeogenesis is catalyzed by glucose-6-phosphatase. To examine the
effect of the cAMP signal transduction pathway on transcription of the
gene encoding the catalytic subunit of glucose-6-phosphatase (G6Pase), G6Pase-chloramphenicol acetyltransferase (CAT) fusion genes were transiently transfected into either the liver-derived HepG2 or kidney-derived LLC-PK cell line. Co-transfection of an expression vector encoding the catalytic subunit of cAMP-dependent
protein kinase (PKA) markedly stimulated G6Pase-CAT fusion gene
expression, and mutational analysis of the G6Pase promoter revealed
that multiple regions are required for this PKA response in both the
HepG2 and LLC-PK cell lines. A sequence in the G6Pase promoter that
resembles a cAMP response element is required for the full PKA response in both HepG2 and LLC-PK cells. However, in LLC-PK cells, but not in
HepG2 cells, a hepatocyte nuclear factor-1 (HNF-1) binding site was
critical for the full induction of G6Pase-CAT expression by PKA.
Changing this HNF-1 motif to that for the yeast transcription factor
GAL4 reduces the PKA response in LLC-PK cells to the same degree as
deleting the HNF-1 site. However, co-transfection of this mutated
construct with chimeric proteins comprising the GAL4-DNA binding domain
ligated to the coding sequence for HNF-1 The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF217652.
Differential Role of Hepatocyte Nuclear Factor-1 in the
Regulation of Glucose-6-phosphatase Catalytic Subunit Gene
Transcription by cAMP in Liver- and Kidney-derived Cell Lines*
, HNF-1
, HNF-3, or HNF-4
completely restored the PKA response. Thus, we hypothesize that, in
LLC-PK cells, HNF-1 is acting as an accessory factor to enhance PKA
signaling through the cAMP response element by altering G6Pase promoter
conformation or accessibility rather than specifically affecting some
component of the PKA signal transduction pathway.
*
This work was supported by National Institutes of Health
Grants DK56374 (to R. O.) and P60 DK20593 (to the Vanderbilt
Diabetes Core laboratory).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.
To whom correspondence should be addressed: Dept. of Molecular
Physiology and Biophysics, 761 MRB II, Vanderbilt University Medical
School, Nashville, TN 37232-0615. Tel.: 615-936-1503; Fax:
615-322-7236.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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