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J. Biol. Chem., Vol. 266, Issue 24, 16247-16254, Aug, 1991
M Horiuchi, N Nakamura, SS Tang, G Barrett and VJ Dzau
Renin gene expression in the mouse kidney and submandibular gland (SMG) are
differentially regulated by cAMP. In this study, we examined the potential
molecular mechanism responsible for this tissue-specific regulation. 32P
end-labeled synthetic oligonucleotide containing mouse renin
cAMP-responsive element (CRE) was incubated with kidney nuclear extracts
from either control or cAMP-treated mice and analyzed by gel mobility shift
assay. Our results demonstrated that cAMP induced a nuclear protein which
complexed with the CRE oligonucleotide in a specific manner. This nuclear
protein-DNA binding was competed effectively by the oligonucleotide
containing human chorionic gonadotropin alpha-subunit CRE but not by the
mouse renin DNA fragment from which the CRE was deleted by site-directed
mutagenesis. In contrast, no DNA-protein complex formation could be
detected when this [32P]CRE oligonucleotide was incubated with the SMG
nuclear extract from control or cAMP-treated mice. However, CRE-binding
protein complex formation was demonstrated in the SMG nuclear extract when
the incubation was performed in the presence of 0.8% sodium deoxycholate
and 1.2% Nonidet P-40, detergents that dissociate protein-protein
complexes. Furthermore, in the absence of deoxycholate, we observed that
SMG nuclear extract attenuated the binding of the kidney CRE- binding
protein to mouse renin CRE in a dose-dependent manner and this inhibitory
effect of SMG nuclear extract disappeared in the presence of sodium
deoxycholate. This inhibitory nuclear protein in SMG is specific for
CRE-binding protein since it does not affect nuclear protein binding to
synthetic DNA oligonucleotides of human collagenase AP-1 and human
metallothionein AP-2. Our data further suggest that inhibitory nuclear
protein is present in lower quantities in other extrarenal tissues, i.e.
testes, liver, brain, heart, but is not detectable in the kidney. Taken
together, these results suggest that the SMG and certain extrarenal tissues
contain nuclear trans-acting factor(s) that interact with CRE-binding
protein, thereby interfering with its binding to mouse renin CRE. The
presence of this inhibitory protein in the mouse SMG nucleus may contribute
to the tissue-specific regulation of the renin gene expression by cAMP.
Molecular mechanism of tissue-specific regulation of mouse renin gene expression by cAMP. Identification of an inhibitory protein that binds nuclear transcriptional factor
Cardiovascular Research Center, Stanford University School of Medicine, California 94305-5246.
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