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J Biol Chem, Vol. 274, Issue 1, 211-217, January 1, 1999

Role of CCAAT Enhancer-binding Protein  in the Thyroid Hormone and cAMP Induction of Phosphoenolpyruvate Carboxykinase Gene Transcription

Edwards A. Park, Shulan Song, Charles Vinson^¶, and William J. Roesler

From the  Department of Pharmacology, College of Medicine, University of Tennessee Health Science Center, Memphis, Tennessee 38163, the  Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada, and the ^¶ Laboratory of Biochemistry, NCI, National Institutes of Health, Bethesda, Maryland 20892

Transcription of the gene for phosphoenolpyruvate carboxykinase (PEPCK) is stimulated by thyroid hormone (T₃) and cAMP. Two DNA elements in the PEPCK promoter are required for T₃ responsiveness including a thyroid hormone response element and a binding site called P3(I) for the CCAAT enhancer-binding protein (C/EBP). Both the  and  isoforms of C/EBP are highly expressed in the liver. C/EBP contributes to the liver-specific expression and cAMP responsiveness of the PEPCK gene. In this study, we examined the ability of C/EBP when bound to the P3(I) site to regulate PEPCK gene expression. We report that C/EBP can stimulate basal expression and participate in the induction of PEPCK gene transcription by T₃ and cAMP. The cAMP-responsive element-binding protein and AP1 proteins that contribute to the induction by cAMP are not involved in the stimulation by T₃. A small region of the transactivation domain of C/EBP is sufficient for the stimulation of basal expression and cAMP responsiveness. Our results suggest that C/EBP and C/EBP are functionally interchangeable when bound to the P3(I) site of the PEPCK promoter.

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