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J. Biol. Chem., Vol. 281, Issue 34, 24390-24397, August 25, 2006

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CCAAT/Enhancer-binding Protein Mediates Induction of Hepatic Phosphoenolpyruvate Carboxykinase by p38 Mitogen-activated Protein Kinase^*

Liping Qiao, Ormond A. MacDougald, and Jianhua Shao¹

From the Graduate Center for Nutritional Sciences, University of Kentucky, Lexington, Kentucky 40536 and the Departments of Molecular and Integrative Physiology and of Internal Medicine, University of Michigan, Ann Arbor, Michigan 48109

Excessive hepatic gluconeogenesis and glucose production are important contributors to hyperglycemia in both type 1 and type 2 diabetes. In diabetic humans and animal models, elevated levels of p38 mitogen-activated protein kinase (p38) are observed in several tissues. Our study shows that activity of p38 is significantly elevated in livers of db/db or streptozocin-induced type 1 diabetic mice. Using cultured hepatoma cells, we find that activation of p38 enhances expression of hepatic gluconeogenic gene phosphoenolpyruvate carboxykinase (PEPCK). Furthermore, our studies demonstrate that activation of p38 stimulates phosphorylation of CCAAT/enhancer-binding protein (C/EBP) at serine 21 and increases its transactivation activity in the context of PEPCK gene transcription. Our results indicate that C/EBP mediates p38-stimulated PEPCK transcription in liver cells.

Received for publication, March 30, 2006 , and in revised form, June 5, 2006.

^* This work was supported by American Diabetes Association Grants 1-06-RA-88 (to O. A. M.) and 1-04-JF-44 (to J. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Graduate Center for Nutritional Sciences, University of Kentucky, 900 S. Limestone, Lexington, KY 40536-0200. Tel.: 859-323-4933 (ext. 81801); Fax: 859-257-3565; E-mail: JianhuaShao{at}uky.edu.

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