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A more recent version of this article appeared on October 6, 2000
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M003656200v1
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Papers In Press, published online ahead of print July 25, 2000
J. Biol. Chem, 10.1074/jbc.M003656200
Submitted on April 28, 2000
Revised on June 30, 2000
Accepted on July 24, 2000

NF-kappa B Inhibits Glucocorticoid and cAMP-Mediated Expression of the PEPCK Gene

Mary Waltner-Law, Marc C. Daniels, Calum Sutherland, and Daryl K. Granner

Molecular Physiology and Biophsyics, Vanderbilt University Medical Center, Nashville, Tennessee 37232-0615

Corresponding Author: daryl.granner{at}mcmail.vanderbilt.edu

Transcription of the phosphoenolpyruvate carboxykinase (PEPCK) gene is regulated by a variety of agents. Glucocorticoids, retinoic acid and glucagon (via its second messenger, cAMP) stimulate PEPCK gene transcription, whereas insulin, phorbol esters, cytokines and oxidative stress have an opposing effect. Stimulation of PEPCK gene expression has been extensively studied and a number of important DNA elements and binding proteins that regulate the transcription of this gene have been identified. However, the mechanisms utilized to turn off expression of this gene are not well-defined. Many of the negative regulators of PEPCK gene transcription also stimulate the nuclear localization and activation of the transcription factor NF-kB, so we hypothesized that this factor could be involved in the repression of PEPCK gene expression. We find that the p65 subunit of NF-kB represses the increase of PEPCK gene transcription mediated by glucocorticoids and cAMP in a concentration-dependent manner. The mutation of an NF-kB binding element identified in the PEPCK gene promoter fails to abrogate this repression. Further analysis suggests that p65 represses PEPCK gene transcription through a proteinoprotein interaction with the coactivator, CREB binding protein (CBP).


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