[HTML][HTML] Activation of protein kinase B/Akt is sufficient to repress the glucocorticoid and cAMP induction of phosphoenolpyruvate carboxykinase gene
J Liao, A Barthel, K Nakatani, RA Roth - Journal of Biological Chemistry, 1998 - ASBMB
A rat hepatoma cell line, H4IIE, was stably transfected with a tamoxifen regulatable Akt-1
construct. Treatment of these cells with tamoxifen caused a rapid stimulation of Akt
enzymatic activity that was comparable with the activity observed with the endogenous Akt
after insulin stimulation. Prior studies have extensively documented that insulin can repress
the glucocorticoid and cAMP-stimulated increase in phosphoenolpyruvate carboxykinase
(PEPCK) gene transcription. Activation of this regulatable Akt with tamoxifen was found to …
construct. Treatment of these cells with tamoxifen caused a rapid stimulation of Akt
enzymatic activity that was comparable with the activity observed with the endogenous Akt
after insulin stimulation. Prior studies have extensively documented that insulin can repress
the glucocorticoid and cAMP-stimulated increase in phosphoenolpyruvate carboxykinase
(PEPCK) gene transcription. Activation of this regulatable Akt with tamoxifen was found to …