Akt Activity Negatively Regulates Phosphorylation of AMP-activated Protein Kinase in the Heart*

@article{Kovacic2003AktAN,
  title={Akt Activity Negatively Regulates Phosphorylation of AMP-activated Protein Kinase in the Heart*},
  author={Suzanne Kovacic and C. Soltys and A. Barr and I. Shiojima and K. Walsh and J. Dyck},
  journal={Journal of Biological Chemistry},
  year={2003},
  volume={278},
  pages={39422 - 39427}
}
In the heart, insulin stimulates a variety of kinase cascades and controls glucose utilization. Because insulin is able to activate Akt and inactivate AMP-activated protein kinase (AMPK) in the heart, we hypothesized that Akt can regulate the activity of AMPK. To address the potential existence of this novel signaling pathway, we used a number of experimental protocols to activate Akt in cardiac myocytes and monitored the activation status of AMPK. Mouse hearts perfused in the presence of… Expand
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