Characterization of 5'AMP-activated protein kinase activity in the heart and its role in inhibiting acetyl-CoA carboxylase during reperfusion following ischemia.

@article{Kudo1996CharacterizationO5,
  title={Characterization of 5'AMP-activated protein kinase activity in the heart and its role in inhibiting acetyl-CoA carboxylase during reperfusion following ischemia.},
  author={Naomi Kudo and Joe Gillespie and Lili Kung and Lee Alan Witters and Rainer Schulz and Alexander A S C Clanachan and Gary D Lopaschuk},
  journal={Biochimica et biophysica acta},
  year={1996},
  volume={1301 1-2},
  pages={67-75}
}
Despite the high expression of 5'AMP activated protein kinase (AMPK) in heart, the activity and function of this enzyme in heart muscle has not been characterized. We demonstrate that rat hearts have a high AMPK activity, comparable to that found in liver, which could be stimulated up to 3-fold by 5'AMP. Cardiac AMPK is also under phosphorylation control, since in vitro incubation of cardiac AMPK with protein phosphatase 2A completely abolished activity, while incubation with ATP/Mg(2… CONTINUE READING
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