Activation of malonyl-CoA decarboxylase in rat skeletal muscle by contraction and the AMP-activated protein kinase activator 5-aminoimidazole-4-carboxamide-1-beta -D-ribofuranoside.

@article{Saha2000ActivationOM,
  title={Activation of malonyl-CoA decarboxylase in rat skeletal muscle by contraction and the AMP-activated protein kinase activator 5-aminoimidazole-4-carboxamide-1-beta -D-ribofuranoside.},
  author={Asish K. Saha and A J Schwarsin and Rapha{\"e}l Roduit and Fr{\'e}d{\'e}ric Mass{\'e} and Virendar K. Kaushik and Keith Tornheim and Marc Prentki and Neil Bertrand Ruderman},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 32},
  pages={24279-83}
}
Alterations in the concentration of malonyl-CoA, an inhibitor of carnitine palmitoyltransferase I, have been linked to the regulation of fatty acid oxidation in skeletal muscle. During contraction decreases in muscle malonyl-CoA concentration have been related to activation of AMP-activated protein kinase (AMPK), which phosphorylates and inhibits acetyl-CoA carboxylase (ACC), the rate-limiting enzyme in malonyl-CoA formation. We report here that the activity of malonyl-CoA decarboxylase (MCD… CONTINUE READING
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