AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle

G. F. Merrill, E. J. Kurth, D. G. Hardie, W. W. Winder

Research output: Contribution to journalArticlepeer-review

896 Scopus citations

Abstract

5-Aminoimidazole-4-carboxamide ribonucleoside (AICAR) has previously been reported to be taken up into cells and phosphorylated to form ZMP, an analog of 5'-AMP. This study was designed to determine whether AICAR can activate AMP-activated protein kinase (AMPK) in skeletal muscle with consequent phosphorylation of acetyl-CoA carboxylase (ACC), decrease in malonyl-CoA, and increase in fatty acid oxidation. Rat hindlimbs were perfused with Krebs-Henseleit bicarbonate containing 4% bovine serum albumin, washed bovine red blood cells, 200 μU/ml insulin, and 10 mM glucose with or without AICAR (0.5-2.0 mM). Perfusion with medium containing AICAR was found to activate AMPK in skeletal muscle, inactivate ACC, and decrease malonyl- CoA. Hindlimbs perfused with 2 mM AICAR for 45 min exhibited a 2.8-fold increase in fatty acid oxidation and a significant increase in glucose uptake. No difference was observed in oxygen uptake in AICAR vs. control hindlimb. These results provide evidence that decreases in muscle content of malonyl-CoA can increase the rate of fatty acid oxidation.

Original languageEnglish (US)
Pages (from-to)E1107-E1112
JournalAmerican Journal of Physiology - Endocrinology and Metabolism
Volume273
Issue number6 36-6
DOIs
StatePublished - 1997

All Science Journal Classification (ASJC) codes

  • Endocrinology, Diabetes and Metabolism
  • Physiology
  • Physiology (medical)

Keywords

  • 5- aminoimidazole-4-carboxamide riboside
  • Acetyl-CoA carboxylase
  • Malonyl-CoA
  • Palmirate oxidation
  • ZMP

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