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-D-ribofuranoside
(AICAR) stimulates myocardial glycogenolysis by allosteric
mechanisms
1 McDonald Research Laboratories/The iCAPTUR4E Centre, Department of Pathology and Laboratory Medicine, University of British Columbia-St.Paul's Hospital, Vancouver, British Columbia V6Z 1Y6; and 2 Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3
We tested the
hypothesis that activation of AMP-activated protein kinase (AMPK)
promotes myocardial glycogenolysis by decreasing glycogen synthase (GS)
and/or increasing glycogen phosphorylase (GP) activities. Isolated
working hearts from halothane-anesthetized male Sprague-Dawley rats
perfused in the absence or presence of 0.8 or 1.2 mM
5-aminoimidazole-4-carboxamide 1-
-D-ribofuranoside (AICAR), an adenosine analog and cell-permeable activator of AMPK, were
studied. Glycogen degradation was increased by AICAR, while glycogen
synthesis was not affected. AICAR increased myocardial 5-aminoimidazole-4-carboxamide 1--D-ribofuranotide
(ZMP), the active intracellular form of AICAR, but did not alter the
activity of GS and GP measured in tissue homogenates or the content of glucose-6-phosphate and adenine nucleotides in freeze-clamped tissue.
Importantly, the calculated intracellular concentration of ZMP achieved
in this study was similar to the Km value of ZMP for GP determined in homogenates of myocardial tissue. We conclude that
the data are consistent with allosteric activation of GP by ZMP being
responsible for the glycogenolysis caused by AICAR in the intact rat heart.
myocardium; glycogen metabolism; adenosine 5'-monophosphate-activated protein kinase
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