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AJP - Endocrinology and Metabolism, Vol 272, Issue 5 E762-E768, Copyright © 1997 by American Physiological Society
ARTICLES |
L. Vergauwen, E. A. Richter and P. Hespel
Department of Kinesiology, Faculty of Physical Education and Physiotherapy, Katholieke Universiteit Leuven, Belgium.
The role of adenosine in regulating glycogen breakdown during electrically induced muscle contractions was investigated in isolated rat hindquarters perfused with a standard medium either lacking or containing 100 microU/ml insulin and/or 1.67 nM isoprenaline. Nonselective A1/A2-adenosine receptor antagonism via caffeine enhanced (P < 0.05) glycogen breakdown in contracting fast-oxidative (FO) fibers by 40%, provided they were exposed to both insulin and isoprenaline. Combined A1/A2-receptor antagonism by 8-cyclopentyl-1,3-dipropylxanthine (CPDPX) plus 3,7-dimethyl-1-proparglyxanthine (DMPX) fully reproduced (P < 0.05) this stimulatory effect. Furthermore, CPDPX plus DMPX also enhanced (P < 0.05) glycogenolysis during contractions in soleus but not in white gastrocnemius muscle. In contrast, CPDPX or DMPX alone did not affect glycogenolysis in either fiber type. Muscle adenosine 3',5'-cyclic monophosphate concentration during contractions was increased (P < 0.05) by CPDPX plus DMPX in both fiber types, whereas glycogen synthase fractional activity was depressed (P < 0.05). Phosphorylase activity was not changed by CPDPX plus DMPX. It is concluded that adenosine exerts a glycogen-sparing action in oxidative skeletal muscle exposed to both insulin and beta-adrenergic stimulation during contraction, presumably via stimulation of glycogen synthase activity.
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