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J. Biol. Chem., Vol. 264, Issue 7, 3859-3863, Mar, 1989
Z Ahmad, FJ Green, HS Subuhi and AM Watanabe
Muscarinic cholinergic agonists such as acetylcholine attenuate
phosphorylation of phospholamban induced by agents that activate cAMP-
dependent protein kinase. However, cAMP accumulation is variably affected
or only slightly reduced; thus, the choline ester might produce effects in
addition to inhibition of adenylate cyclase. We hypothesized that
acetylcholine might regulate a phosphatase in mammalina myocardium.
Exposure of Langendoff-perfused guinea pig ventricles to isoproterenol (10
nM) for 45 s increased phosphatase inhibitor-1 activity 2-fold.
Co-administration of acetylcholine (100 nM) antagonized the effect of
isoproterenol, and atropine (1 microM) blocked the effect of acetylcholine.
Forskolin (1 microM) caused a 3- fold increase in inhibitor-1 activity, and
acetylcholine markedly attenuated the effect of forskolin. However,
acetylcholine did not lower cAMP levels in the same tissues. Both
isoproterenol and forskolin reduced the type 1 phosphatase activity
intrinsic to sarcoplasmic reticulum by 25-50%, using [32P]phosphorylase a
or 32P-labeled membrane vesicles as a substrate for the phosphatase.
Co-administration of acetylcholine markedly attenuated these effects of
isoproterenol and forskolin. Acetylcholine alone caused a 50% increase in
type 1 phosphatase activity. We concluded that inhibitor-1 and type 1
phosphatase can be regulated in intact cardiac muscle by agents that
increase intracellular cAMP and by acetylcholine.
Autonomic regulation of type 1 protein phosphatase in cardiac muscle
Department of Medicine, Indiana University School of Medicine, Indianapolis 46202.
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