AJP - Heart and Circulatory Physiology, Vol 266, Issue 3 1138-H1144, Copyright © 1994 by American Physiological Society

ARTICLES

M2-specific muscarinic cholinergic receptor-mediated inhibition of cardiac regulatory protein phosphorylation

R. C. Gupta, J. Neumann, P. Boknik and A. M. Watanabe
Henry Ford Hospital, Detroit, Michigan 48202.

Acetylcholine acting via muscarinic cholinoceptors decreased phosphorylation of phospholamban and troponin I without reducing adenosine 3',5'-cyclic monophosphate (cAMP) levels or cAMP-dependent protein kinase activity ratio in the presence of 10-100 nM isoproterenol in guinea pig ventricular myocytes. The effect of acetylcholine was more pronounced when adenosine deaminase (5 U/ml) was present and incubation period was short (10 s). Okadaic acid, an inhibitor of protein phosphatase activity, blocked the acetylcholine-mediated inhibition of isoproterenol-stimulated phosphorylation of phospholamban. It is suggested that acetylcholine reduces protein phosphorylation by a cAMP-independent mechanism in guinea pig ventricular myocytes.

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