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Science 17 June 1988: Vol. 240. no. 4859, pp. 1655 - 1657 DOI: 10.1126/science.2454507
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Articles
Science, Vol 240, Issue 4859, 1655-1657
Copyright © 1988 by American Association for the Advancement of Science
Modulation of acetylcholine receptor desensitization by forskolin is independent of cAMP
PK Wagoner
and
BS Pallotta
Department of Molecular Pharmacology, Glaxo Research Laboratories, Chapel Hill, NC 27599.
Biochemical and electrophysiological studies suggest that adenosine 3',5'-monophosphate (cAMP)-dependent phosphorylation of the nicotinic acetylcholine receptor channel is functionally significant because it modifies the receptor's rate of desensitization to acetylcholine. In studies that support this conclusion researchers have used forskolin to stimulate cAMP-dependent phosphorylation in intact muscle. It is now shown that although forskolin facilitated desensitization in voltage-clamped rat muscle, this effect was not correlated with the abilities of forskolin and forskolin analogs to activate adenylate cyclase or phosphorylate the receptor. Furthermore, elevation of intracellular cAMP or addition of the catalytic subunit of A-kinase failed to alter desensitization. Therefore, in intact skeletal muscle, cAMP-dependent phosphorylation does not modulate desensitization.
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