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J. Biol. Chem., Vol. 265, Issue 22, 12846-12853, 08, 1990
SJ Pandol and MS Schoeffield-Payne
The present studies were performed to determine the role of cyclic GMP in
regulating agonist mediated calcium entry in the pancreatic acinar cell. In
guinea pig-dispersed pancreatic acini the findings demonstrated that
carbachol stimulated a transient 20-40-fold rise in cellular cyclic GMP
followed by a sustained 3-4-fold rise in cellular cyclic GMP. The guanylate
cyclase inhibitor, 6-anilino-5,8- quinolinedione (LY83583), caused a
dose-dependent inhibition of carbachol-stimulated increases in cellular
cyclic GMP both during the initial transient large increase in cyclic GMP
and the sustained increase in cyclic GMP. LY83583 also inhibited cellular
Ca2+ influx during carbachol stimulation and reloading of the
agonist-sensitive pool of Ca2+ at the termination of carbachol stimulation
with atropine. The effect of the inhibition on reloading of the
agonist-sensitive pool was secondary to its effects on the plasma membrane
C2+ entry. The addition of dibutyryl cyclic GMP to LY83583-treated acini
restored Ca2+ influx across the plasma membrane. Nitroprusside increased
both cellular cyclic GMP and the rate of Ca2+ influx. During periods when
plasma membrane Ca2+ entry was activated, cellular cyclic GMP levels were
increased. These results suggest that agonist-induced increases in cellular
cyclic GMP are necessary and sufficient to mediate the effects of the
agonist on the plasma membrane Ca2+ entry mechanism.
Cyclic GMP mediates the agonist-stimulated increase in plasma membrane calcium entry in the pancreatic acinar cell
Department of Medicine, Veterans Administration, San Diego, California.
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