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(Received for publication, March 22, 1996, and in revised form, May 23, 1996)
From the Department of Pathology, Division of Molecular and
Cellular Pathology, The University of Alabama at Birmingham,
Birmingham, Alabama 35294-0019
The effects of cyclic GMP (cGMP) and activation
of cGMP-dependent protein kinase (PKG) on the
phosphorylation of the inositol 1,4,5-trisphosphate (IP3)
receptor were examined in intact rat aorta using the technique of back
phosphorylation. Aorta treated with the nitric oxide donors,
S-nitroso-N-acetylpenicillamine and sodium
nitroprusside, or the selective PKG activator,
8-(4-para-chlorophenylthio)-cGMP (8-CPT-cGMP), demonstrated
increased IP3 receptor phosphorylation in situ,
which was both time- and concentration-dependent with a
stoichiometry of 0.5 mol of phosphate/mol of receptor above control.
Treatment of aorta with the adenyl cyclase activator, forskolin, also
demonstrated increased phosphorylation of the IP3 receptor
on the PKG site, although the selective cAMP-dependent
protein kinase activator, 8-(4-para-chlorophenylthio)-cAMP
(8-CPT-cAMP), did not increase the phosphorylation of the
IP3 receptor. Moreover, the PKG selective inhibitor, KT
5823, inhibited both sodium nitroprusside and forskolin-induced
IP3 receptor phosphorylation more potently than the
selective cAMP-dependent protein kinase inhibitor, KT 5720, suggesting
that PKG mediates the increase in IP3 receptor
phosphorylation by both cyclic nucleotides in intact aorta. These
results provide further support for the notion that PKG is activated by
both cAMP and cGMP in intact vascular smooth muscle and that PKG
performs a critical role in cyclic nucleotide-dependent
relaxation of blood vessels.
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