Phosphorylation of the Inositol 1,4,5-Trisphosphate Receptor
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 271, Issue: 36, Page: 21933-21938
1996
- 183Citations
- 38Captures
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Article Description
The effects of cyclic GMP (cGMP) and activation of cGMP-dependent protein kinase (PKG) on the phosphorylation of the inositol 1,4,5-trisphosphate (IP 3 ) 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 IP 3 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 IP 3 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 IP 3 receptor. Moreover, the PKG selective inhibitor, KT 5823, inhibited both sodium nitroprusside and forskolin-induced IP 3 receptor phosphorylation more potently than the selective cAMP-dependent protein kinase inhibitor, KT 5720, suggesting that PKG mediates the increase in IP 3 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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819618818; http://dx.doi.org/10.1074/jbc.271.36.21933; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0029814390&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/8702997; https://linkinghub.elsevier.com/retrieve/pii/S0021925819618818; https://dx.doi.org/10.1074/jbc.271.36.21933
Elsevier BV
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