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The effect of calyculin A was rapid (within 5 min) and persisted in the presence of phosphodiesterase inhibition. However, in contrast to protein kinase C activation or intracellular calcium elevation, the phosphatase inhibitors were less effective in potentiating the cAMP response stimulated by forskolin or cholera toxin, and their effects were not blocked by calphostin C or N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide. The adrenergic-stimulated cGMP response was also less sensitive to the phosphatase inhibition. Therefore, our results suggest that 1) the adrenergic-stimulated cAMP signal is subjected to the tonic inhibition by phosphoprotein phosphatase; 2) phosphatase inhibitors enhance cAMP synthesis through their actions at the receptor level; and 3) the cAMP signal is more sensitive to the regulation by phosphorylation than cGMP in rat pinealocytes.<\/jats:p>","DOI":"10.1152\/ajpendo.1995.268.3.e458","type":"journal-article","created":{"date-parts":[[2017,12,22]],"date-time":"2017-12-22T01:10:52Z","timestamp":1513905052000},"page":"E458-E466","source":"Crossref","is-referenced-by-count":5,"title":["Phosphatase inhibitors potentiate adrenergic-stimulated cAMP and cGMP production in rat pinealocytes"],"prefix":"10.1152","volume":"268","author":[{"given":"A. K.","family":"Ho","sequence":"first","affiliation":[{"name":"Department of Physiology, Faculty of Medicine, University of Alberta,Edmonton, Canada."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C. 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