Cyclic AMP-dependent regulation of activities of synthetase and phosphodiesterase of 2?,5?-oligoadenylate in NIH 3T3 cells

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Abstract
Treatment of NIH 3T3 cells with adenylate cyclase activator adrenaline (10−6 M) or cAMP phosphodiesterase inhibitor theophylline (10−3 M) was shown to lead to intracellular cAMP elevation followed by a 2.0- to 2.5-fold increase in the 2′,5′-oligoadenylate synthetase activity. This process was blocked by actinomycin D. The rise in the intracellular cAMP level was also followed by a 3–4-fold decrease in the activity of 2′-phosphodiesterase. Propranolol prevented this inhibition but actinomycin D produced only a negligible effect on the process. Incubation of the cell homogenate with purified catalytic subunit of CAMP-dependent protein kinase and ATP also resulted in a decrease of 2′-phosphodiesterase activity. These results indicate that cAMP is involved in the regulation of enzymes of the 2′,5′-oligoadenylate system. The possibility that certain biological functions of cAMP are implemented via 2′,5′-oligoadenylate-dependent processes is discussed.

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