CYCLIC AMP and cyclic GMP have been postulated to be in certain cases, antagonistic intracellular messengers of many hormones and neurotransmitters acting at the cell membrane1. At least part of their antagonism may be the result of their ability to affect, in opposite directions, specific protein kinases and phosphates which work on common substrates (enzymes, structural proteins). Cyclic AMP and cyclic GMP have been found to activate, and the former also to inhibit, specific protein kinases2–5; cyclic AMP can activate or inhibit5–8 specific protein phosphates, and both cyclic nucleotide-sensitive protein kinases and protein phosphates have been isolated forming a complex with their substrate5. Some of these effects of cyclic nucleotides, however, have been found to depend on the type and concentration (not necessarily physiological) of the ion used in the assay5 and no direct evidence exists to show that one of the cyclic nucleotides opposes the effects of the other on protein phosphorylation. We report here that physiological concentrations (10−7 M–10−9 M) of cyclic GMP oppose the cyclic AMP (10−6M) dependent phosphorylation of a soluble, perhaps tubulin-related brain protein, possibly by activation of a phosphoprotein phosphatase.
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