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Effects of adenosine and guanosine on thyroidal ornithine decarboxylase, protein kinase, and the adenosine 3',5'-monophosphate-adenylate cyclase system in the mouse.

Ornithine decarboxylase (ODC), the rate-limiting enzymatic step in polyamine synthesis, is stimulated in intact mouse thyroid in vitro by TSH, dibutyryl cAMP, and cholera toxin by approximately 6-fold. The inclusion of adenosine (5 mM) or guanosine (5 mM) in the incubation medium totally abolished this stimulation of ODC, whereas inosine (5 mM) had no effect; this inhibition of ODC could not be explained by a general adenosine- or guanosine-induced inhibition of protein synthesis. In addition to the well characterized cAMP-dependent protein kinase (CNDPK) which uses ATP as a phosphate donor and histone as substrate, mouse thyroid also has a protein kinase that uses GTP as a phosphate donor (PK-G). The PK-G was not stimulated by cAMP, was not inhibited by the protein kinase-inhibitor, and was most active with casein. Adenosine inhibited CNDPK in a dose-related manner, with 50% inhibition at 250 μM, whereas guanosine or inosine had no effect even at 2.4 mM. However, PK-G was inhibited equally by adenosine o...