Hormonal regulation of thyroidal protein phosphokinase activities. II. Differential sensitivity of type I and type II cAMP-dependent enzymes to the treatment of rats with thyroxine.
Two cAMP-dependent protein kinase activities can be separated from rat thyroid cytosol. Their elution properties during the gel chromatography, as well as their sedimentation coefficients after sucrose-gradient ultracentrifugation and their capacity to dissociate in the presence of histones, suggest they are like the Type I and Type II protein kinases described in many other tissues. The sensitivity of the two types of kinases to thyroxine treatment is different. The activity of Type I is not changed during the first 5 days of treatment. Thereafter, it decreased by about 50% and is maintained at that level for up to one month. The activity of the Type II enzyme decreased rapidly by about 30-40% already on the second day of treatment, and after 10 days it reached 50% of the initial level. This differential reactivity of the two types of enzymes to the thyroxine treatment leads to profound modifications in their relative activities between the second and the fifth day of treatment. The significance of these results and the possible role of the two types of kinases in the control of different steps of iodine metabolism have been discussed.
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D000242:Cyclic AMP / Q000494:pharmacology*; D003600:Cytosol / Q000201:enzymology; D004789:Enzyme Activation; D008297:Male; D006656:Protamine Kinase / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D013961:Thyroid Gland / Q000201:enzymology*; D013974:Thyroxine / Q000494:pharmacology*; D014461:Ultracentrifugation
D000242:Cyclic AMP; D011494:Protein Kinases; D006656:Protamine Kinase; D013974:Thyroxine