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Activity and sub cellular distribution of protein kinase dependent on cyclic amp in liver from normal and adrenalectomized rats

, : Activity and sub cellular distribution of protein kinase dependent on cyclic amp in liver from normal and adrenalectomized rats. European Journal of Biochemistry 66(3): 499-506

Whether glucocorticoids control the activity and (or) the subcellular distribution of protein kinase dependent on cyclic[c]AMP was examined, since they influence cAMP-dependent responses to other hormones. Protein kinase activity was determined in rat liver homogenates and subcellular fractions, nuclear, large granular, microsomal and supernatant obtained by differential sedimentation in 0.25 M sucrose. Of the tissue protein kinase activity, 63% was detected in absence of cAMP reside in the particulate fractions. Upon addition of exogenous cAMP, protein kinase activity is stimulated 1.8, 1.2, 1.2 and 4.5-fold in nuclear, large granular, microsomal and supernatant fractions, respectively. Under these conditions, 66% of tissue activity is found in the supernatant fraction. The activity sensitive to exogenous cAMP resolves into a major (84%) cytosoluble and a minor (16%) nucleomicrosomal component. The latter activity resists elution with isotonic saline and is increased in the presence of Triton X-100. Three groups of rats were studied: control and adrenalectomized with or without cortisol treatment. In whole liver homogenates, protein kinase activity detected in absence of exogenous cAMP and sensitivity of the enzyme to cAMP were comparable in all groups. The distribution patterns of protein kinase activity among the fractions were essentially the same in all groups of animals, whether or not particles had been treated with Triton X-100. In cell-free experiments, glucocorticoids alone or in combination with their intracellular receptor did not modify protein kinase activity of rat liver. These results do not support the possibility that glucocorticoids influence cAMP-dependent protein kinase in rat liver. This study provides data, not available before, on subcellular distribution of this enzyme in rat liver.


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