Effects of db cAMP on tyrosine hydroxylase activity of ganglia and nerve endings

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Abstract
Preincubation of intact superior cervical ganglia or nictitating membrane for 2 h with dibutyryl cyclic AMP (db cAMP) increased the hydroxylation of tyrosine. This effect was not blocked by the protein synthesis inhibitor, cycloheximide. The K m of tyrosine hydroxylase for the substrate, tyrosine, and for the cofactor, reduced pteridine, were decreased by db cAMP. There were no changes in the V max of the enzyme. The inhibitory potency of noradrenaline on the hydroxylation of tyrosine was also decreased. Thus an inductive effect may be ruled out. The activation of the enzyme was only observed when the tissues were preincubated with the db cAMP and not when the cyclic nucleotide was added to the isolated enzyme. Preincubation of cervical ganglia for 4 h with db cAMP increased activity of decarboxylase and monoamine oxidase in tissue homogenates without changing the tyrosine hydroxylase activity.