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. 1978;42(2):139-44.
doi: 10.1007/BF01675352.

Activation of rat pheochromocytoma tyrosine hydroxylase by a cyclic AMP-dependent protein kinase in a cell-free system

G S Drummond, E Symchowicz, M Goldstein, L Shenkman

Activation of rat pheochromocytoma tyrosine hydroxylase by a cyclic AMP-dependent protein kinase in a cell-free system

G S Drummond et al. J Neural Transm. 1978.

Abstract

Short term exposure of PC-12 cells to dibutyryl cyclic AMP (dB-cAMP) results in an activation of tyrosine hydroxylase. In the cell-free system the PC-12 tyrosine hydroxylase activity is stimulated by addition of c-AMP, Mg+2 and ATP. Exogenous c-AMP dependent protein kinase further stumulates tyrosine hydroxylase activity. The kinetic data suggests that the PC-12 tyrosine hydroxylase in the basal state is in a non-phosphorylated form but under phosphorylating conditions the enzyme is activated and its kinetics properties are altered.

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