Activation of Tyrosine Hydroxylase in PC12 Cells by the Cyclic GMP and Cyclic AMP Second Messenger Systems

  title={Activation of Tyrosine Hydroxylase in PC12 Cells by the Cyclic GMP and Cyclic AMP Second Messenger Systems},
  author={Robert Roskoski and Laura M. Roskoski},
  journal={Journal of Neurochemistry},
Tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis, is subject to regulation by a variety of agents. [] Key Result We found that treatment of rat PC12 cells with sodium nitroprusside (an activator of guanylate cyclase), 8-bromocyclic GMP, forskolin (an activator of adenylate cyclase), and 8-bromocyclic AMP all produced an increase in tyrosine hydroxylase activity measured in vitro or an increased conversion of [14C]tyrosine to labeled catecholamine in situ.
Adenosine Receptor Activation and the Regulation of Tyrosine Hydroxylase Activity in PC 12 and PC 18 Cells
It is concluded that both cell types generated adenine nucleotides which activate the adenosine receptor in an autocrine or paracrine fashion, and that PC12 cells released ATP in a calcium‐dependent process in response to activation of the nicotinic receptor.
Phosphorylation of tyrosine hydroxylase by cGMP-dependent protein kinase in intact bovine chromaffin cells.
Experiments performed with a cGMP-dependent protein kinase inhibitor, the Rp-isomer of 8-(4-chlorophenylthio)-cyclic guanosine monophosphorothioate, demonstrated that the phosphorylation increases evoked by both compounds were mediated by the activation of cG MP-dependentprotein kinase.
In Vitro Phosphorylation of Bovine Adrenal Chromaffin Cell Tyrosine Hydroxylase by Endogenous Protein Kinases
Abstract: Under phosphorylating conditions, addition of Ca2+ or cyclic AMP to the 100,000 g supernatant of purified bovine adrenal chromaffin cells increases both the incorporation of 32P into
Protein kinase A and nicotinic activation of bovine adrenal tyrosine hydroxylase
The results indicate that both basal TOH activity and nicotinic activation of TOH in bovine chromaffin cells require protein kinase A activity, and it is unlikely that nicotinics activation of ToH is directly mediated by an activation of protein kinases A in response to elevated cyclic AMP levels.
Regulation of tyrosine hydroxylase activity in rat PC12 cells by neuropeptides of the secretin family.
It is suggested that the PC12 cells contain a secretin-preferring receptor that increases cAMP levels and brings about an activation of tyrosine hydroxylase activity through the stimulation of cAMP-dependent protein kinase.
Inactivation of Tyrosine Hydroxylase Activity by Ascorbate In Vitro and in Rat PC12 Cells
It is reported here that ascorbate is one agent that inactivates striatal tyrosine hydroxylase activity with an EC50 of 5.9 μM under phosphorylating conditions, and the inactivation seen under in vitro conditions appears to have a counterpart under more physiological conditions.
Intricate Regulation of Tyrosine Hydroxylase Activity and Gene Expression
Regulatory mechanisms provide not only redundancy but also diversity in the control of catecholamine biosynthesis.
Gene Regulation of Catecholamine Biosynthetic Enzymes by Nitric Oxide in PC12 Cells
Treatment of PC12 cells with the NO donor, sodium nitroprusside (SNP) for 6 hours significantly increased TH, DBH and PNMT mRNA levels and supported a contributing role of PKA, PKC and PKG in SNP-mediated induction for all three CA genes.
Tryptophan Hydroxylase Is Phosphorylated by Protein Kinase A
Results indicate that tryptophan hydroxylase is phosphorylated by protein kinase A in brain and question whether thisprotein kinase exerts direct regulatory influence over tryptophile hydroxolase activity via phosphorylation.


Tyrosine Hydroxylase Activation and Inactivation by Protein Phosphorylation Conditions
It appears that the activation‐inactivation process is not mediated solely by the modulation of enzyme feedback inhibition or changes in the Km, for 6‐MPH4, and to demonstrate that inactivation is not associated with proteolytic degradation or irreversible de‐naturation, the inactivated form of the enzyme can be reactivated.
Tyrosine Hydroxylase Inactivation Following cAMP‐Dependent Phosphorylation Activation
Following its phosphorylation activation in rat striatal homogenates, it is found that tyrosine hydroxylase is inactivated by two distinct processes: in the first case, reversible phosphorylaton and dephos‐phorylation and, in the second case, an irreversible loss of activity of the phosphorylated form of tyrosin hydroxyase.
Adenosine-dependent activation of tyrosine hydroxylase is defective in adenosine kinase-deficient PC12 cells.
  • R. Erny, J. Wagner
  • Biology, Computer Science
    Proceedings of the National Academy of Sciences of the United States of America
  • 1984
Genetic evidence is provided that adenosine-dependent activation of TyrOHase is mediated by acute increases in cAMP, which might function as either a presynaptic or a postsynaptic receptor that regulates rates of transmitter synthesis in response to cell activity.
Calcium/phospholipid-dependent protein kinase (protein kinase C) phosphorylates and activates tyrosine hydroxylase.
Two-dimensional phosphopeptide maps of tyrosine hydroxylase were identical whether the phosphorylation was catalyzed by protein kinase C or by the catalytic subunit of cAMP-dependentprotein kinase.
Relationship between activation and phosphorylation of tyrosine hydroxylase by 56 mm K+ in PC12 cells in culture.
The results suggest that, although there is a relationship between activation and phosphorylation of tyrosine hydroxylase after potassium-evoked depolarization of rat pheochromocytoma PC12 cells in culture, this relationship may be complex.
Distribution of cyclic-GMP-dependent protein kinase in various rat tissues and cell lines determined by a sensitive and specific radioimmunoassay.
  • U. Walter
  • Biology, Chemistry
    European journal of biochemistry
  • 1981
The results suggest thatcyclic-GMP-dependent protein kinase is ubiquitously distributed although its level varies significantly from tissue to tissue and cell type to type, and support the hypothesis that cyclic- GMP- dependent protein kinases is involved in mediating some of the intracellular effects of those hormones, neurotransmitters and drugs which regulate the intrACEllular level of cyclic GMP.
Regulation of the concentration of adenosine 3',5'-cyclic monophosphate and the activity of tyrosine hydroxylase in the rat superior cervical ganglion by three neuropeptides of the secretin family
  • N. Ip, C. Baldwin, R. Zigmond
  • Biology, Chemistry
    The Journal of neuroscience : the official journal of the Society for Neuroscience
  • 1985
A strong correlation was found between the cAMP level and the TH activity in individual ganglia exposed to these peptides, and 8-bromoadenosine 3′,5′-cyclic monophosphate and forskolin also increased TH activity.