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

@article{Roskoski1987ActivationOT,
  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},
  year={1987},
  volume={48}
}
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
TLDR
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.
TLDR
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
TLDR
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.
TLDR
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
TLDR
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
TLDR
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
TLDR
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
TLDR
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.
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