Protein kinase A-dependent phosphorylation modulation of cardiac sodium channel kinetics

1995 ◽  
Vol 28 (1) ◽  
pp. 73-74 ◽  
Keyword(s):  
Protein Kinase ◽  
Sodium Channel ◽  
Protein Kinase A ◽  
Channel Kinetics ◽  
Cardiac Sodium Channel ◽  
Kinase A

scholarly journals Modulation of Cardiac Sodium Channel Gating by Protein Kinase A Can Be Altered by Disease-linked Mutation

2003 ◽  
Vol 278 (47) ◽  
pp. 46718-46726 ◽  
Author(s):  
Michihiro Tateyama ◽  
Ilaria Rivolta ◽  
Colleen E. Clancy ◽  
Robert S. Kass
Keyword(s):  
Protein Kinase ◽  
Sodium Channel ◽  
Protein Kinase A ◽  
Channel Gating ◽  
Cardiac Sodium Channel ◽  
Kinase A

scholarly journals Activation of Protein Kinase A Modulates Trafficking of the Human Cardiac Sodium Channel in Xenopus Oocytes

2000 ◽  
Vol 87 (1) ◽  
pp. 33-38 ◽  
Author(s):  
Jingsong Zhou ◽  
Jianxun Yi ◽  
NingNing Hu ◽  
Alfred L. George ◽  
Katherine T. Murray
Keyword(s):  
Protein Kinase ◽  
Sodium Channel ◽  
Protein Kinase A ◽  
Xenopus Oocytes ◽  
Cardiac Sodium Channel ◽  
Kinase A

scholarly journals Intracellular Sodium Regulates Opioid Signalling in Peripheral Neurons

2017 ◽  
Author(s):  
Alexandros H. Kanellopoulos ◽  
Jing Zhao ◽  
Edward C. Emery ◽  
John N Wood
Keyword(s):  
Protein Kinase ◽  
Sodium Channel ◽  
Protein Kinase A ◽  
Fold Increase ◽  
Intracellular Sodium ◽  
Peripheral Neurons ◽  
Dependent Inhibition ◽  
Dose Dependent Inhibition ◽  
Kinase A

AbstractOpioid receptors signal more effectively in sensory neurons from pain-free mice lacking the voltagegated sodium channel Nav1.7. Type-A GPCRs are known to be regulated through a specific sodium binding site, the occupancy of which diminishes agonist binding. We have used an electrophysiological assay of Protein Kinase A activity to examine the role of intracellular sodium on opioid signalling. Phosphorylation of sodium channel Nav1.8 by activation of Protein Kinase A with db-cAMP is unaffected by altered intracellular sodium. By contrast, there is a dose-dependent inhibition of fentanyl action on Nav1.8 currents when intracellular sodium is increased from 0 mM to 20 mM. Fentanyl shows a 50% loss of activity and 80-fold increase in EC50 with 20 mM intracellular sodium. These data demonstrate that altered intracellular sodium levels modulate opioid receptor signalling.

Protein kinase A phosphorylation enhances sodium channel currents in Xenopus oocytes

1992 ◽  
Vol 263 (3) ◽  
pp. C660-C666 ◽  
Author(s):  
R. D. Smith ◽  
A. L. Goldin
Keyword(s):  
Protein Kinase ◽  
Sodium Channel ◽  
Protein Kinase A ◽  
Rat Brain ◽  
Xenopus Oocytes ◽  
Kinase Inhibitor ◽  
Sodium Current ◽  
Specific Inhibitor ◽  
Channel Currents ◽  
Kinase A

The voltage-sensitive rat brain sodium channel is known to be phosphorylated by adenosine 3',5'-cyclic monophosphate (cAMP)-dependent protein kinase A (PKA), but the functional significance of that phosphorylation is unknown. We have shown that rat brain sodium channel currents expressed in Xenopus oocytes were enhanced by induction of PKA activity. Stimulation of the beta 2-adrenergic receptor or treatment with dibutyryl cAMP resulted in increased sodium current amplitudes without affecting the voltage dependence of channel activation or inactivation. These increases were completely blocked by preinjection of protein kinase inhibitor, a specific inhibitor of PKA. Injection of phosphatase into the oocytes resulted in a significant decrease in sodium current amplitude, indicating that phosphorylation is important for basal levels of sodium channel activity in oocytes. The enhancement was specific for the rat brain IIA sodium channel, because currents expressed from the rat muscle microI sodium channel were not enhanced by the same procedures. These data demonstrate a modulatory role of PKA phosphorylation on brain sodium channel function and suggest a means by which the electrical excitability of cells may be regulated.

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