Calmodulin and a Cyclic Nucleotide-Dependent Protein Kinase Facilitate the Prolactin-Induced Increase in Tyrosine Hydroxylase Activity in Tuberoinfundibular Dopaminergic Neurons

Endocrine ◽  
2001 ◽  
Vol 16 (2) ◽  
pp. 105-112 ◽  
Author(s):  
Lydia A Arbogast
Keyword(s):  
Tyrosine Hydroxylase ◽  
Protein Kinase ◽  
Cyclic Nucleotide ◽  
Dopaminergic Neurons ◽  
Hydroxylase Activity ◽  
Dependent Protein Kinase ◽  
Tyrosine Hydroxylase Activity ◽  
Dependent Protein

scholarly journals Structural basis of cyclic nucleotide selectivity in cGMP dependent protein kinase II

2015 ◽  
Vol 16 (S1) ◽  
Author(s):  
James C. Campbell ◽  
Kevin Y. Li ◽  
Jeong Joo Kim ◽  
Gilbert Huang ◽  
Albert S. Reger ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cyclic Nucleotide ◽  
Structural Basis ◽  
Dependent Protein Kinase ◽  
Cgmp Dependent Protein Kinase ◽  
Protein Kinase Ii ◽  
Dependent Protein

PI3-kinase/Akt modulates vascular smooth muscle tone via cAMP signaling pathways

2001 ◽  
Vol 91 (4) ◽  
pp. 1819-1827 ◽  
Author(s):  
Padmini Komalavilas ◽  
Shyamal Mehta ◽  
Christopher J. Wingard ◽  
Daniel T. Dransfield ◽  
Jyoti Bhalla ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Vascular Smooth Muscle ◽  
Cyclic Nucleotide ◽  
Muscle Tone ◽  
Pi3 Kinase ◽  
Dependent Protein Kinase ◽  
Smooth Muscle Tone ◽  
Dependent Protein ◽  
Vascular Smooth Muscle Tone

Phosphatidylinositol 3-kinase (PI3-kinase) activates protein kinase B (also known as Akt), which phosphorylates and activates a cyclic nucleotide phosphodiesterase 3B. Increases in cyclic nucleotide concentrations inhibit agonist-induced contraction of vascular smooth muscle. Thus we hypothesized that the PI3-kinase/Akt pathway may regulate vascular smooth muscle tone. In unstimulated, intact bovine carotid artery smooth muscle, the basal phosphorylation of Akt was higher than that in cultured smooth muscle cells. The phosphorylation of Akt decreases in a time-dependent manner when incubated with the PI3-kinase inhibitor, LY-294002. Agonist (serotonin)-, phorbol ester (phorbol 12,13-dibutyrate; PDBu)-, and depolarization (KCl)-induced contractions of vascular smooth muscles were all inhibited in a dose-dependent fashion by LY-294002. However, LY-294002 did not inhibit serotonin- or PDBu-induced increases in myosin light chain phosphorylation or total O2 consumption, suggesting that inhibition of contraction was not mediated by reversal or inhibition of the pathways that lead to smooth muscle activation and contraction. Treatment of vascular smooth muscle with LY-294002 increased the activity of cAMP-dependent protein kinase and increased the phosphorylation of the cAMP-dependent protein kinase substrate heat shock protein 20 (HSP20). These data suggest that activation of the PI3-kinase/Akt pathway in unstimulated smooth muscle may modulate vascular smooth muscle tone (allow agonist-induced contraction) through inhibition of the cyclic nucleotide/HSP20 pathway and suggest that cyclic nucleotide-dependent inhibition of contraction is dissociated from the myosin light chain contractile regulatory pathways.

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