Regulation of Na,K-ATPase by cAMP-Dependent Protein Kinase Anchored on Membrane via A-Kinase Anchoring Protein Subtype, AKAP-150, in Rat Parotid Gland

2003 ◽  
Vol 986 (1) ◽  
pp. 636-638 ◽  
Author(s):  
K. KURIHARA ◽  
N. NAKANISHI
1988 ◽  
Vol 67 (2) ◽  
pp. 462-466 ◽  
Author(s):  
A.R. Shahed ◽  
D.W. Allmann

Stimulation of amylase secretion from parotid glands by beta-adrenergic agonists is mediated by the activation of adenylate cyclase and the resultant increase in cellular cAMP. Since NaF is known to increase adenylate cyclase activity and cAMP accumulation in intact cells, we investigated whether it would stimulate amylase secretion from isolated rat parotid gland cells. The results provide evidence that the addition of NaF (0.01 - 10 mmol/L) increased cAMP concentration (1.5-2.8-fold) in, and amylase secretion (16-93%) from, isolated parotid gland acinar cells. NaF was found to increase cAMP-dependent protein kinase activity ratios (51-84%) in a concentration-and time-dependent manner. The data suggest that the stimulation of amylase secretion from parotid gland cells by NaF may be mediated by an increase in the cellular cAMP concentration, which exerts its effect, at least in part, by increasing the activity of cAMP-dependent protein kinase.


2020 ◽  
Vol 92 (3) ◽  
Author(s):  
Nidia Carolina Moreno‐Corona ◽  
Orestes Lopez‐Ortega ◽  
Jose Mizael Flores Hermenegildo ◽  
Laura Berron‐Ruiz ◽  
Juan Carlos Rodriguez‐Alba ◽  
...  

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