Characterization and relationship to exocrine secretion of rat parotid gland cyclic AMP-dependent protein kinase

1981 ◽  
Vol 26 (4) ◽  
pp. 333-337 ◽  
Author(s):  
B.J. Baum ◽  
F.T. Colpo ◽  
C.R. Filburn
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Parotid Gland ◽  
Exocrine Secretion ◽  
Dependent Protein Kinase ◽  
Rat Parotid Gland ◽  
Dependent Protein ◽  
Rat Parotid

Effect of NaF on cAMP Accumulation, cAMP-dependent Protein Kinase Activity in, and Amylase Secretion from, Rat Parotid Gland Cells

1988 ◽  
Vol 67 (2) ◽  
pp. 462-466 ◽  
Author(s):  
A.R. Shahed ◽  
D.W. Allmann
Keyword(s):  
Protein Kinase ◽  
Parotid Gland ◽  
Amylase Secretion ◽  
Protein Kinase Activity ◽  
Camp Concentration ◽  
Dependent Protein Kinase ◽  
Gland Cells ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Rat Parotid

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.

scholarly journals Co-ordinated changes in the cyclic AMP signalling system and the phosphorylation of two nuclear proteins of Mr 130,000 and 110,000 during proliferative stimulation of the rat parotid gland by isoprenaline. Possible identity of the two proteins with pp135 and nucleolin

1989 ◽  
Vol 263 (3) ◽  
pp. 785-793 ◽  
Author(s):  
J Hoffmann ◽  
G Schwoch
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Parotid Gland ◽  
Dna Synthesis ◽  
Beta Agonist ◽  
Nuclear Proteins ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
32P Incorporation ◽  
Stimulation Of

Parotid glands were stimulated to growth by repeated injection of the beta-agonist isoprenaline into rats. Incubation of intact parotid-gland lobules with [32P]Pi and subsequent analysis of nuclear proteins revealed in the stimulated glands an increased 32P incorporation into two acid-soluble non-histone proteins with apparent Mr values of 110,000 and 130,000 (p110 and p130). After a single injection of isoprenaline, leading to a biphasic increase in DNA synthesis (maximum at 24 h), the same two proteins showed a transiently increased 32P incorporation at 17 h after injection. At this time point at the onset of DNA synthesis the total activity of soluble cyclic AMP-dependent protein kinase decreased. No change in p110/p130 phosphorylation was observed at 0.3 h after stimulation, a time of maximal stimulation of secretion. Administration of the beta-antagonist propranolol 8 h after the injection of isoprenaline suppressed the increase in DNA synthesis, the preceding changes in the concentration of cyclic AMP and in the activity of cyclic AMP-dependent protein kinase, as well as the increased phosphorylation of p110 and p130. Cross-reactivity of p110 and p130 with specific antisera against two nucleolar phosphoproteins of similar molecular mass (nucleolin and pp135), as well as their localization in a nucleolar cell fraction, indicated a possible identity of p110 and p130 with these two proteins. Our results suggest that nucleolin and pp135 are nuclear target proteins of cyclic AMP in the cyclic AMP-influenced regulation of the transition of cells from the G1 to the S phase.

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