scholarly journals Acute α1-adrenergic stimulation of cardiac protein synthesis may involve increased intracellular pH and protein kinase activity

1991 ◽  
Vol 274 (3) ◽  
pp. 903-903
Keyword(s):  
Protein Synthesis ◽  
Protein Kinase ◽  
Intracellular Ph ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Adrenergic Stimulation ◽  
Stimulation Of

scholarly journals Acute α1-adrenergic stimulation of cardiac protein synthesis may involve increased intracellular pH and protein kinase activity

1991 ◽  
Vol 273 (2) ◽  
pp. 347-353 ◽  
Author(s):  
S J Fuller ◽  
C J Gaitanaki ◽  
R J Hatchett ◽  
P H Sugden
Keyword(s):  
Protein Synthesis ◽  
Protein Kinase ◽  
Intracellular Ph ◽  
Polynomial Regression ◽  
Kinase Inhibitor ◽  
Adenine Nucleotide ◽  
Protein Kinase Activity ◽  
Adrenergic Stimulation ◽  
Rat Cardiomyocytes ◽  
Stimulation Of

In the presence of 5 microM-DL-propranolol and in HCO3(-)-containing buffers, 1 microM-adrenaline acutely stimulated protein synthesis by about 25% in the anterogradely perfused rat heart. This stimulation was opposed by low (1-10 nM) concentrations of prazosin, but not by similar concentrations of yohimbine, suggesting involvement of the alpha 1-adrenoceptor. Under the same conditions, adrenaline raised intracellular pH (pHi) by about 0.1 unit. The increase in pHi induced by adrenaline was prevented by 5 nM-prazosin, but not by 5 nM-yohimbine, again suggesting involvement of the alpha 1-adrenoceptor. Since an increase in pHi stimulates protein synthesis in the heart [Sugden & Fuller (1991) Biochem. J. 273, 339-346], the increase in pHi induced by adrenaline may be involved in its stimulation of protein synthesis. Adrenaline also increased phosphocreatine concentrations. As discussed, the increase in pHi induced by adrenaline may be responsible for this effect. Using second-order polynomial regression analysis, we showed that rates of protein synthesis were significantly correlated (P less than 0.0001) with phosphocreatine concentrations. We discuss two possible reasons for this correlation: (i) increases in pHi stimulate protein synthesis and separately raise phosphocreatine concentrations, or (ii) the increase in protein synthesis rates is a consequence of the raised phosphocreatine concentrations induced by the increase in pHi. Rates of protein synthesis were not significantly correlated with ATP/ADP concentration ratios, nor with any of the following: ATP, ADP, AMP or total adenine nucleotide concentrations. In freshly isolated adult rat cardiomyocytes, the protein kinase inhibitor staurosporine (1 microM) prevented stimulation of protein synthesis by 0.3 microM-adrenaline (and by 1 microM-phorbol 12-myristate 13-acetate or 1 m-unit of insulin/ml). The results are discussed within a mechanistic framework initiated by stimulation of the hydrolysis of membrane phospholipids by alpha 1-adrenergic agonists.

β-Adrenergic stimulation of cyclic AMP and protein kinase activity in the thyroid

Nature ◽  
1975 ◽  
Vol 254 (5498) ◽  
pp. 347-349 ◽  
Author(s):  
STEPHEN W. SPAULDING ◽  
GERARD N. BURROW
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Adrenergic Stimulation ◽  
Stimulation Of

14-Deoxyandrographolide alleviates ethanol-induced hepatosteatosis through stimulation of AMP-activated protein kinase activity in rats

Alcohol ◽  
2014 ◽  
Vol 48 (2) ◽  
pp. 123-132 ◽  
Author(s):  
Samir Mandal ◽  
Sibabrata Mukhopadhyay ◽  
Sukdeb Bandhopadhyay ◽  
Gargi Sen ◽  
Tuli Biswas
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Amp Activated Protein Kinase ◽  
Stimulation Of

Effects of isoproterenol on cylic-AMP metabolism in rat ventral prostate

1976 ◽  
Vol 54 (3) ◽  
pp. 327-335 ◽  
Author(s):  
B. K. Tsang ◽  
R. L. Singhal
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Kinase Activity ◽  
Activity Ratio ◽  
Ventral Prostate ◽  
Adrenergic Stimulation ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Stimulation Of

β-Adrenergic stimulation of the ventral prostate cyclic-AMP system was investigated by examining the influence of isoproterenol on endogenous cyclic-AMP levels as well as on the activities of adenylate cyclase (EC 4.6.1.1) and cyclic-AMP-dependent and independent protein kinases (EC 2.7.1.37). Administration of isoproterenol (1 mg/kg, ip) resulted in rapid elevation of adenylate cyclase activity (119%) and cyclic-AMP levels (593%). The observed isoproterenol-stimulated changes in cyclic-AMP metabolism of the ventral prostate were time-dependent and maximal stimulation was seen 5 min after treatment with this β-adrenergic agonist. The increases in prostatic adenylate cyclase and cyclic-AMP also were related to the dose of isoproterenol administered and maximal enhancement of these parameters was seen with 1 mg/kg dose of the agonist. Whereas pretreatment of rats with propranolol (3 mg/kg, ip) partially reversed these alterations, administration of an α-adrenergic antagonist, phentolamine, even at a dose of 5 mg/kg, failed to elicit any appreciable effect. Stimulation of prostatic soluble protein kinase by isoproterenol was associated with a decrease (33%) in the activity of the cyclic-AMP-dependent protein kinase with a concomitant increase (25%) in that of the independent enzyme. Whereas the ability of the enzyme to bind cyclic-[3H] AMP in vitro was decreased (54%) following isoproterenol treatment, the protein kinase activity ratio (−cyclic-AMP/+cyclic-AMP) was significantly elevated from 0.51 ± 0.05 to 0.95 ± 0.08. Although propranolol alone had little or no effect on these parameters, it inhibited partially the isoproterenol-induced alterations in cyclic-AMP-dependent protein kinase and the cyclic-AMP binding capacity. Treatment with propranolol also blocked the increases in the kinase activity ratio and in the activity of cyclic-AMP-independent enzyme seen with isoproterenol. Data suggest that the concentration of ventral prostate cyclic-AMP as well as the activities of adenylate cyclase and cyclic-AMP-dependent and independent form of protein kinases are subject to modulation by β-adrenergic stimulation.

Phosphorylation of the salivary Na+-K+-2Cl− cotransporter

2002 ◽  
Vol 282 (4) ◽  
pp. C817-C823 ◽  
Author(s):  
Kinji Kurihara ◽  
Nobuo Nakanishi ◽  
Marilyn L. Moore-Hoon ◽  
R. James Turner
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Acinar Cells ◽  
Good Evidence ◽  
Protein Kinase Activity ◽  
Adrenergic Stimulation ◽  
Parotid Acinar Cells ◽  
Rat Parotid ◽  
Phosphopeptide Mapping ◽  
Kinase A

We studied the phosphorylation of the secretory Na+-K+-2Cl− cotransporter (NKCC1) in rat parotid acinar cells. We have previously shown that NKCC1 activity in these cells is dramatically upregulated in response to β-adrenergic stimulation and that this upregulation correlates with NKCC1 phosphorylation, possibly due to protein kinase A (PKA). We show here that when ATP is added to purified acinar basolateral membranes (BLM), NKCC1 is phosphorylated as a result of membrane-associated protein kinase activity. Additional NKCC1 phosphorylation is seen when PKA is added to BLMs, but our data indicate that this is due to an effect of PKA on endogenous membrane kinase or phosphatase activities, rather than its direct phosphorylation of NKCC1. Also, phosphopeptide mapping demonstrates that these phosphorylations do not take place at the site associated with the upregulation of NKCC1 by β-adrenergic stimulation. However, this upregulatory phosphorylation can be mimicked by the addition of cAMP to permeabilized acini, and this effect can be blocked by a specific PKA inhibitor. These latter results provide good evidence that PKA is indeed involved in the upregulatory phosphorylation of NKCC1 and suggest that an additional factor present in the acinar cell but absent from isolated membranes is required to bring about the phosphorylation.

scholarly journals Interleukin 1 and the glomerular mesangium. III. IL-1-dependent stimulation of mesangial cell protein kinase activity

1988 ◽  
Vol 34 (1) ◽  
pp. 26-35 ◽  
Author(s):  
David H. Lovett ◽  
Michael Martin ◽  
Stuart Bursten ◽  
Marta Szamel ◽  
Diethard Gemsa ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Mesangial Cell ◽  
Interleukin 1 ◽  
Cell Protein ◽  
Protein Kinase Activity ◽  
Glomerular Mesangium ◽  
Stimulation Of
Sign in / Sign up

Export Citation Format

Share Document