The Role of Calcium and Cyclic AMP in PKD

2015 ◽  
pp. 169-196 ◽  
Author(s):  
James P. Calvet ◽  
Keyword(s):  
Cyclic Amp

scholarly journals Role of cyclic AMP in the control of cell-specific gene expression

1993 ◽  
Vol 4 (6) ◽  
pp. 204-209 ◽  
Author(s):  
Wolfgang Schmid ◽  
Doris Nitsch ◽  
Michael Boshart ◽  
Günther Schütz
Keyword(s):  
Gene Expression ◽  
Cyclic Amp ◽  
Specific Gene ◽  
Specific Gene Expression

scholarly journals Regulation of the expression of the mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase gene. Its role in the control of ketogenesis

1992 ◽  
Vol 283 (1) ◽  
pp. 261-264 ◽  
Author(s):  
N Casals ◽  
N Roca ◽  
M Guerrero ◽  
G Gil-Gómez ◽  
J Ayté ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Rat Liver ◽  
Genetic Expression ◽  
Fat Feeding

We have explored the role of mitochondrial 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase in regulating ketogenesis. We had previously cloned the cDNA for mitochondrial HMG-CoA synthase and have now studied the regulation in vivo of the expression of this gene in rat liver. The amount of processed mitochondrial HMG-CoA synthase mRNA is rapidly changed in response to cyclic AMP, insulin, dexamethasone and refeeding, and is greatly increased by starvation, fat feeding and diabetes. We conclude that one point of ketogenic control is exercised at the level of genetic expression of mitochondrial HMG-CoA synthase.

scholarly journals Heterologous desensitization of the cyclic AMP-independent glycogenolytic response in rat liver cells

1981 ◽  
Vol 200 (3) ◽  
pp. 509-514 ◽  
Author(s):  
B Bréant ◽  
S Keppens ◽  
H De Wulf
Keyword(s):  
Cyclic Amp ◽  
Glycogen Phosphorylase ◽  
Liver Glycogen ◽  
Receptor Interaction ◽  
Alpha Adrenergic Receptors ◽  
Rat Liver Cells ◽  
Heterologous Desensitization ◽  
Highly Correlated ◽  
Alpha Agonist

Vasopressin and alpha-adrenergic agonists are known to be potent cyclic AMP-independent Ca2+-dependent activators of liver glycogen phosphorylase. When hepatocytes are pre-incubated with increasing concentrations of vasopressin or of the alpha-agonist phenylephrine, they become progressively unresponsive to a second addition of the respective agonist. The relative abilities of six vasopressin analogues and of five alpha-agonists to activate glycogen phosphorylase and to cause subsequent desensitization are highly correlated, indicating that the same vasopressin and alpha-adrenergic receptors are involved in both responses. About 5-times-higher peptide concentrations are needed to desensitize the cells than to activate their glycogen phosphorylase, whereas the concentrations of alpha-agonists required for the desensitization are only twice those needed for the activation of phosphorylase. The desensitization is not mediated by a perturbation in the agonist-receptor interaction. It is clearly heterologous, i.e. it is not agonist-specific, and must therefore involve a mechanism common to both series of agonists. The evidence for a role of Ca2+ movements or phosphatidylinositol turnover is briefly discussed.

The role of cyclic AMP in canine secretin-stimulated bile flow

1979 ◽  
Vol 27 (1) ◽  
pp. 57-61 ◽  
Author(s):  
D.L. Kaminski ◽  
M.J. Ruwart ◽  
Y.G. Deshpande
Keyword(s):  
Cyclic Amp ◽  
Bile Flow

scholarly journals The role of insulin in the modulation of glucagon-dependent control of phenylalanine hydroxylation in isolated liver cells

1987 ◽  
Vol 242 (3) ◽  
pp. 655-660 ◽  
Author(s):  
M J Fisher ◽  
A J Dickson ◽  
C I Pogson
Keyword(s):  
Cyclic Amp ◽  
Insulin Action ◽  
Phenylalanine Hydroxylase ◽  
Liver Cells ◽  
Phosphorylation State ◽  
Isolated Liver Cells ◽  
The Impact ◽  
Isolated Liver ◽  
Stimulation Of

The stimulation of phenylalanine hydroxylation in isolated liver cells by sub-maximally effective concentrations of glucagon (less than 0.1 microM) is antagonized by insulin (0.1 nM-0.1 microM). This phenomenon is a consequence of a decrease in the glucagon-stimulated phosphorylation of phenylalanine hydroxylase from liver cells incubated in the presence of insulin. The impact of insulin on the phosphorylation state and activity of the hydroxylase is mimicked by incubation of liver cells in the presence of orthovanadate (10 microM). A series of cyclic AMP and cyclic GMP analogues enhanced phenylalanine hydroxylation: in each case insulin diminished the stimulation of flux. These results are discussed in the light of the characteristics of insulin action on other metabolic processes.

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