scholarly journals Stimulatory effect of the intestinal peptide PHI on glycogenolysis and gluconeogenesis in isolated rat hepatocytes

1983 ◽  
Vol 214 (3) ◽  
pp. 999-1002 ◽  
Author(s):  
J E Felíu ◽  
J Marco
Keyword(s):  
Cyclic Amp ◽  
Pyruvate Kinase ◽  
Glycogen Phosphorylase ◽  
Rat Hepatocytes ◽  
Fold Increase ◽  
Isolated Rat Hepatocytes ◽  
Mediated Effects ◽  
Dose Dependent ◽  
Isolated Rat ◽  
Stimulation Of

The newly isolated peptide PHI provoked a dose-dependent stimulation of glycogenolysis and gluconeogenesis in isolated rat hepatocytes; at 1 microM-PHI, both processes were increased 1.6-fold as compared with basal values. These PHI-mediated effects were accompanied by the activation of glycogen phosphorylase and the inactivation of pyruvate kinase. PHI (1 microM) also caused a 2-fold increase in hepatocyte cyclic AMP.

scholarly journals Effect of adenosine and inosine on ureagenesis in hepatocytes

1987 ◽  
Vol 245 (2) ◽  
pp. 371-374 ◽  
Author(s):  
R Guinzberg P ◽  
I Laguna ◽  
A Zentella ◽  
R Guzman ◽  
E Piña
Keyword(s):  
Uric Acid ◽  
Rat Hepatocytes ◽  
Physiological Significance ◽  
Isolated Rat Hepatocytes ◽  
Dose Dependent ◽  
Isolated Rat ◽  
Stimulation Of

Adenosine and inosine produced a dose-dependent stimulation of ureagenesis in isolated rat hepatocytes. Hypoxanthine, xanthine and uric acid were without effect. Half-maximally effective concentrations were 0.08 microM for adenosine and 5 microM for inosine. Activation of ureagenesis by both nucleosides had the following characteristics: (a) it was observed with either glutamine or (NH4)2CO3, provided that glucose was present; (b) it was not detected when glucose was replaced by lactate plus oleate; (c) it was mutually antagonized by glucagon, but not by adrenaline; and (d) it was dependent on Ca2+. We suggest that the action of adenosine and inosine on ureagenesis might be of physiological significance.

scholarly journals Calcium rather than cyclic AMP is an intracellular messenger of parathyroid hormone action on glycogen metabolism in isolated rat hepatocytes

1989 ◽  
Vol 258 (3) ◽  
pp. 889-894 ◽  
Author(s):  
T Mine ◽  
I Kojima ◽  
E Ogata
Keyword(s):  
Parathyroid Hormone ◽  
Cyclic Amp ◽  
Glucose Production ◽  
Rat Hepatocytes ◽  
Free Calcium ◽  
Dependent Manner ◽  
Isolated Rat Hepatocytes ◽  
Glucose Output ◽  
Dose Dependent ◽  
Isolated Rat

The synthetic 1-34 fragment of human parathyroid hormone (1-34hPTH) stimulated glucose production in isolated rat hepatocytes. The effect of 1-34hPTH was dose-dependent and 10(10) M-1-34 hPTH elicited the maximum glucose output, which was approx. 80% of that by glucagon. Although 1-34hPTH induced a small increase in cyclic AMP production at concentrations higher than 10(-9) M, 10(-10) M-1-34hPTH induced the maximum glucose output without significant elevation of cyclic AMP. This is in contrast to the action of forskolin, which increased glucose output to the same extent as 10(-10) M-1-34hPTH by causing a 2-fold elevation of cyclic AMP. In addition to increasing cyclic AMP, 1-34hPTH caused an increase in cytoplasmic free calcium concentration ([Ca2+]c). When the effect of 1-34hPTH on [Ca2+]c was studied in aequorin-loaded cells, low concentrations of 1-34hPTH increased [Ca2+]c: the 1-34hPTH effect on [Ca2+]c was detected at as low as 10(-12) M and increased in a dose-dependent manner. 1-34hPTH increased [Ca2+]c even in the presence of 1 microM extracellular calcium, suggesting that PTH mobilizes calcium from an intracellular pool. In line with these observations, 1-34hPTH increased the production of inositol trisphosphate. These results suggest that: (1) PTH activates both cyclic AMP and calcium messenger systems and (2) PTH stimulates glycogenolysis mainly via the calcium messenger system.

scholarly journals Effects of phorbol esters on α1-adrenergic-mediated and glucagon-mediated actions in isolated rat hepatocytes

1985 ◽  
Vol 228 (1) ◽  
pp. 277-280 ◽  
Author(s):  
J A García-Sáinz ◽  
F Mendlovic ◽  
M A Martínez-Olmedo
Keyword(s):  
Cyclic Amp ◽  
Dose Response ◽  
Response Curve ◽  
Phorbol Esters ◽  
Rat Hepatocytes ◽  
Metabolic Effects ◽  
Isolated Rat Hepatocytes ◽  
The Right ◽  
Isolated Rat ◽  
Stimulation Of

Phorbol 12-myristate 13-acetate (PMA) inhibited the stimulation of ureogenesis produced by adrenaline, but produced a minimal displacement to the right of the dose-response curve for glucagon. However, PMA diminished the accumulation of cyclic AMP induced by glucagon. Dissociation between the cyclic AMP concentrations and the metabolic effects induced by glucagon is evidenced in the presence of phorbol esters.

scholarly journals P2-purinergic control of liver glycogenolysis

1985 ◽  
Vol 231 (3) ◽  
pp. 797-799 ◽  
Author(s):  
S Keppens ◽  
H De Wulf
Keyword(s):  
Cyclic Amp ◽  
Glycogen Phosphorylase ◽  
Purinergic Receptors ◽  
Rat Hepatocytes ◽  
Adrenergic Agonists ◽  
Isolated Rat Hepatocytes ◽  
P2 Purinergic Receptors ◽  
Heterologous Desensitization ◽  
Dose Dependent ◽  
Liver Glycogenolysis

Purinergic agonists cause a dose-dependent activation of glycogen phosphorylase in isolated rat hepatocytes. Half-maximally effective concentrations are 5 × 10(-7)M for ATP, 2 × 10(-6)M for ADP, and about 5 × 10(-5) M for AMP and adenosine. This potency series indicates the presence of P2-purinergic receptors. The mode of action of ATP appears to be identical with that of the Ca2+-dependent glycogenolytic hormones angiotensin, vasopressin and alpha 1-adrenergic agonists. (1) They all require Ca2+ for phosphorylase activation; (2) they do not increase cyclic AMP levels; (3) they are susceptible to heterologous desensitization by vasopressin and phenylephrine; (4) they lower cyclic AMP concentrations in hepatocytes stimulated by glucagon, most probably mediated by an enhanced phosphodiesterase activity.

scholarly journals Control of gluconeogenesis and of enzymes of glycogen metabolism in isolated rat hepatocytes. A parallel study of the effect of phenylephrine and of glucagon

1978 ◽  
Vol 176 (3) ◽  
pp. 791-797 ◽  
Author(s):  
Louis Hue ◽  
Juan Emilio Felíu ◽  
Henri-Géry Hers
Keyword(s):  
Protein Kinase ◽  
Pyruvate Kinase ◽  
Incubation Medium ◽  
Glycogen Phosphorylase ◽  
Glycogen Synthase ◽  
Rat Hepatocytes ◽  
Glycogen Metabolism ◽  
Parallel Study ◽  
Isolated Rat Hepatocytes ◽  
Isolated Rat

Hepatocytes isolated from the livers of fed rats were used for a comparative study of the effects of phenylephrine, vasopressin and glucagon on gluconeogenesis and on enzymes of glycogen metabolism. When hepatocytes were incubated in the presence of Ca2+, phenylephrine stimulated gluconeogenesis from pyruvate less than did glucagon, but, in contrast with this hormone, it did not affect the activities of protein kinase and pyruvate kinase, nor the concentration of phosphoenolpyruvate, and it did not decrease the release of 3H2O from [6-3H]glucose. The effects of vasopressin were similar to those of phenylephrine. Gluconeogenesis from fructose was also stimulated by phenylephrine and, more markedly, by glucagon at the expense of the conversion of fructose into lactate. Insulin was able to antagonize the stimulatory effect of phenylephrine on gluconeogenesis from pyruvate. When Ca2+ was removed from the incubation medium, phenylephrine still stimulated gluconeogenesis from pyruvate, but it also caused an activation of protein kinase and an inactivation of pyruvate kinase; accordingly, the concentration of phosphoenolpyruvate was increased, and, in contrast, vasopressin had no effect on all these parameters. The property of phenylephrine to cause the activation of glycogen phosphorylase was decreased by glucose or by the absence of Ca2+; it was abolished when these two conditions were combined. Glycogen synthase was inactivated by phenylephrine in the presence or the absence of Ca2+, although presumably by different mechanisms.

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