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.

scholarly journals The polyamine-dependent modulation of phenylalanine hydroxylase phosphorylation state and enzymic activity in isolated liver cells

1986 ◽  
Vol 237 (1) ◽  
pp. 277-279 ◽  
Author(s):  
M J Fisher ◽  
A J Dickson ◽  
C I Pogson
Keyword(s):  
Protein Phosphatase ◽  
Phenylalanine Hydroxylase ◽  
Liver Cells ◽  
Enzymic Activity ◽  
Phosphorylation State ◽  
Isolated Liver Cells ◽  
Phosphatase 2A ◽  
Pre Treatment ◽  
Isolated Liver

The role of polyamines in the control of phenylalanine hydroxylase phosphorylation state and enzymic activity was investigated. Pre-treatment of liver cells with spermine (1 mM) abolishes the glucagon (1 nM)-stimulated increase in hydroxylase phosphorylation. Concurrently there is a decrease in phenylalanine hydroxylation flux, reflecting decreased enzyme activity; 50% inhibition occurs at approx. 10 microM-spermine. These results are discussed in the context of reports concerning the properties of protein phosphatase 2A.

scholarly journals Effect of treatment in vivo of rats with bacterial endotoxin on fructose 2,6-bisphosphate metabolism and L-pyruvate kinase activity and flux in isolated liver cells

1992 ◽  
Vol 284 (3) ◽  
pp. 761-766 ◽  
Author(s):  
E D Ceppi ◽  
R G Knowles ◽  
K M Carpenter ◽  
M A Titheradge
Keyword(s):  
Pyruvate Kinase ◽  
Intact Cell ◽  
Total Activity ◽  
Liver Cells ◽  
Bacterial Endotoxin ◽  
Phosphorylation State ◽  
Isolated Liver Cells ◽  
Effect Of Treatment ◽  
Isolated Liver ◽  
Stimulation Of

The effect of treatment of rats with bacterial endotoxin on fructose 2,6-bisphosphate (Fru-2,6-P2) metabolism was investigated in isolated liver cells prepared from 18 h-starved animals. The results obtained support the hypothesis that a stimulation of 6-phosphofructo-1-kinase (PFK-1) activity and an inhibition of fructose-1,6-bisphosphatase (Fru-1,6-P2ase) may be one mechanism underlying the inhibition of gluconeogenesis from lactate and pyruvate by endotoxin. We suggest that the stimulation of PFK-1 and inhibition of Fru-1,6-P2ase activity is the result of a 2-3-fold increase in Fru-2,6-P2. The latter is not due to changes in the total activity or phosphorylation state of the bifunctional 6-phosphofructo-2-kinase (PFK-2)/fructose-2,6-bisphosphatase, but appears to be the result of a decrease in the cytosolic concentration of phosphoenolpyruvate (PEP), an inhibitor of PFK-2 activity. The effect of endotoxin is resistant to the presence of glucagon, which has comparable effects in cells prepared from both control and endotoxin-treated animals. The mechanism by which endotoxin treatment of the rat decreases PEP and gluconeogenesis remains to be established. However, it does not involve alterations in either the total activity or the phosphorylation state of pyruvate kinase, nor does it involve increased flux through this enzyme in the intact cell, which is in fact decreased in this model of septic shock. It is suggested that the decreased flux may result from a lower rate of formation of PEP, suggesting that the prime lesion in sepsis is an inhibition of one or more of the steps leading to PEP formation.

Decreased glucagon-stimulated cyclic AMP production by isolated liver cells of rats with type 2 diabetes

1983 ◽  
Vol 32 (1) ◽  
pp. 13-26 ◽  
Author(s):  
Bernard Portha ◽  
Hilda Chamras ◽  
Yvonne Broer ◽  
Luc Picon ◽  
Gabriel Rosselin
Keyword(s):  
Type 2 Diabetes ◽  
Cyclic Amp ◽  
Liver Cells ◽  
Isolated Liver Cells ◽  
Isolated Liver

scholarly journals The role of haem in the regulation of rat liver tryptophan metabolism

1986 ◽  
Vol 240 (1) ◽  
pp. 259-263 ◽  
Author(s):  
M Salter ◽  
C I Pogson
Keyword(s):  
Rat Liver ◽  
Intraperitoneal Injection ◽  
Liver Cells ◽  
Tryptophan Metabolism ◽  
Isolated Liver Cells ◽  
Tryptophan Oxidation ◽  
Isolated Liver

At saturating concentrations of tryptophan, the activity of tryptophan 2,3-dioxygenase was the same in isolated liver cells and in extracts with added haematin. Intraperitoneal injection of haematin did not increase tryptophan oxidation in livers subsequently perfused in situ. Preincubation of liver cells with physiological concentrations of tryptophan caused maximal saturation of tryptophan 2,3-dioxygenase with haem in liver cells. In cell-free extracts tryptophan 2,3-dioxygenase exhibited complex kinetics with haem. The results have important implications for the understanding of the role of haem in tryptophan metabolism.

scholarly journals The effect of experimental diabetes on phenylalanine metabolism in isolated liver cells

1985 ◽  
Vol 227 (1) ◽  
pp. 169-175 ◽  
Author(s):  
M A Santana ◽  
M J Fisher ◽  
A J Bate ◽  
C I Pogson
Keyword(s):  
Enzyme Activity ◽  
Hormonal Regulation ◽  
Metabolic Flux ◽  
Phenylalanine Hydroxylase ◽  
Experimental Diabetes ◽  
Liver Cells ◽  
Enzyme Protein ◽  
Isolated Liver Cells ◽  
Phenylalanine Metabolism ◽  
Isolated Liver

Chronic (10-day) diabetes was associated with increased metabolic flux through phenylalanine hydroxylase in isolated liver cells. This flux was stimulated by 0.1 microM-glucagon, but not by 10 microM-noradrenaline; 0.1 microM-insulin affected neither basal nor glucagon-stimulated flux. The increased rate of phenylalanine hydroxylation in diabetes was accompanied by parallel increases in enzyme activity (as measured with artificial cofactor) and immunoreactive-enzyme-protein content. In contrast with total protein synthesis, which decreased, phenylalanine hydroxylase synthesis persisted at the control rate in cells from diabetic animals. These findings are discussed in relation to the hormonal regulation of the hydroxylase and the known metabolic consequences of chronic diabetes.

scholarly journals Acceleration of gluconeogenesis from lactate by lysine (Short Communication)

1973 ◽  
Vol 134 (2) ◽  
pp. 671-672 ◽  
Author(s):  
Neal W. Cornell ◽  
Patricia Lund ◽  
Reginald Hems ◽  
Hans A. Krebs
Keyword(s):  
Amino Acid ◽  
Cyclic Amp ◽  
Short Communication ◽  
Liver Cells ◽  
Dibutyryl Cyclic Amp ◽  
Isolated Liver Cells ◽  
Isolated Liver

l-Lysine (2mm) causes an increase (mean 60%) in the rate of gluconeogenesis from lactate in isolated liver cells. The effect is of a catalytic nature. No other amino acid has the same effect, though ornithine is slightly active. The effect is additional to the stimulatory effects of oleate and of dibutyryl cyclic AMP.

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