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M Balage

Publications and source records attributed to M Balage.

27 records · Page 2Linked to original sources
PubMed1986

Effect of dietary protein level on the first steps of glucagon action in rat liver plasma membranes.

Binding of glucagon and glucagon-stimulated cyclic AMP production were studied in highly purified liver plasma membranes from growing rats fed a 12% protein diet (group 1) or 20% protein diet; this latter was given either in normal (group 2) or restricted (group 3) amounts. Groups 2 and 3 exhibited significantly higher peripheral glucagonemia than group 1 (amounting to 286 and 160% of group 1, respectively). Specific [125I]iodoglucagon binding to plasma membranes was similar in all groups. Scatchard analysis revealed no further differences between affinity constants and binding capacities in the three groups. Hormone degradation was constant. As membrane recovery and membrane purity were unaltered, these results suggest that hyperglucagonemia caused by increasing dietary protein level is not associated with any significant modification of glucagon binding sites in rat liver. In the presence of a potent phosphodiesterase inhibitor (3-isobutyl-1-methyl xanthine 0.2 mM) the glucagon-stimulated cyclic AMP production was higher in rats fed the 20% protein diet, which was given in normal amounts, than in rats fed the 12% protein diet. In contrast when the 20% protein diet was given in restricted amounts the glucagon-stimulated cyclic AMP production was similar to that in the 12% protein-fed rats.

Animals↗
PubMed1986

[Hormonal control of hepatic metabolism in ruminants].

Insulin/glucagon control of hepatic metabolism, i.e. a endocrine-nervous system, is one of the general systems of integration in vertebrates. In this system, substrates coming from the digestive tract or from extrahepatic metabolism are important messenger molecules. Liver uptake of insulin and glucagon mainly accounts for high metabolic clearance rates of these hormones in both ruminants and non-ruminants. Glucagon infusion into ruminants results in an increase in the net hepatic uptake of glucose precursors and gluconeogenesis. Glucagon effects have also been demonstrated in isolated hepatocytes. Glucagon, through its effect on pyruvate carboxylase (EC 6.4.1.1.) may regulate gluconeogenesis. Insulin infusion induces hypoglycaemia. As a result, glucagon secretion increases and counterregulates insulin action. However, it has been shown that hepatic gluconeogenesis decreases during euglycaemic hyperinsulin clamp, mainly due to a decrease in the hepatic supply of glucose precursors following insulin action in extrahepatic tissues. Insulin fails to elicit any significant effect in vitro. Hepatocytes exhibit insulin and glucagon receptors. The apparent characteristics of hormone binding in vitro are similar in ruminants and non-ruminants, but the characteristics of postreceptor events are unknown in the former. Glucagon, which influences hepatic glucose synthesis, may be a major hormone in ruminants.

Amino Acids↗
PubMed1984

Glucagon kinetics in growing rats fed different levels of protein and/or energy.

The present work was carried out to evaluate the kinetic parameters of glucagon in growing rats divided into three groups: T, H and E. Group T (Control group) was fed a control diet (crude protein: 11.8%). Groups H and E received a high protein diet (crude protein: 19%) distributed in either equal (Group H) or restricted amounts (Group E) with respect to the control. Thus, the main characteristic of Group H was the high level of protein intake (+ 68%) when Group E rats underwent a moderate increase in protein intake but a striking caloric deprivation (-25%). In all cases, the animals were fed a meal every 4 hours. The kinetic parameters of glucagon metabolism were estimated from the plasma disappearance curves of 125I-glucagon for five minutes following a pulse injection of purified 125I-glucagon (1 muCi, about 3.8 ng/100 g BW). Plasma 125I-glucagon was measured after gel filtration of plasma on Biogel P-10. Tissue radioactivity (mainly liver and kidneys) was recorded seven minutes after 125I-glucagon injection. The results showed that the plasma 125I-glucagon level was higher in Group H than in the other groups 1 min after the injection. At all other times (2, 3.5 and 5 min) it was similar in all groups. 125I-glucagon was rapidly cleared from plasma and rapidly taken up by the liver and kidneys. In the 3 experimental groups, mean half-life and metabolic clearance rate were estimated to be 2 min and 6 ml/min/100 g BW, respectively. Excess protein intake resulted in a reduction in the apparent initial distribution volume of 125I-glucagon without modifying significantly its turn-over rate and metabolic clearance rate. Kidneys and liver (6% BW) accounted for about 20% of the 125I-glucagon uptake by tissues 7 min after injection. Group H kidneys and liver were more labelled than in other groups. These results suggest that increased protein intake (without further caloric deprivation) can induce some changes in glucagon metabolism which could partially contribute to the increase in glucagonemia usually observed in animals fed high protein diets.

Animals↗
PubMed1983

Glucagon binding to purified liver plasma membranes from growing rats undergoing energy restriction.

The purpose of this work was to investigate liver glucagon receptors in growing rats fed a control diet (11.8% crude protein) or a high-protein diet (19.8% crude protein) given in restricted amounts. The animals were fed every 4 hours. 125I-glucagon binding to purified liver plasma membranes was studied. Membrane purity was analysed with marker enzymes. The alteration of glucagon during incubation was measured. The results show that specific 125I-glucagon binding increased with time at 30 degrees C, reaching a maximal value within 120 min. The increasing level of unlabelled glucagon inhibited 125I-glucagon binding at steady state. Apparent specific 125I-glucagon binding at steady state was lower in experimental animals than in controls. This correlated with the increase in glucagon breakdown and decrease in membrane purity. Alternatively, glucagon binding to its receptors could drop. Unlabelled glucagon excess produced a time-dependent dissociation of glucagon-receptor complexes (half-life: up to 1 h). Feeding the experimental diet increased the dissociation of labelled glucagon-receptor complexes.

Animals↗
PubMedDate not supplied

Metabolic clearance of insulin from the cerebrospinal fluid in the anesthetized rat.

Infusion of 125I-(Tyr A14)-insulin at tracer doses into the cerebrospinal fluid (CSF) resulted in a slow rate of increase in the CSF-labeled insulin during the first 2 hours with a plateau thereafter. Labeled insulin was cleared from the CSF at a higher rate than 3H-inulin, a marker of CSF bulk flow. The labeled insulin was mainly distributed in all the ventricular and periventricular brain regions. Small amounts of degraded insulin appeared in the CSF. Coinfusion with an excess of unlabeled insulin impaired the clearance and degradation of labeled insulin. It also inhibited the labeling in medial hypothalamus, olfactory bulbs and brain stem. In contrast, coinfusion of ribonuclease B (used to test the specificity of uptake) was without any effect. It was concluded that there is an active insulin intake from CSF into brain specific compartments that is presumably essential for the effects of insulin on brain function.

Anesthesia↗
PubMedDate not supplied

Insulin action on skeletal muscle protein metabolism during catabolic states.

Insulin plays a major role in the regulation of skeletal muscle protein turnover but its mechanism of action is not fully understood, especially in vivo during catabolic states. These aspects are presently reviewed. Insulin inhibits the ATP-ubiquitin proteasome proteolytic pathway which is presumably the predominant pathway involved in the breakdown of muscle protein. Evidence of the ability of insulin to stimulate muscle protein synthesis in vivo was also presented. Many catabolic states in rats, e.g. streptozotocin diabetes, glucocorticoid excess or sepsis-induced cytokines, resulted in a decrease in insulin action on protein synthesis or degradation. The effect of catabolic factors would therefore be facilitated. In contrast, the antiproteolytic action of insulin was improved during hyperthyroidism in man and early lactation in goats. Excessive muscle protein breakdown should therefore be prevented. In other words, the anabolic hormone insulin partly controlled the 'catabolic drive'. Advances in the understanding of insulin signalling pathways and targets should provide information on the interactions between insulin action, muscle protein turnover and catabolic factors.

Animals↗