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PubMed1989

Effect of cyclosporin A on carbohydrate metabolism in the rat.

Liver and kidney carbohydrate metabolism was investigated in rats treated with daily doses of 15 mg/kg body weight cyclosporin A (CyA) for 2 and 8 weeks or of 50 mg/kg body weight CyA for 2 weeks. The higher dosage caused significantly reduced liver glycogen and liver glycogen synthetase activity (of both active I-form and total enzyme activity), whereas the activity of the glycogen-degrading enzyme phosphorylase (active a-form and total activity) remained unchanged. Plasma glucose and glucagon levels, as well as blood ketone bodies of these animals, increased significantly and plasma insulin decreased. In contrast, kidney glycogen and glucose content were higher in rats treated with 50 mg CyA, probably due to enhanced ketone body utilization. Reduced liver glycogen synthetase activity was also found in rats treated with 15 mg CyA. Our data suggest that hypoinsulinemia, induced by CyA, might be a contributing factor to the hyperglycemia, which is mainly due to inhibition of liver glycogen synthesis.

Animals↗
PubMedDate not supplied

Normal values of glycogen content in the dog skeletal muscle and liver.

Glycogen content was measured in the dog quadriceps femoris muscle and liver tissue under resting conditions after 24 h fasting period, using small tissue samples taken by a needle biopsy technique. The glycogen content in the quadriceps femoris ranged from 35.3 to 60.2 mM glucosyl units per kg of wet muscle with a mean of 50.0 +/- (SE) 1.2. The mean value of the liver glycogen content was 235.0 +/- 19.4 mM glucosyl units per kg of wet liver tissue with the average 121.1--316.1 mM glucosyl units per kg of wet tissue. It was calculated that approximately 127 mM glucosyl units of the glycogen is stored in the dog liver.

Animals↗
PubMed1986

Kinetic properties of glycogen synthase and phosphorylase and structural aspects of glycogen in the db/db mouse liver.

Kinetic studies were carried out on liver glycogen synthase and phosphorylase isolated from genetically diabetic db/db mice. Glycogen synthase a and b enzymes from diabetic mice had Vmax values 30% and 20% lower, respectively, than the enzymes from normal mice. Glycogen synthase b from diabetic mice also had a 30% lower I0.5 for Pi and ATP at physiologic concentrations of UDP-glucose (0.25 mM) compared with the normal enzyme. Kinetic studies of phosphorylase a showed that, at low glycogen concentrations (0.25 mg/ml), the Vmax of the diabetic enzyme was twofold greater than that of the normal enzyme. This was probably related to the diabetic phosphorylase a having a lower apparent Km for glycogen. This enzyme also had a slightly higher I0.5 for ATP compared with the enzyme from normal mice. Structural studies of liver glycogen isolated from these diabetic mice showed differences from normal mouse glycogen. Both the alpha- and beta-amylase limits were lower in the diabetic glycogen, and the average chain lengths, exterior chain lengths, and interior chain lengths calculated from these limits were all shorter in the glycogen from diabetic mice. Although both normal and diabetic glycogen absorbed light maximally at 430 nm when complexed with iodine, the absolute absorbance value was significantly lower for the diabetic glycogen. These data suggest an altered branching pattern of liver glycogen from the diabetic mice and it is suggested that this altered structure may ultimately influence the activities of glycogen-metabolizing enzymes. These results provide further characterization of the db/db mouse and show heretofore undescribed changes in phosphorylase a kinetics and glycogen structure that occur in diabetes.

Animals↗
PubMed1978

[The role of maternal parathyroids and vitamin D3 metabolites in fetal growth and the deposition of glycogen reserves in the maternal and fetal liver in rats].

Thyro-parathyroidectomy of pregnant Rats at 12.5 days of gestation decreased maternal liver glycogen on 21.5 days of gestation and fetal weight as well as fetal liver glycogen stores. The graft of one parathyroid gland or the injection of 1 alpha-hydroxycholecalciferol in these thyro-parathyroidectomized mothers increased their liver glycogen stores at 21.5 days of gestation. These treatments also markedly increased both fetal weight and fetal liver glycogen stores. It was concluded that maternal 1,25-dihydorxycholecalciferol, which is synthesized under the control of parathyroid hormone secretion, controls fetal growth and liver glycogen stores. The mechanism of these effects (direct or indirect) requires further investigations.

Animals↗
PubMed1982

Changes in liver lobule glycogen zonation during prolonged fasting of rats previously fed a 30% casein diet and adapted to a controlled feeding schedule.

Changes in the lobular distribution of liver glycogen were studied during the prolonged fasting of young adult male Sprague-Dawley rats that were previously adapted to a 30% casein diet and to the 2 + 22 controlled feeding and lighting schedule. The optical density of glycogen, revealed in fixed liver cryostat sections by the periodic acid-Schiff procedure, was determined in the periportal (P), midlobular (M), and centrilobular (C) regions of the liver lobule at various times during a 196-hour fasting period. The prolonged fast could be divided into 3 phases with respect to liver glycogen variation: initial glycogen depletion, glycogen resurgence, and final glycogen depletion. Glycogen was lost from all regions of the liver lobule during the initial glycogen depletion phase. During the glycogen resurgence phase, a lobular glycogen concentration gradient formed (P greater than M greater than C). The simultaneous occurrence of increasing liver glycogen, increasing liver tyrosine aminotransferase activity, and decreasing body fat during glycogen resurgence suggests that the young adult rat does not spare body protein during starvation. During the final glycogen depletion phase, liver glycogen was again present in a lobular gradient (P greater than M greater than C) but the absolute amount of glycogen in each region of the lobule was markedly reduced in comparison with rats killed during glycogen resurgence.

Adaptation, Physiological↗
PubMed1975

Thyroid metabolism in the recessive sex-linked dwarf female chicken. 3. The influence of exogenous thyroid hormones in glycogen metabolism.

The influence of exogenous thyroid hormones on glycogen-body and liver glycogen was studied in fasted and full-fed 3 wk. old dwarf and non-dwarf White Leghorn chickens. The results indicated that in contrast to normals, the glycogen-body of the dwarf was still physiologically active at age 3 wks. and they also exhibited a relatively higher liver glycogen concentration. The liver glycogen concentration was significantly higher in T3-treated, full-fed dwarf chickens when compared with other groups. The data were interpreted to suggest that the differential response observed in both dwarf and non-dwarf chickens of increasing liver glycogen levels with T3 and T4 injections indicated that the proper ratios of serum T3:T4 were probably more vital to the normal metabolic functions than changes in the individual concentrations of either T3 or T4.

Animals↗
PubMed1988

Glycogen phosphorylase activation by progesterone in liver.

Glycogen phosphorylase activity is increased before protein synthesis activation by progesterone. This effect is not blocked by antibiotics (actinomycin D and cycloheximide) that are known to inhibit mRNA or protein synthesis. At times similar to those of phosphorylase activation, cAMP are not enhanced, as would be expected considering the classical glycogenolytic cascade, but depleted with respect to control values. A little earlier, cGMP levels are significantly increased.

Animals↗
PubMed1976

Glycogen regulation in isolated perfused near term monkey liver.

Glycogen metabolism was studied in the isolated perfused liver of the monkey conceptus at 90% of gestation using an in situ recirculating perfusion system. Net uptake of glucose and galactose and the activities of the enzymes, glycogen synthetase and phosphorylase, were studied in response to varied perfusate composition. Synthetase activity was expressed as %I. the percentage of total synthetase activity in the active form. Perfusate glucose concentrations as high as 700 mg/100 ml did not lead to net glucose uptake of to an increase in the baseline %I synthetase (4 +/- 1, mean +/- SEM). In the presence of 300 mg/100 ml glucose, insulin at 10(-7) M in creased %I to 8 +/- 2, and galactose greater than 75 mg/100 ml increased %I to 8 +/- 1. The combination of galactose, glucose, and insulin increased %I to 40 +/- 5. With this latter combination, synthetase activity was proportional to perfusate glucose concentration above 100 mg/100 ml. Phosphorylase activity was diminished by either galactose or insulin, and phosphorylase activity was lowest in the group receiving galactose, glucose, and insulin. Galactose was taken up by all livers, but net glucose uptake was not observed under any condition; net hexose uptake was observed in perfusions with galactose. Glycogen levels did not vary significantly with varied perfusate composition during the 30-min perfusion periods.

Animals↗
PubMedDate not supplied

[Diurnal changes in the glucose and glycogen levels of the blood and liver of rats in chronic consumption of alcohol and after its withdrawal].

Chronic ethanol ingestion by rats exerts almost no effect on the diurnal rhythms of the blood and hepatic glucose concentrations. The rhythm of liver glycogen alters substantially in ethanol-fed animals, the phase of the rhythm being shifted and the daily mean level of glycogen being reduced by a factor of 2. Much more drastic disturbances in carbohydrate metabolism occur after ethanol withdrawal than with ethanol consumption. The diurnal rhythm of liver glycogen becomes inverted in phasing, and the rhythmic amplitude reduced greatly as compared with controls. Both the blood and hepatic glucose concentrations are maintained at nearly constant levels for 18-21 h after ethanol withdrawal, but then the level of blood glucose sharply falls, while that of hepatic glucose somewhat increases. The liver cytosolic water/blood plasma water gradient of glucose 24 h after ethanol withdrawal achieves a value of 4 and remains low 24 h later. The liver glycogen level remains relatively high over the 24 h period after ethanol withdrawal despite the severe hypoglycemia, that can be a result of a limitation of the liver cell membrane permeability for glucose.

Alcoholism↗
PubMed1963

Glycogen deposition in the liver induced by cortisone: dependence on enzyme synthesis.

The deposition of liver glycogen in starved rats given a single dose of cortisone is inhibited by puromycin and actinomycin. The former agent interferes with induced enzyme formation in general, and the latter with the cortisone-induced rise in liver enzyme levels. The results suggest that the regulatory eJffect of cortisone on carbohydrate metabolism may be brought about -by its action on the cellular concentration of certain enzyme proteins.

Animals↗
PubMed1982

Potentiation of insulin secretory response of rats by BCG injection.

Effects of BCG cells on blood insulin, glucose, glycerol and free fatty acid (FFA), and liver glycogen were examined in rats in vivo. Freund's complete adjuvant (FCA) was used as a solution containing BCG cells. Insulin secretion and lactate production by isoproterenol were enhanced by FCA injection. Hyperglycemia induced by epinephrine was somewhat attenuated by treating rats with FCA. The increment of plasma FFA by isoproterenol was smaller in FAC-injected rats than that in control rats. The amount of glycogen in liver was increased by FCA treatment Anti-insulin antiserum (AIS) did not modify the lactate producing action of isoproterenol. FFA release stimulated by isoproterenol was enhanced by AIS. Liver glycogen content in FCA-injected rats was decreased by AIS injection. These results suggest that some component(s) of BCG cells may enhance insulin release stimulated by secretagogues, and insulin thus released attenuates some metabolic effects of the agonist.

Animals↗
PubMed1982

Morphological and biochemical observations on hepatic glycogen metabolism in genetically diabetic (db/db) mice.

Changes in hepatocyte glycogen morphology, liver glycogen, and blood glucose and insulin levels were studied at various time points after initiation of feeding in 10 week old genetic diabetic (db/db) mice (n = 8) and their lean littermates adapted to a controlled feeding regimen (6 h fed - 18 h fast). In spite of hyperinsulinemic (insulin greater than or equal to 97.60 +/- 88 uU/ml) and hyperglycemic (glucose greater than or equal to 437.1 +/- 49.5 mg/dl) conditions favoring glycogen synthesis, feeding-induced hepatic glycogen deposition was less efficient in the diabetic mice. An apparent decreased ability to mobilize hepatic glycogen during fasting and maintenance of relatively high fasting liver glycogen concentrations were however attributable to the anti-glycogenolytic effects of high blood glucose and insulin concentrations. Histochemical determinations (PAS) on livers of db/db mice showed typical lobular patterns of glycogen distribution during deposition and depletion of the polysaccharide. At stages of maximum glycogen (6 h after initiation of feeding), periportal cells displayed intensely stained masses of glycogen with centrilobular cells staining more diffusely. Ultrastructural studies revealed smooth endoplasmic reticulum (SER) in close association with glycogen during its deposition and depletion. The preservation of normal glycogen morphology and SER-glycogen ultrastructure indicates that functioning of the SER in hepatic glycogen metabolism is normal in midly diabetic (db/db) mice.

Animals↗
PubMed1998

Effects of dichloroacetate on glycogen metabolism in B6C3F1 mice.

Dichloroacetate (DCA) is a by-product of drinking water chlorination. Administration of DCA in drinking water results in accumulation of glycogen in the liver of B6C3F1 mice. To investigate the processes affecting liver glycogen accumulation, male B6C3F1 mice were administered DCA in drinking water at levels varying from 0.1 to 3 g/l for up to 8 weeks. Liver glycogen synthase (GS) and glycogen phosphorylase (GP) activities, liver glycogen content, serum glucose and insulin levels were analyzed. To determine whether effects were primary or attributable to increased glycogen synthesis, some mice were fasted and administered a glucose challenge (20 min before sacrifice). DCA treatments in drinking water caused glycogen accumulation in a dose-dependent manner. The DCA treatment in drinking water suppressed the activity ratio of GS measured in mice sacrificed at 9:00 AM, but not at 3:00 AM. However, net glycogen synthesis after glucose challenge was increased with DCA treatments for 1-2 weeks duration, but the effect was no longer observed at 8 weeks. Degradation of glycogen by fasting decreased progressively as the treatment period was increased, and no longer occurred at 8 weeks. A shift of the liver glycogen-iodine spectrum from DCA-treated mice was observed relative to that of control mice, suggesting a change in the physical form of glycogen. These data suggest that DCA-induced glycogen accumulation at high doses is related to decreases in the degradation rate. When DCA was administered by single intraperitoneal (i.p.) injection to naïve mice at doses of 2-200 mg/kg at the time of glucose challenge, a biphasic response was observed. Doses of 10-25 mg/kg increased both plasma glucose and insulin concentrations. In contrast, very high i.p. doses of DCA (> 75 mg/kg) produced progressive decreases in serum glucose and glycogen deposition in the liver. Since the blood levels of DCA produced by these higher i.p. doses were significantly higher than observed with drinking water treatment, we conclude that apparent differences with data of previous investigations is related to substantial differences in systemic dose and/or dose-time relations.

Administration, Oral↗
PubMed1978

Schedule of protein ingestion and circadian variations of glycogen phosphorylase, glycogen synthetase and phosphoenolpyruvate carboxykinase in rat liver.

The circadian rhythms of liver glycogen and hepatic activity of glycogen synthetase (GS), glycogen phosphorylase (GP) and phosphoenolpyruvate carboxykinase (PEPCK) were studied in adult male rats. The rats either received a mixed diet ad libitum (10% protein) or a protein meal (1.85 g protein) given at 09:00 or 21:00 hours, with free access to a protein-free diet (separately-fed). When the protein meal was ingested at 09:00 hours it was followed by a drop in liver glycogen and a persistent daylight increase in GP and PEPCK activities, this phenomenon being attenuated when proteins were ingested during darkness (21:00 hours). Moreover in the latter case, the circadian rhythm of liver glycogen was modified (glycogen accumulation occurring later) and the protein meal ingestion was followed after a transient decrease by a high and sustained GS activity during a long period (12 hours). The drop in the hepatic glycogen level and the unusually long daylight period of sustained GP and PEPCK activities in separately-fed rats consuming the protein meal at 09:00 hours suggests that, in this case, part of the ingested nitrogen could have been catabolized and used for gluconeogenesis, thus explaining our previous observation of lower nitrogen retention observed in this group of rats.

Animals↗
PubMed1998

Glycogen storage diseases and the liver.

Carbohydrate metabolism in the liver is responsible for plasma glucose homeostasis. Liver glycogen storage diseases are metabolic disorders which result in abnormal storage amounts and/or forms of glycogen, and often (but not always) have hepatomegaly and hypoglycaemia as presenting features. To understand the clinical complexity of the glycogen storage diseases, it is necessary to understand the properties and regulation of the proteins involved in glycogen metabolism. Advances in treatment have greatly improved metabolic control and hence the quality of life and survival. However, the lack of understanding of the molecular basis of some of the clinical features of glycogen storage diseases makes it difficult logically to devise optimal treatment regimens to prevent some of the long-term complications. Recently, molecular biology has greatly advanced our understanding of the proteins and genes involved in liver glycogen metabolism and has led to better and less invasive methods of diagnosis of these disorders.

Glycogen Storage Disease↗
PubMed1999

Leptin has acute effects on glucose and lipid metabolism in both lean and gold thioglucose-obese mice.

Leptin is reported to have effects in peripheral tissues that are independent of its central effects on food intake and body weight. In this study, the acute effects of a single dose of recombinant mouse leptin on lipid and glucose metabolism in lean and gold thioglucose-injected obese mice were examined. Changes were measured 2 h after leptin injection. In lean mice, liver and white adipose tissue (WAT) lipogenesis was inhibited. The activity of the pyruvate dehydrogenase complex (PDHCa), the rate-determining step for glucose oxidation, was reduced in heart, liver, quadriceps muscle, and both brown and white adipose tissues. Muscle and liver glycogen and liver triglyceride (TG) content was unchanged, but muscle TG was decreased. In obese mice, liver and WAT lipogenesis was inhibited and PDHCa reduced in heart and quadriceps muscle. Muscle and liver glycogen was decreased but not TG. Serum insulin was reduced in obese but not lean mice. These results are consistent with a role for leptin in the maintenance of steady-state energy stores by decreasing lipid synthesis and increasing fat mobilization, with decreased glucose oxidation occurring as a result of increased fatty acid oxidation.

Adipose Tissue↗
PubMed1985

Compartmentation of glycogen metabolism in the liver.

The incorporation of radioactivity into liver glycogen has been shown not only to be a metabolically inhomogeneous process but also to depend critically on the nature of the precursor. D-Galactose is incorporated into glycogen by a mechanism which is separate from that associated with the incorporation of D-glucose. D-Galactose is favoured for incorporation into high-molecular-weight glycogen and consequently is affected more by treatment of the animal with the antibiotic tunicamycin, since high-molecular-weight glycogen is preferentially found in the lysosomal compartment.

Animals↗
PubMedDate not supplied

Diurnal rhythms in the liver hexokinase and glucokinase activity, in the level of glycogen in liver, skeletal and heart muscles and in the level of blood glucose in laboratory mice.

The experiments were carried out on 84 male Swiss mice. The first group was kept in light-dark conditions L:D = 6:18 and the second one--in reversed photoperiod--L:D = 18:6. After 6 weeks of the experiment the level of glucose in blood, the activity of hexokinase and glucokinase, and the summary activity of these enzymes in the liver, the concentration of glycogen in the liver, myocardium and gastrocnemius muscle were determined. A diurnal rhythm in the level of blood glucose was observed in L:D = 6:18. The rhythm of hexokinase and glucokinase activity in the liver was detected neither under conditions of L:D = 6:18 nor in L:D = 18:6. A diurnal rhythm of the summary activity of hexokinase and glucokinase in the liver was detected in L:D = 6:18. The diurnal rhythm of the level of glycogen in the liver and gastrocnemius muscle was observed in both types of photoperiod. In the myocardium the rhythm was detected neither under L:D = 6:18 nor L:D = 18:6 conditions.

Animals↗