Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “LIVER GLYCOGEN”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 325 records · Page 18Linked to original sources
PubMed1983

Phosphorylation and inactivation of rat liver glycogen synthase by cAMP-dependent protein kinase and cAMP-independent synthase (casein) kinase-1.

Phosphorylation of liver glycogen synthase by cAMP-dependent protein kinase (A-kinase) results in the incorporation of approximately 0.7 to 1.0 mol of PO4/subunit. Analyses of the tryptic peptides by isoelectric focusing and peptide mapping reveal the presence of a single 32P-labeled peptide. This extent of phosphorylation does not result in a significant reduction of the synthase activity ratio. Phosphorylation of the liver synthase by cAMP-independent synthase (casein) kinase-1 results in the incorporation of 1.6 to 2.2 mol of PO4/subunit. Although at least 4 tryptic peptides have been found to be labeled with 32P, no significant reduction of the synthase activity ratio was observed. Under the same assay conditions, the muscle synthase is effectively inactivated by either kinase alone or in combination. Inactivation of liver synthase can be achieved after phosphorylation by A-kinase and followed by synthase (casein) kinase-1. However, the inactivation becomes less effective if the order of the addition of these two kinases is reversed. Under the latter assay condition, the phosphate incorporation is less than additive in the presence of both kinases. Prior phosphorylation of the synthase by A-kinase transforms the synthase to become a better substrate for synthase (casein) kinase-1 as evidenced by a 3- to 5-fold increase in the rate of phosphorylation. This increased rate of phosphorylation of the synthase by synthase (casein) kinase-1 results from the rapid phosphorylation of a site neighboring to that previously phosphorylated by A-kinase.

Animals↗
PubMed1977

Effects of hypo and hyperthyroidism on the response to glucose loading of blood glucose, ketones and insulin and liver glycogen as studied in the fasted rat.

After receiving an i.p. glucose load, 24 h fasted thyroidectomized rats showed a progressive increase in blood glucose and a slow decrease in blood ketone bodies. Both liver glycogen and plasma insulin levels showed no differences within 60 min of the glucose administration. It is suggested that the glucose intolerance in these animals is partly due to an insulin deficiency. Thyroidectomized rats treated daily with 25 microgram of L-thyroxine/100 g body weight for 40 days responded to the glucose test with a supranormal and more persistent elevation of blood glucose but with a faster and a greater fall in blood ketone bodies, as compared to controls. Sixty min after the glucose loading, liver glucogen levels were lower and plasma insulin were slightly higher than controls. It is suggested that a diminished extraction of glucose during transhepatic passage can be responsible for the impaired glucose tolerance observed in the hyperthyroid animals.

Animals↗
PubMed1989

Effect of centrally administered glucagon on liver glycogen & enzymes in anaesthetised dogs.

Glucagon (0.01 microgram) administered through the intracerebroventricular route in anaesthetised mongrel dogs, caused a significant rise in blood glucose and a fall in liver glycogen (P less than 0.01). Concurrently, it increased the liver phosphorylase, glutamic oxaloacetic transaminase, glutamic pyruvic transminase and lipase activities by 30 min. Identical changes were observed in vagotomised animals. In pancreatectomised animals as well as in spinal cord transectomised animals, glucagon did not cause these changes. The study indicated that the hyperglycaemia produced by the centrally administered glucagon, is possibly a result of liver glycogenolysis and gluconeogenesis induced by endogenous glucagon secreted from the pancreas, the stimulus for which is the hypothalamo-pancreatic fibres responding to glucagon sensitive neurones in the hypothalamus.

Animals↗
PubMed1983

Inhibitory effect of fasting on the activation of liver glycogen phosphorylase of rats by arginine-vasopressin.

The i.v. bolus of 50 ng kg-1 Arginine-vasopressin administered to adult male rats anaesthetized with Pentobarbital (50 mg kg-1 i.p.) increases the activity of liver glycogen phosphorylase in fed and 24 h fasted rats to the same extent; after 25 ng kg-1 of the drug the enzyme response after fasting is barely detectable, whereas in the fed animals a response similar to that after 50 ng kg-1 persists.

Animals↗
PubMed1986

The diurnal rhythm of liver glycogen phosphorylase: correlating changes in enzyme activity and enzymic protein.

The diurnal rhythm of phosphorylase activity in mouse liver extracts was correlated with the 24 h fluctuations in phosphorylase protein. This last measurement was made using rocket immunoelectrophoresis. The peak activity of phosphorylase appeared coincident (at 18:00 h) with the greatest amount of phosphorylase protein detected. Conversely, the lowest activity measured and lowest enzymic protein content both occurred at 02:00 h. Regression analysis revealed a significant positive correlation between enzyme activity and protein. Thus changes in the cellular concentration of this enzyme are implicated in the diurnal rhythm of liver glycogen.

Animals↗
PubMed1997

Interleukin-6 secretion in mice is associated with reduced glucose-6-phosphatase and liver glycogen levels.

Mice bearing interleukin-6 (IL-6)-secreting tumor were used to study the chronic effect of IL-6 on carbohydrate metabolism. Mice were injected with allogeneic tumor cells transduced with the murine IL-6 gene. Serum IL-6 levels were correlated exponentially with tumor weight. Secretion of IL-6 from the developed tumors was associated with decreased food consumption, reduced body weight, and reduced blood glucose levels. Insulin levels did not change, and 2-deoxyglucose uptake was not affected in most tissues examined. A significant increase of 2-deoxyglucose uptake was measured in the liver. Glycogen content in the liver determined 0, 6, 12, and 18 days after tumor inoculation was 42, 23, 12, and 3 mg/g, respectively. The activity of phosphoenolpyruvate carboxykinase was not affected. The activity of glucose-6-phosphatase (G-6-Phase) determined 6, 12, and 18 days after tumor injection was 84, 70, and 50% of G-6-Pase activity in pair-fed mice bearing nonsecreting tumors, respectively. G-6-Pase mRNA levels were markedly reduced due to inhibition of G-6-Pase gene transcriptional rate.

Animals↗
PubMed1994

Validation of 13C NMR measurements of liver glycogen in vivo.

The natural abundance 13C NMR intensity of the glycogen C1 resonance was measured in the surgically exposed liver of rabbits in vivo (n = 17) by integration from 98 to 104 ppm and compared double blindedly to the subsequent biochemical measurement. Coil loading was measured each time from a reference sphere at the coil center and the NMR intensity was normalized accordingly. For quantification, the normalized NMR intensity was calibrated using aqueous glycogen solutions ranging from 110 to 1100 mumol glucosyl units/g (n = 14). An in vivo range from 110 to 800 mumol glucosyl units/g wet weight was measured with a highly linear correlation with concentration (r = 0.85, P < 0.001). The in vivo NMR concentration was 0.95 +/- 0.05 (mean +/- standard error, n = 17) of the concomitant enzymatic measurement of glycogen content. We conclude that the 13C NMR signal of liver glycogen C1 is essentially 100% visible in vivo and that natural abundance 13C NMR spectroscopy can provide reliable noninvasive estimates of in vivo glycogen content over the physiological range of liver glycogen concentrations when using adequate localization and integration procedures.

Animals↗
PubMed1993

Opposite effects of hyperglycemia and insulin deficiency on liver glycogen synthase phosphatase activity in the diabetic rat.

The specific effect of hyperglycemia on the reported decrease in liver glycogen synthase phosphatase activity was studied in STZ-induced diabetic rats with normal fasting insulinemia. Four groups of animals were investigated: control (nondiabetic), diabetic hyperglycemic (STZ), diabetic normoglycemic (STZ followed by 3-day phloridzin treatment), and a diabetic normoglycemic group injected with glucose to reinstate hyperglycemia. None of the treatments significantly altered fasting plasma insulin and glucagon concentrations. We found that hepatic synthase phosphatase activity decreased in STZ-induced diabetic rats and was further markedly reduced when glycemia was normalized in the diabetic animals. This additional decrease in phosphatase activity was almost fully reversed when hyperglycemia was restored by acute glucose infusion of the normoglycemic diabetic rats. In parallel, the levels of liver G6P and F6P were markedly reduced in the diabetic normoglycemic rats and restored with reinstatement of hyperglycemia. In contrast, liver microsomal glucose-6-phosphatase activity was enhanced and glucokinase activity was lowered in all diabetic groups, regardless of glycemia. Our results indicate that hyperglycemia per se counteracts part of the loss of hepatic synthase phosphatase in diabetic animals and provokes the stable conversion of synthase phosphatase from a less active to a more active form.

Animals↗
PubMed1979

[Changes in carbohydrate digestion enzymes and liver glycogen during heat adaptation].

Adult white rats were exposed daily during 30 days to 2-hour heating (40--41 degrees)--adaptation, and then were transferred to ordinary temperature conditions at 25--27 degrees--desadaptation. The initial period of adaptation revealed a decrease of the liver glycogen content and a relatively constant level of glycemia. A considerable activation of the carbohydrate digestion enzyme systems followed this lowering of energy resources. Metabolic regulatory mechanisms seem to take part in this activation which plays an adaptive role in maintenance of constant glycemia level under these stressful conditions.

Adaptation, Physiological↗
PubMed1986

Regulation of liver glycogen synthase phosphatase activity by ATP-Mg.

The kinetics of a synthase phosphatase reaction inhibited by ATP-Mg in a liver glycogen particle preparation were complex. In the presence of a physiological concentration of ATP-Mg, synthase phosphatase activity in the glycogen particle follows a biphasic course. Initially, the reaction was inhibited but later the reaction rate accelerated. The reaction was inhibited but the rate was constant in the presence of ATP-Mg with the addition of a physiological concentration of glucose 6-phosphate (Glc 6-P). Therefore, in most subsequent experiments Glc 6-P was added. The concentration of ATP-Mg at which 50% maximal inhibition (I0.5) occurred was approximately 0.1 mM in preparations obtained from rats given glucagon prior to being killed. In preparations from animals given glucose, the I0.5 was increased to 2.0 mM. The maximum inhibition was little changed in preparations from glucose- or glucagon-treated animals. Thus, administration of glucose in vivo reduced the sensitivity of the synthase phosphatase to ATP-Mg inhibition. Complexes of ATP with paramagnetic ions such as Co2+ and Mn2+ were less inhibitory than complexes with diamagnetic ions, including Ca2+ and Mg2+. Magnesium complexes of adenosine tetraphosphate and 5'-adenylimidodiphosphate also were inhibitory. Inhibition was independent of phosphorylase a and not a nonspecific, polyvalent anion effect. The best explanation for the distinctive effects of ATP-Mg in preparations from glucagon- and glucose-treated animals is that the respective treatments promote and stabilize different forms of synthase D or possibly synthase phosphatase with different affinities for ATP-Mg. These forms are interconvertible, as previously suggested, in studies employing EDTA (20).

Adenine Nucleotides↗
PubMed1985

The effect of dexamethasone on plasma glucose and liver glycogen levels in premetamorphic Rana catesbeiana tadpoles and frogs.

Premetamorphic Rana catesbeiana tadpoles and adult frogs demonstrate significant elevations in plasma glucose levels following dexamethasone (dex) injections. This response is greatest in the tadpole 24 hr after dex administration and is still detectable at 48 hr. Liver glycogen levels increase in the frog, but not in the tadpole, following daily injections of dex for five consecutive days. The response of the tadpole to dex occurs at a time when hepatic cytosolic glucocorticoid receptors have been observed, but when endogenous corticosterone is absent.

Animals↗
PubMed1969

Rats enriched with odd-carbon fatty acids: maintenance of liver glycogen during starvation.

In young rats a diet containing triundecanoin as the major source of fat produces substantial enrichment of adipose tissue triglycerides with undecanoate and higher fatty acids with odd-numbered carbons. The terminal three-carbon residues arising from beta-oxidation of these acids are glucogenic and help to counteract the decreases in liver glycogen and serum glucose ordinarily induced by prolonged fasting.

Adipose Tissue↗
PubMed1989

Effect of pre- and postnatal protein undernutrition on glycemia, ketonemia and liver glycogen concentration in suckling rats.

Pregnant Wistar rats were fed ad libitum diets containing either 25% (control) or 8% casein (undernourished) from conception through the gestation and lactation periods. Rats from undernourished dams had lower birth weights than control rats and this difference persisted up to day 21 of postnatal life. Livers obtained from undernourished animals aged 10, 15 and 20 days weighed 50% less than control livers. Liver glycogen concentration was much higher in 7- and 10-day-old undernourished rats than in normal rats, but no differences were observed between groups aged 15 or 20 days. Malnutrition caused a decrease in glycemia from 10 days of age and an increase in ketonemia at 10 and 15 days of age. The results show that pre- and postnatal protein malnutrition causes changes in carbohydrate and lipid metabolism in rats during the period of brain growth spurt.

Animals↗
PubMed1999

Contributions of dietary carbohydrate and ethanol to alterations in liver glycogen levels and glycolytic activity.

Hepatic glycogen levels are decreased in rats as a consequence of chronic ethanol consumption. In earlier studies ethanol (36% of total calories consumed) replaced carbohydrate in the ethanol-containing diet, thus leading to the possibility that the decreases in liver glycogen were a result of limited dietary carbohydrate. In the present study, rats were administered ethanol in low-carbohydrate (LC) or high-carbohydrate (HC) diets to determine if lowered dietary carbohydrate contributes to the decrease in glycogen levels associated with ethanol consumption. The glycogen content of isolated hepatocytes was not different between rats fed LC or HC in control or ethanol-containing diets. Lactate and pyruvate were measured to determine the effects of dietary carbohydrate and ethanol on glycolytic activity, and were not significantly altered by changes in the levels of dietary carbohydrate. However, ethanol-containing diets resulted in decreased concentrations of hepatic glycogen, lactate, and pyruvate as compared with controls in both LC and HC diets. These observations demonstrate that decreases in glycogen content and lactate + pyruvate concentrations are due to chronic ethanol consumption rather than a carbohydrate deficiency, when carbohydrate is maintained above 10% of total calories.

Animals↗
PubMed1975

[Effects of nialamide on brain monoamine consumption and liver glycogen content in rats chronically treated with insulin].

Male rats weighing about 50 g were fed a normal-balanced diet for 100 days during which time i.p. injections of saline solution (2 ml/kg) or insulin (4 IU/kg) and/or nialamide (30 mg/kg) were given every two days. The animals were sacrificed 16 hr after the last injection and the brains and livers were extracted for the measurement of tyramine consumption and liver glycogen deposition. It was found that the decrease of glycogen deposition and tyramine consumption induced by nialamide was inhibited by a simultaneous administration of insulin.

Animals↗
PubMed2006

Establishment of correlation between in vitro enzyme binding potency and in vivo pharmacological activity: application to liver glycogen phosphorylase a inhibitors.

In drug discovery, establishing a correlation between in vitro potency and in vivo activity is critical for the validation of the selected target and for developing confidence in the in vitro screening strategy. The present study developed a competition equilibrium dialysis assay using a 96-well dialysis technique to determine the intrinsic Kd for 13 inhibitors of human liver glycogen phosphorylase a (GPa) in the presence of liver homogenate to mimic the physiological environment. The results provided evidence that binding of an inhibitor to GPa was affected by extra cofactors present in the liver homogenate. A good correlation was demonstrated between the in vitro Kd determined under liver homogenate environment and free liver concentration of an inhibitor at the minimum efficacious dose in diabetic ob/ob mice. This study revealed important elements (such as endogenous cofactors missing from the in vitro assay and free concentration at the target tissue) that contributed to a better understanding of the linkage between in vitro and in vivo activity. The approach developed here may be applied to many drugs in pharmacology studies in which the correlation between in vitro and in vivo activities for the target tissue (such as solid tumors, brain, and liver) is critical.

Animals↗
PubMed1982

[Liver glycogen, blood glucose, somatotropic hormone, and hypophyseal thyrotropin in neonatal rats treated with cortisol and in malnourished ones].

A population of rats treated with a single dose of cortisol on their first day of life and a population of rats underfed since day sixteen of gestation until sacrificed have been studied. Body, brain and liver glycogen content have been measured at eight, twelve and twenty-two days of life and compared to controls of the same age. Pituitary growth hormone and thyrotrophin content have also been measured in the same population of animals and at the same stages of life. Results are compared to those found in "neo-T4" rats -- which receive 30 micrograms T4 in 5 doses during the first days of life -- at the same ages.

Animals↗
PubMed1982

Rabbit liver glycogen synthase kinases. Characterization of a protein kinase (PC0.7) able to phosphorylate glycogen synthase and phosvitin.

A rabbit liver protein kinase (PC0.7), able to phosphorylate glycogen synthase and phosvitin, has been extensively purified. The enzyme had apparent Mr = 170,000-190,000 as judged by gel filtration and was associated with two major polypeptide species, alpha (Mr = 43,000) and beta (Mr = 25,000). Two other polypeptides, Mr = 38,000 and Mr = 35,000, were also detected. Treatment with trypsin led to an enzyme composed only of polypeptides of Mr = 35,000 and Mr = 25,000. The beta-polypeptide underwent autophosphorylation when incubated with Mg2+ and ATP or GTP. The protein kinase was effective in utilizing both ATP and GTP as the phosphoryl donor (apparent Km values 5-11 microM and 9-19 microM, respectively). The enzyme phosphorylated phosvitin, casein, and glycogen synthase but not histone or phosphorylase and was inhibited by heparin. Phosphorylation of glycogen synthase proceeded to approximately 0.5 phosphate/subunit with little inactivation of the glycogen synthase. The phosphorylation occurred predominantly in a 21,000-dalton CNBr fragment of glycogen synthase that had been previously shown to reside toward the COOH terminus of the molecule. The liver PC0.7 appeared very similar to an analogous enzyme isolated from rabbit muscle (DePaoli-Roach, A. A., Ahmad, Z., and Roach, P. J. (1981) J. Biol. Chem. 256, 8955-8962). The present work, therefore, provides a point of contact between the Ca2+ and cyclic nucleotide-independent glycogen synthase kinases of rabbit liver and muscle.

Animals↗