Altered hepatic glycogen metabolism and glucoregulatory hormones during sepsis

1976 ◽  
Vol 230 (5) ◽  
pp. 1296-1301 ◽  
Author(s):  
RT Curnow ◽  
EJ Rayfield ◽  
DT George ◽  
TV Zenser ◽  
FR DeRubertis
Keyword(s):  
Cyclic Amp ◽  
Portal Vein ◽  
Glycogen Synthase ◽  
Glycogen Metabolism ◽  
Liver Glycogen ◽  
Hepatic Glycogen ◽  
In Situ Perfusion ◽  
Glucoregulatory Hormones

Levels of glucose, insulin, and glucagon in portal vein plasma and of liver glycogen and cyclic AMP and activities of glycogen synthase and phosphorylase in liver were assayed in control (CONT) rats and rats infected (INF) with Diplococcus pneumoniae. In INF rats compared with CONT rats, insulin and glucagon levels were higher (8,12,24 h). Activity of synthase I was lower (8, 12, 24 h) and of phosphorylase higher (12 and 24 h) in INF rats. Cyclic AMP levels were higher in INF rats at 12 and 24 h. Total synthase activity was lower in INF rats at 24 h. Glucose given intravenously increased glycogen less in INF than in CONT rats and activated synthase and inactivated phosphorylase in all animals except at 24 h in INF rats. However, in situ perfusion of the livers at 24 h with glucose in buffer decreased phosphorylase activities in all animals and increased synthase I activities in CONT but not INF rats.

The variable clinical phenotype of three patients with hepatic glycogen synthase deficiency

2017 ◽  
Vol 30 (4) ◽  
Author(s):  
Çiğdem Seher Kasapkara ◽  
Zehra Aycan ◽  
Esma Açoğlu ◽  
Saliha Senel ◽  
Melek Melahat Oguz ◽  
...  
Keyword(s):  
Glycogen Synthase ◽  
Glucose Monitoring ◽  
Glycogen Metabolism ◽  
Liver Glycogen ◽  
Postprandial Hyperglycemia ◽  
Hepatic Glycogen ◽  
Case Presentation ◽  
Ketotic Hypoglycemia ◽  
Fasting Hypoglycemia ◽  
Lactic Acidemia

AbstractBackground:Glycogen synthase deficiency, also known as glycogenosis (GSD) type 0 is an inborn error of glycogen metabolism caused by mutations in theCase presentation:Herein we report three new cases of liver glycogen synthase deficiency (GSD0). The first patient presented at the 4 years of age with recurrent hypoglycemic seizures. The second patient who is the brother of the first patient presented at 15 months with asymptomatic incidental hypoglycemia. Glucose monitoring in both patients revealed daily fluctuations from fasting hypoglycemia to postprandial hyperglycemia and lactic acidemia. A third patient was consulted for ketotic hypoglycemia and postprandial hyperglycemia at the 5 years of age.Conclusions:Genetic analyses of the siblings revealed homozygosity for mutation c.736C>T on the

scholarly journals Altered liver glycogen metabolism in fed genetically obese mice

1983 ◽  
Vol 216 (2) ◽  
pp. 273-280 ◽  
Author(s):  
G van de Werve ◽  
F Assimacopoulos-Jeannet ◽  
B Jeanrenaud
Keyword(s):  
Cyclic Amp ◽  
Glycogen Synthase ◽  
Glycogen Metabolism ◽  
Liver Glycogen ◽  
Obese Mice ◽  
Apparent Paradox ◽  
Sequential Inactivation ◽  
Altered Liver ◽  
Isolated Liver

The cyclic AMP and glycogen concentrations and the activities of phosphorylase kinase, phosphorylase a and glycogen synthase a were not different in livers from lean or ob/ob mice despite increased plasma glucose and insulin in the obese group. The liver water content was decreased by 10% in the obese mice. In hepatocytes isolated from lean mice and incubated with increasing glucose concentrations (14-112 mM), a sequential inactivation of phosphorylase and activation of glycogen synthase was observed. In hepatocytes from obese mice the inactivation of phosphorylase was not followed by an activation of synthase. The inactivation of phosphorylase occurred more rapidly and was followed by an activation of synthase in hepatocytes isolated from both groups of mice when in the incubation medium Na+ was replaced by K+ or when Ca2+ was omitted and 2.5 mM-EGTA included. The inactivation of phosphorylase and activation of synthase were not different in broken-liver-cell preparations from lean and obese animals. The re-activation of phosphorylase in liver filtrates in the presence of 0.1 microM-cyclic AMP and MgATP was inhibited by about 70% by EGTA and stimulated by Ca2+ and was always greater in preparations from ob/ob mice. The apparent paradox between the impairment of glycogen metabolism in isolated liver preparations and the situation in vivo in obese mice is discussed.

Metabolic effects of oral fructose in the liver of fasted rats

1984 ◽  
Vol 247 (4) ◽  
pp. E505-E512 ◽  
Author(s):  
C. B. Niewoehner ◽  
D. P. Gilboe ◽  
G. A. Nuttall ◽  
F. Q. Nuttall
Keyword(s):  
Uric Acid ◽  
Portal Vein ◽  
Hepatic Vein ◽  
Glycogen Synthase ◽  
Control Level ◽  
Liver Glycogen ◽  
Glycogen Storage ◽  
Metabolic Effects ◽  
Serum Triglycerides ◽  
Fasted Rats

Twenty-four-hour-fasted rats were given fructose (4 g/kg) by gavage. Fructose absorption and the portal vein, aorta, and hepatic vein plasma fructose, glucose, lactate, and insulin concentrations as well as liver fructose and fructose 1-P, glucose, glucose 6-P, UDPglucose, lactate, pyruvate, ATP, ADP, AMP, inorganic phosphate (Pi), cAMP, and Mg2+, and glycogen synthase I and phosphorylase alpha were measured at 10, 20, 30, 40, 60 and 120 min after gavage. Liver and muscle glycogen and serum uric acid and triglycerides also were measured. Fifty-nine percent of the fructose was absorbed in 2 h. There were modest increases in plasma and hepatic fructose, glucose, and lactate and in plasma insulin. Concentrations in the portal vein, aorta, and hepatic vein plasma indicate rapid removal of fructose and lactate by the liver and a modest increase in production of glucose. The source of the increase in plasma lactate is uncertain. Hepatic glucose 6-P increased twofold; UDPglucose rose transiently and then decreased below the control level. Fructose 1-P increased linearly to a concentration of 3.3 mumol/g wet wt by 120 min. There was no change in ATP, ADP, AMP, cAMP, Pi, or Mg2+. Serum triglycerides and uric acid were unchanged. Glycogen synthase was activated by 20 min without a change in phosphorylase alpha. This occurred with a fructose dose that did not significantly increase either the liver glucose or fructose concentrations. Liver glycogen increased linearly after 20 min, and glycogen storage was equal in liver (38.4%) and muscle (36.5%).(ABSTRACT TRUNCATED AT 250 WORDS)

Effect of nonworking heterotopic transplantation on rat heart glycogen metabolism

1995 ◽  
Vol 268 (1) ◽  
pp. E48-E54 ◽  
Author(s):  
P. H. McNulty ◽  
W. X. Liu ◽  
M. C. Luba ◽  
J. A. Valenti ◽  
G. V. Letsou ◽  
...  
Keyword(s):  
Rat Heart ◽  
Insulin Infusion ◽  
Glycogen Synthase ◽  
Glycogen Metabolism ◽  
Work History ◽  
Glycogen Concentration ◽  
Mechanical Unloading ◽  
History Of ◽  
Stimulation Of

To determine whether the contractile work history of cardiac muscle influences its responsiveness to insulin, we examined the effect of insulin infusion on glycogen metabolism in the rat heart 1 wk after transplantation into a nonworking heterotopic infrarenal position. Nonworking heterografts had higher basal glycogen concentrations than did in situ working hearts of the same animals (29.9 +/- 2.7 vs. 23.3 +/- 0.8 mumol/g; P < 0.05), and a smaller fraction of their glycogen synthase enzyme activity was in the physiologically active glycogen synthase I form (8 +/- 2 vs. 22 +/- 3%; P < 0.02). During a 25-min infusion of insulin (1 U/min) and glucose (30 mg.kg-1.min-1), the fractional glycogen synthase I activity of heterografts remained lower than that of in situ hearts (29 +/- 5 vs. 56 +/- 7%; P < 0.02) and heterografts synthesized glycogen more slowly (0.126 +/- 0.07 vs. 0.352 +/- 0.06 mumol.g-1.min-1; P < 0.02). These effects could be duplicated by a 24-h fast, which similarly increased myocardial glycogen concentration (to 32.9 +/- 5.6 mumol/g). These observations suggest that the performance of repetitive contractile work is necessary to maintain the myocardium maximally responsive to insulin. Mechanical unloading increases myocardial glycogen concentration, thereby reducing the magnitude of insulin's stimulation of glycogen synthase and consequently the rate of incorporation of circulating glucose into glycogen.

Hormonal Control of Hepatic Glycogen Metabolism in Food-deprived, Continuously Swimming Coho Salmon (Oncorhynchus kisutch)

1993 ◽  
Vol 50 (8) ◽  
pp. 1676-1682 ◽  
Author(s):  
M. M. Vijayan ◽  
A. G. Maule ◽  
C. B. Schreck ◽  
T. W. Moon
Keyword(s):  
Coho Salmon ◽  
Glycogen Synthase ◽  
Oncorhynchus Kisutch ◽  
Glucose Production ◽  
Glycogen Metabolism ◽  
Hormonal Control ◽  
Hepatic Glycogen ◽  
Anabolic Hormone ◽  
Total Glucose ◽  
Glycogen Breakdown

The plasma cortisol concentration and liver cytosolic glucocorticoid receptor activities of continuously swimming, food-deprived coho salmon (Oncorhynchus kisutch) did not differ from those of resting, fed fish. Plasma glucose concentration was significantly higher in the exercising, starved fish, but there were no significant differences in either hepatic glycogen concentration or hepatic activities of glycogen phosphorylase, glycogen synthase, pyruvate kinase, or lactate dehydrogenase between the two groups. Total glucose production by hepatocytes did not differ significantly between the two groups; glycogen breakdown accounted for all the glucose produced in the resting, fed fish whereas it explained only 59% of the glucose production in the exercised animals. Epinephrine and glucagon stimulation of glucose production by hepatocytes was decreased in the exercised fish without significantly affecting hepatocyte glycogen breakdown in either group. Insulin prevented glycogen breakdown and enhanced glycogen deposition in exercised fish. The results indicate that food-deprived, continuously swimming coho salmon conserve glycogen by decreasing the responsiveness of hepatocytes to catabolic hormones and by increasing the responsiveness to insulin (anabolic hormone).

scholarly journals The Role of Hormones in the Regulation of Glycogen Metabolism in the Clawed Toad Xenopus Laevis (Daudin)

2019 ◽  
pp. 17-24
Author(s):  
Daphna Atar-Zwillenberg ◽  
Michael Atar ◽  
Gianni Morson ◽  
Udo Spornitz
Keyword(s):  
Blood Glucose ◽  
Xenopus Laevis ◽  
Muscle Glycogen ◽  
Hormonal Regulation ◽  
Glycogen Content ◽  
Glycogen Metabolism ◽  
Liver Glycogen ◽  
Hepatic Glycogen ◽  
Lipid Levels ◽  
Liver Glycogen Content

The hormonal regulation of amphibian glycogen metabolism was studied in Xenopus laevis as a typical member of the anurans (tailless amphibians).The main focus of this study was given to the effects of various hormones on the glycogen/glucose balance in adult toads. We determined biochemically the liver and muscle glycogen contents as well as the blood glucose and lipid levels for a number of hormones and also diabetes inducing substances. Additionally, we examined ultrastructure changes in hepatocytes induced by the various treatments, and also investigated the activity of carbohydrate-relevant enzymes by histochemistry. With one exception, the liver glycogen content of Xenopus remained basically unchanged by the treatments or was even slightly enhanced. Only human chorionic gonadotropin, through which the vitellogenic response is triggered, prompts a significant decrease of liver glycogen in females. Under the same conditions the male liver glycogen content remained stable. Muscle glycogen contents were not affected by any of the treatments. Blood glucose and lipid levels on the other hand were elevated considerably in both sexes after application of either epinephrine or cortisol. The ultrastructural examination revealed a proliferation of Rough Endoplasmic Reticulum (RER) in hepatocytes from epinephrine treated toads of both sexes as well as from HCG treated females. By histochemistry, we detected an elevated glucose-6-phosphatase activity in the hepatocytes from toads treated with either epinephrine or cortisol. These treatments also led to enhanced glycogen phosphorylase activity in males, and to a slightly elevated glyceraldehyde-3-phosphate dehydrogenase activity in females. Our results show that the hepatic glycogen is extremely stable in adult Xenopus. Only vitellogenesis causes a marked utilization of glycogen. Since the blood glucose levels are elevated in epinephrine or cortisol treated toads without the liver glycogen being affected, we conclude that either protein and/or lipid metabolism are involved in carbohydrate metabolism in Xenopus laevis.

Effects of glucagon with or without insulin administration on liver glycogen metabolism

1995 ◽  
Vol 269 (2) ◽  
pp. E231-E238 ◽  
Author(s):  
N. Ercan ◽  
M. C. Gannon ◽  
F. Q. Nuttall
Keyword(s):  
Plasma Glucose ◽  
Glycogen Phosphorylase ◽  
Glycogen Metabolism ◽  
Liver Glycogen ◽  
Hepatic Glycogen ◽  
Insulin Administration ◽  
Similar Increase ◽  
Glycogen Concentration ◽  
Ad Libitum ◽  
Glucagon And Insulin

Rats fed ad libitum were given insulin alone (4 U/kg), glucagon alone (25 micrograms/kg), or insulin and glucagon sequentially. Phosphorylase a and synthase R activities, hepatic glycogen, uridine diphosphoglucose, inorganic phosphate (Pi), and plasma glucose, lactate, glucagon, and insulin concentrations were determined over the subsequent 40 min. In separate animals, muscle extraction of 2-deoxy-D-[3H]glucose also was determined. After glucagon administration, glycogen phosphorylase a and plasma glucose were increased within 5 min. However, the glycogen concentration did not decrease for 20 min. Glucagon administration to rats pretreated with insulin stimulated a similar increase in phosphorylase a activity. Again, glycogen was not degraded for 20 min. After insulin only, glycogen concentration remained unchanged. Plasma glucose decreased as expected. In each group, muscle extraction of 2-deoxy-D-[3H]glucose increased compared with the controls (P < 0.05). In summary, glucagon and/or insulin administration did not stimulate significant glycogen degradation for 20 min, even though phosphorylase was activated. The mechanism remains to be determined.

Lack of defect in insulin action on hepatic glycogen synthase and phosphorylase in insulin-resistant monkeys

1998 ◽  
Vol 274 (6) ◽  
pp. G1005-G1010
Author(s):  
Heidi K. Ortmeyer ◽  
Noni L. Bodkin
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Muscle Glycogen ◽  
Rhesus Monkeys ◽  
Insulin Action ◽  
Glycogen Phosphorylase ◽  
Glycogen Synthase ◽  
Liver Glycogen ◽  
Hepatic Glycogen ◽  
Insulin Resistant

It is well known that an alteration in insulin activation of skeletal muscle glycogen synthase is associated with insulin resistance. To determine whether this defect in insulin action is specific to skeletal muscle, or also present in liver, simultaneous biopsies of these tissues were obtained before and during a euglycemic hyperinsulinemic clamp in spontaneously obese insulin-resistant male rhesus monkeys. The activities of glycogen synthase and glycogen phosphorylase and the concentrations of glucose 6-phosphate and glycogen were measured. There were no differences between basal and insulin-stimulated glycogen synthase and glycogen phosphorylase activities or in glucose 6-phosphate and glycogen contents in muscle. Insulin increased the activities of liver glycogen synthase ( P < 0.05) and decreased the activities of liver glycogen phosphorylase ( P ≤ 0.001). Insulin also caused a reduction in liver glucose 6-phosphate ( P = 0.05). We conclude that insulin-resistant monkeys do not have a defect in insulin action on liver glycogen synthase, although a defect in insulin action on muscle glycogen synthase is present. Therefore, tissue-specific alterations in insulin action on glycogen synthase are present in the development of insulin resistance in rhesus monkeys.

Effect of vasoactive intestinal polypeptide on glycogen metabolism in rat hepatocytes

1982 ◽  
Vol 242 (4) ◽  
pp. E262-E272 ◽  
Author(s):  
C. L. Wood ◽  
J. J. Blum
Keyword(s):  
Phosphatase Activity ◽  
Vasoactive Intestinal Polypeptide ◽  
Glycogen Synthase ◽  
Gut Hormones ◽  
Rat Hepatocytes ◽  
Glycogen Metabolism ◽  
Hepatic Glycogen ◽  
Glycogen Deposition ◽  
Intestinal Polypeptide

The effects of vasoactive intestinal polypeptide (VIP) on several enzymes of glycogen metabolism in rat hepatocytes were compared with those of glucagon and of vasopressin (ADH). VIP caused phosphorylase activation and glycogenolysis in hepatocytes from fed rats. In hepatocytes from fasted rats incubated with glucose, lactate, and pyruvate, VIP inhibited net glycogen deposition, inactivated glycogen synthase, and activated phosphorylase. VIP was about 100-fold less potent than glucagon and 1,000-fold less potent than ADH in causing activation of phosphorylase. The ability of VIP to activate phosphorylase was not altered by chelation of the calcium in the medium. The half maximal effective doses of VIP for both phosphorylase activation and stimulation of glycogenolysis were 10-30 nM. Treatment with VIP, ADH, or glucagon did not decrease phosphorylase phosphatase activity. Each of these hormones, however, lengthened the lag time before synthase phosphatase activity was expressed in vitro. Other gut hormones tested did not affect hepatocyte glycogen metabolism. These results do not support the concept of physiologic control of hepatic glycogen metabolism by VIP or by other gut hormones.

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