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PubMed1973

Levels of glycogen and trehalose in Mycobacterium smegmatis and the purification and properties of the glycogen synthetase.

The levels of glycogen, free trehalose, and lipid-bound trehalose were compared in Mycobacterium smegmatis grown under various conditions of nitrogen limitation. In a mineral salts medium supplemented with yeast extract and containing fructose as the carbon source, the accumulation of glycogen increased dramatically as the NH(4)Cl content of the medium was lowered. However, levels of free trehalose remained relatively constant. Cells were grown in low nitrogen medium and were then shifted to medium containing high nitrogen. Under these conditions, there was a rapid accumulation of glycogen in low nitrogen, and this glycogen was rapidly depleted when cells were placed in high nitrogen medium. Again the concentration of free trehalose remained fairly constant. However, when cells were grown in low nitrogen medium with [(14)C]fructose and then transferred to high nitrogen medium with unlabeled fructose, the specific radioactivity (counts per minute per micromole) of the free trehalose fell immediately, indicating that it was being synthesized and turned over continually. On the other hand, the specific radioactivity of the glycogen and bound trehalose declined much more slowly, suggesting that these two compounds were not turning over as rapidly or were being synthesized at a much slower rate. Experiments on the incorporation of [(14)C]fructose into glycogen and trehalose indicated that cells in high nitrogen medium synthesized much less glycogen than those in low nitrogen. However, synthesis of both free trehalose and bound trehalose was the same in both cases. The specific enzymatic activities of the glycogen synthetase and the trehalose phosphate synthetase varied somewhat from one growth condition to another, but there was no correlation between enzymatic activity and the amount of glycogen or trehalose, suggesting that changes in glycogen levels were not due to increased synthetic capacity. The glycogen synthetase was purified about 35-fold and its properties were examined. This enzyme was specific for adenosine diphosphate glucose as the glucosyl donor.

Ammonium Sulfate↗

PubMed1968

Glucose and glycogen metabolism in erythrocytes from normal and glycogen storage disease type III subjects.

Active glycogen metabolism has been demonstrated in both normal and glycogen-rich erythrocytes taken from patients with type III glycogen storage disease. Activity of all enzymes catalyzing the reactions required for the synthesis and degradation of glycogen have been demonstrated in the mature erythrocytes. Uniformly labeled glucose-(14)C is incorporated into glycogen in intact cells of both types during incubation. Replacement of the glucose-(14)C by unlabeled glucose in the medium resulted in a significant loss of radioactivity from cellular glycogen. In the absence of the substrate a progressive shortening of outer branches occurred during incubation of intact glucogen-rich cells. Using cells from patients with type III glycogen storage disease, which have sufficient glycogen content to be analyzed by beta-amylolysis, we demonstrated that the glucosyl units are first incorporated in the outer tiers, then transferred to the core where they tend to accumulate due to the absence of amylo-1,6-glucosidase. The glycogen-rich cells have a more rapid rate of glucose utilization upon incubation which is not reflected by a higher lactate production. The increased rate of glucose utilization did not result from an increased rate of glucose incorporation into glycogen in affected cells. The rate of (14)CO(2) production from glucose-1-(14)C during incubation was not significantly different in the two types of cells unless methylene blue was added as an electron acceptor, in which case the glycogen-rich cells oxidized glucose to CO(2) more rapidly.

Blood Glucose↗

PubMed1978

[Studies on the activities of glycogen synthetase and glycogen phosphorylase in the human endometrium (author's transl)].

Glycogen content, glycogen synthetase and glycogen phosphorylase were studied in the endometrial tissues of 28 women with normal menstrual cycles and in the decidual tissues of 24 women with normal early pregnancies. The endometrial glycogen synthetase enzyme increased gradually from the proliferative phase to the secretory phase and reached maximal activity during the sixteenth to twenty-third days of the cycle, a time coincident with maximal glycogen content, while the glycogen phosphorylase reached its maximal activity on and after the twenty-fourth day of the cycle. In addition, glycogen phosphorylase activity in the decidual tissue during the early period of gestation (4--10 weeks) was lower than that in the endometrial tissue during the late secretory phase of the cycle, and in particular, the active form (-AMP) was significantly (p less than 0.005) low, with the result that the glycogen content in the decidua was significantly (p less than 0.05) higher than that in the endometrium. On the other hand, in 20 normal pregnant women during the 6--10th weeks of gestation, the glycogen contents in the decidua and in the placental villi were 599 +/- 44 mg/100 g wet weight (mean +/- standard error of the mean) and 731 +/- 55 mg/100 g, respectively, but the difference between them was statistically not significant. The levels of glycogen synthetase and glycogen phosphorylase enzyme in the decidua were significantly (p less than 0.005) higher than those in the placental villi.

Chorionic Villi↗

PubMed2000

Effects of lithium and insulin on glycogen synthesis in L6 myocytes: additive effects on inactivation of glycogen synthase kinase-3.

In insulin-sensitive L6 myocytes, insulin stimulated glycogen synthesis in a dose-dependent manner and lithium further stimulated glycogen synthesis at all insulin concentrations. Lithium alone at 20 mM stimulated glycogen synthesis to the degree similar to the maximal insulin response. Effects of lithium and insulin were fully additive for both glycogen synthesis and glycogen synthase activity. In L6 myocytes, insulin increased phosphorylation of Akt1 and glycogen synthase kinase-3 alpha and beta (GSK-3 alpha and beta), resulting in its activation and inactivation, respectively. Unlike insulin, lithium directly inhibited GSK-3 (both alpha and beta) without affecting phosphorylation of GSK-3. Moreover, lithium in vitro could further inhibit enzyme activity of GSK-3 (both alpha and beta) that was isolated from insulin-stimulated cells (thus already phosphorylated and inactivated by insulin). In summary, insulin increases glycogen synthesis by the Akt1/GSK-3/glycogen synthase pathway, but lithium increases glycogen synthesis by direct inhibition of GSK-3 in L6 myocytes. Inhibitory effects of lithium and insulin on GSK-3 (both alpha and beta) were additive, which may account, at least in part, for their additive effects on glycogen synthase activity and glycogen synthesis in L6 myocytes.

Animals↗

PubMed2000

Activation of direct and indirect pathways of glycogen synthesis by hepatic overexpression of protein targeting to glycogen.

Glycogen-targeting subunits of protein phosphatase-1, such as protein targeting to glycogen (PTG), direct the phosphatase to the glycogen particle, where it stimulates glycogenesis. We have investigated the metabolic impact of overexpressing PTG in liver of normal rats. After administration of PTG cDNA in a recombinant adenovirus, animals were fasted or allowed to continue feeding for 24 hours. Liver glycogen was nearly completely depleted in fasted control animals, whereas glycogen levels in fasted or fed PTG-overexpressing animals were 70% higher than in fed controls. Nevertheless, transgenic animals regulated plasma glucose, triglycerides, FFAs, ketones, and insulin normally in the fasted and fed states. Fasted PTG-overexpressing animals receiving an oral bolus of [U-(13)C]glucose exhibited a large increase in hepatic glycogen content and a 70% increase in incorporation of [(13)C]glucose into glycogen. However, incorporation of labeled glucose accounted for only a small portion of the glycogen synthesized in PTG-overexpressing animals, consistent with our earlier finding that PTG promotes glycogen synthesis from gluconeogenic precursors. We conclude that hepatic PTG overexpression activates both direct and indirect pathways of glycogen synthesis. Because of its ability to enhance glucose storage without affecting other metabolic indicators, the glycogen-targeting subunit may prove valuable in controlling blood glucose levels in diabetes.

Adenoviridae↗

PubMed1994

Muscle glycogen repletion and pre-exercise glycogen content: effect of carbohydrate loading in rats previously fed a high fat diet.

We have recently reported that rates of muscle glycogen repletion during the early period of recovery were increased by carbohydrate (CHO) loading in rats previously fed a high fat diet. However, the reason for this remained unanswered. The purpose of this study was to examine whether an increase of glycogen utilization due to an elevated pre-exercise glycogen store would enhance rates of glycogen repletion in muscle. Despite an equal degree of glycogen depletion, the rates of glycogen repletion of soleus, red and white gastrocnemius muscles by postexercise administration of glucose (3.0 g.kg-1 body mass) and citrate (0.5 g.kg-1 body mass) were faster in the CHO loaded (3 days) rats than in the nonloaded rats, as a result of elevated pre-exercise glycogen content and consequently the greater glycogen utilization. The higher rate of muscle glycogen repletion may in part be explained by increased postexercise glycogen synthase activity.

Animal Feed↗

PubMed1982

Glycogen and glycogen enzymes in the liver and striated muscle of rats under altered thyroid states.

Changes induced in liver and striated muscle glycogen and glycogen enzymes (glycogen synthetase, glycogen phosphorylase and alpha-amylase) by hypothyroidism and hyperthyroidism in rats have been determined. There were no changes in liver glycogen synthetase, phosphorylase and amylase activities in the hypothyroid group. Hyperthyroid rats showed lower liver glycogen synthetase, phosphorylase a and amylase activities. In muscle, hypothyroid rats had lower phosphorylase activity. In the hyperthyroid group glycogen synthetase was increased.--The results presented do not completely agree with the glycogen levels found in both tissues studied, and they are obviously more related to other factors such as glucose availability. It can be concluded that under the conditions studied, the glycogen enzyme levels could not alone explain the variations of glycogen levels.

Amylases↗

PubMed2005

Phosphorylation-dependent translocation of glycogen synthase to a novel structure during glycogen resynthesis.

Glycogen metabolism has been the subject of extensive research, but the mechanisms by which it is regulated are still not fully understood. It is well accepted that the rate-limiting enzymes in glycogenesis and glycogenolysis are glycogen synthase (GS) and glycogen phosphorylase (GPh), respectively. Both enzymes are regulated by reversible phosphorylation and by allosteric effectors. However, evidence in the literature indicates that changes in muscle GS and GPh intracellular distribution may constitute a new regulatory mechanism of glycogen metabolism. Already in the 1960s, it was proposed that glycogen was present in dynamic cellular organelles that were termed glycosomas but no such cellular entities have ever been demonstrated. The aim of this study was to characterize muscle GS and GPh intracellular distribution and to identify possible translocation processes of both enzymes. Using in situ stimulation of rabbit tibialis anterior muscle, we show GS and GPh intracellular redistribution at the beginning of glycogen resynthesis after contraction-induced glycogen depletion. We identify a new "player," a new intracellular compartment involved in skeletal muscle glycogen metabolism. They are spherical structures that were not present in basal muscle, and we present evidence that indicate that they are products of actin cytoskeleton remodeling. Furthermore, for the first time, we show a phosphorylation-dependent intracellular distribution of GS. Here, we present evidence of a new regulatory mechanism of skeletal muscle glycogen metabolism based on glycogen enzyme intracellular compartmentalization.

Actins↗

PubMed1995

Transient ischemia induces regional myocardial glycogen synthase activation and glycogen synthesis in vivo.

Glycogen is consumed during ischemic preconditioning and synthesized during the subsequent period of ischemic tolerance. To better understand this sequence, we examined the effect of brief coronary artery occlusions on regional myocardial glycogen metabolism in intact, anesthetized rats. Sequential 2-min periods of left coronary artery occlusion reduced the glycogen concentration of the anterior left ventricle approximately 30% relative to the posterior region. During subsequent reperfusion, the activity of the physiologically active glycogen synthase I form of glycogen synthase increased threefold in the anterior region (0.58 +/- 0.11 vs. 0.18 +/- 0.08 mumol.g-1.min-1, P < 0.01), stimulating a similar regional increase in glycogen synthesis rate (0.24 +/- 0.04 vs. 0.08 +/- 0.03 mumol.g-1.min-1, P < 0.01). These events were preceded by a rise in regional glucose 6-phosphate concentration, which increased the activity of a myocardial glycogen synthase phosphatase. In diabetic rats glycogen synthase phosphatase activity was significantly lower, and postischemic glycogen synthase activation was significantly impaired. These data suggest the operation of a feedback loop in which transient ischemia leads to a glucose 6-phosphate-mediated increase in the activity of a phosphoprotein phosphatase active toward glycogen synthase. This suggests phospho-protein phosphatase activation may be a feature of the preconditioned myocardium.

Animals↗

PubMed1994

Insulin but not progesterone promotes the biosynthesis of glycogen in Xenopus laevis oocytes: implications on the control of glycogen synthase by phosphorylation, dephosphorylation.

Insulin, the well-known hypoglycemic hormone, mimics progesterone in promoting the resumption of meiosis within the oocyte of Xenopus laevis. Both hormones exert their action through the inhibition of protein kinases and the activation of protein phosphatases. Because glycogen synthase is an enzyme regulated by a kinases/phosphatases cascade, we investigated the effect of insulin and progesterone on the regulation of glycogen synthesis and glycogen synthase throughout the oogenesis of Xenopus laevis oocytes. In this framework the maximal activity of synthase "a" is concomitant with the vitellogenic period characterized by a drastic increase in the amount of glycogen. Oocyte glycogen synthase is inhibited by cAMP-dependent phosphorylation and stimulated by 20 mM Mg2+. The magnesium effect is inhibited by mu molar concentrations of okadaic acid and suggests that oocyte glycogen synthase is activated by dephosphorylation achieved by protein phosphatase-1. The okadaic acid effect is itself thwarted by the specific inhibitor of protein kinase A, confirming the role of this kinase in the regulation of glycogen synthase. Finally, working on intact ripe oocytes, we showed that insulin but not progesterone increases glycogen synthesis and glycogen synthase "a" activity and lowers the rates of phosphorylation, especially in the glycogen-bound proteins.

Animals↗

PubMed2005

Molecular cloning and seasonal expression of oyster glycogen phosphorylase and glycogen synthase genes.

To investigate the control at the mRNA level of glycogen metabolism in the cupped oyster Crassostrea gigas, we report in the present paper the cloning and characterization of glycogen phosphorylase and synthase cDNAs (Cg-GPH and Cg-GYS, respectively, transcripts of main enzymes for glycogen use and storage), and their first expression profiles depending on oyster tissues and seasons. A strong expression of both genes was observed in the labial palps and the gonad in accordance with specific cells located in both tissues and ability to store glucose. Cg-GPH expression was also found mainly in muscle suggesting ability to use glycogen as readily available glucose to supply its activity. For seasonal examinations, expression of Cg-GYS and Cg-GPH genes appeared to be regulated according to variation in glycogen content. Relative levels of Cg-GYS transcripts appeared highest in October corresponding to glycogen storage and resting period. Relative levels of Cg-GPH transcripts were highest in May corresponding to mobilization of glycogen needed for germ cell maturation. Expression of both genes would likely be driven by the oyster's reproductive cycle, reflecting the central role of glycogen in energy storage and gametogenic development in C. gigas. Both genes are useful molecular markers in the regulation of glycogen metabolism and reproduction in C. gigas but enzymatic regulation of glycogen phosphorylase and synthase remains to be elucidated.

Amino Acid Sequence↗

PubMed1996

Increased glycogen accumulation in transgenic mice overexpressing glycogen synthase in skeletal muscle.

To investigate the role of glycogen synthase in controlling glycogen accumulation, we generated three lines of transgenic mice in which the enzyme was overexpressed in skeletal muscle by using promoter-enhancer elements derived from the mouse muscle creatine kinase gene. In all three lines, expression was highest in muscles composed primarily of fast-twitch fibers, such as the gastrocnemius and anterior tibialis. In these muscles, glycogen synthase activity was increased by as much as 10-fold, with concomitant increases (up to 5-fold) in the glycogen content. The uridine diphosphoglucose concentrations were markedly decreased, consistent with the increase in glycogen synthase activity. Levels of glycogen phosphorylase in these muscles increased (up to 3-fold), whereas the amount of the insulin-sensitive glucose transporter 4 either remained unchanged or decreased. The observation that increasing glycogen synthase enhances glycogen accumulation supports the conclusion that the activation of glycogen synthase, as well as glucose transport, contributes to the accumulation of glycogen in response to insulin in skeletal muscle.

Animals↗

PubMed1998

Mitochondrial respiratory mutants in yeast inhibit glycogen accumulation by blocking activation of glycogen synthase.

Control of glycogen synthase activity by protein phosphorylation is important for regulating the synthesis of glycogen. In this report, we describe a regulatory linkage between the ability of yeast cells to respire and activation of glycogen synthase. Strains containing respiration-deficient mutations in genes such as COQ3, required for the synthesis of coenzyme Q, were reduced in their ability to accumulate glycogen in response to limiting glucose. This lowered glycogen accumulation results from inactivation of the rate-determining enzyme, glycogen synthase (Gsy2p). Reduced glycogen synthase activity is coincident with lowered glucose 6-phosphate and ATP levels in the respiration-deficient cells deprived of glucose. Alanine substitutions of three previously characterized phosphorylation sites in Gsy2p, Ser-650, Ser-654, or Thr-667, each suppressed the glycogen defect in cells unable to respire, suggesting that inactivation of this enzyme is mediated by phosphorylation of these residues. Inactivation of glycogen synthase requires the RAS signaling pathway that controls cAMP-dependent protein kinase and is independent of Pho85p previously identified as a Gsy2p kinase. These results suggest that yeast cells unable to shift from a fermentative to a respiratory metabolic regimen block accumulation of glycogen by inactivating Gsy2p through protein phosphorylation.

Adenosine Triphosphate↗

PubMed2000

Identification of binding sites on protein targeting to glycogen for enzymes of glycogen metabolism.

The activation of protein phosphastase-1 (PP1) by insulin plays a critical role in the regulation of glycogen metabolism. PTG is a PP1 glycogen-targeting protein, which also binds the PP1 substrates glycogen synthase, glycogen phosphorylase, and phosphorylase kinase (Printen, J. A., Brady, M. J., and Saltiel, A. R. (1997) Science 275, 1475-1478). Through a combination of deletion analysis and site-directed mutagenesis, the regions on PTG responsible for binding PP1 and its substrates have been delineated. Mutagenesis of Val-62 and Phe-64 in the highly conserved (K/R)VXF PP1-binding motif to alanine was sufficient to ablate PP1 binding to PTG. Phosphorylase kinase, glycogen synthase, and phosphorylase binding all mapped to the same C-terminal region of PTG. Mutagenesis of Asp-225 and Glu-228 to alanine completely blocked the interaction between PTG and these three enzymes, without affecting PP1 binding. Disruption of either PP1 or substrate binding to PTG blocked the stimulation of PP1 activity in vitro against phosphorylase, indicating that both binding sites may be important in PTG action. Transient overexpression of wild-type PTG in Chinese hamster ovary cells overexpressing the insulin receptor caused a 50-fold increase in glycogen levels. Expression of PTG mutants that do not bind PP1 had no effect on glycogen accumulation, indicating that PP1 targeting is essential for PTG function. Likewise, expression of the PTG mutants that do not bind PP1 substrates did not increase glycogen levels, indicating that PP1 targeting glycogen is not sufficient for the metabolic effects of PTG. These results cumulatively demonstrate that PTG serves as a molecular scaffold, allowing PP1 to recognize its substrates at the glycogen particle.

Alanine↗

PubMed1986

Regulation of rabbit fetal glycogen: effect of in utero fetal decapitation on the metabolism of glycogen in fetal heart, lung, and liver.

To understand the control mechanisms involved in the regulation of fetal glycogen, we have studied the effect of in utero fetal decapitations on glycogen metabolism in rabbit fetal heart, lung, and liver. In utero fetal decapitations were performed between days 18 and 21 of gestation. Two to four fetuses on one side of the horn were decapitated. Fetuses were delivered between days 23 and 26 or between days 28 and 30 of gestation. Fetal heart, lungs, and liver were analyzed for DNA, protein, glycogen, glycogen synthase (I and D forms), glycogen phosphorylase (a and b forms), phosphofructokinase, pyruvate kinase, and lactic dehydrogenase. In fetal heart and lung, no difference was observed in any of the above measurements in the intact and decapitated fetuses. In contrast, fetal liver does not appear to develop the glycogen system as indicated by the very low levels of glycogen (0.02 mg/mg DNA) in decapitated fetuses as compared with intact fetuses (0.4 mg/mg DNA). Similarly the levels of glycogen synthase and phosphorylase were two to three times lower in livers from decapitated fetuses as compared with the livers from intact fetuses. The three enzymes phosphofructokinase, pyruvate kinase, and lactic dehydrogenase were not affected by fetal decapitation in all three tissues. These results indicate that the fetal hypothalamic-pituitary-adrenal (thyroid) axis is not required at least after day 18 of gestation for the normal accumulation and subsequent utilization of glycogen in fetal heart and lungs, while it is an absolute requirement for the development of the fetal liver glycogen system.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1988

Impaired insulin-stimulated muscle glycogen synthase activation in vivo in man is related to low fasting glycogen synthase phosphatase activity.

Insulin-mediated glycogen synthase activity in skeletal muscle correlates with the rate of insulin-mediated glycogen deposition and is reduced in human subjects with insulin resistance. To assess the role of glycogen synthase phosphatase as a possible mediator of reduced glycogen synthase activity, we studied 30 Southwestern American Indians with a broad range of insulin action in vivo. Percutaneous biopsies of the vastus lateralis muscle were performed before and during a 440-min euglycemic clamp at plasma insulin concentrations of 89 +/- 5 and 1,470 +/- 49 microU/ml (mean +/- SEM); simultaneous glucose oxidation was determined by indirect calorimetry. After insulin stimulation, glycogen synthase activity was correlated with the total and nonoxidative glucose disposal at both low (r = 0.73, P less than 0.0001; r = 0.68, P less than 0.0001) and high (r = 0.75, P less than 0.0001; r = 0.74, P less than 0.0001) plasma insulin concentrations. Fasting muscle glycogen synthase phosphatase activity was correlated with both total and nonoxidative glucose disposal rates at the low (r = 0.48, P less than 0.005; r = 0.41, P less than 0.05) and high (r = 0.47, P less than 0.05; r = 0.43, P less than 0.05) plasma insulin concentrations. In addition, fasting glycogen synthase phosphatase activity was correlated with glycogen synthase activity after low- (r = 0.47, P less than 0.05) and high- (r = 0.50, P less than 0.01) dose insulin stimulations. These data suggest that the decreased insulin-stimulated glucose disposal and reduced glycogen synthase activation observed in insulin resistance could be secondary to a low fasting glycogen synthase phosphatase activity.

Adult↗

PubMed1980

Effects of acute variation of fetal glycemia on glycogen storage and on glycogen synthase and phosphorylase activities in the liver of the rat fetus.

The effects of variations of glycemia from 1.7 to 35 mM on the activity of glycogen synthase and phosphorylase, on glycogen content, and on U-14C-glucose incorporation into glycogen in the liver of the near-term rat fetus were investigated. Hypoglycemia did not affect the activities of phosphorylase and synthase; total glycogen content was not modified, but incorporation of labeled glucose was markedly decreased. This is consistent with a decreased glycogen synthesis. A slight hyperglycemia (about 5.5 mM) sharply decreased phosphorylase a (active) activity but increased slightly glycogen synthase a activity; liver glycogen content and labeled glucose incorporation were both enhanced. Higher levels of glycemia induced a decrease of phosphorylase a activity of the same order, but by contrast, glycogen synthase a activity increased progressively with increasing glycemia. Sequential study showed that hyperglycemia first induced the decrease of phosphorylase activity, then increased synthase activity. Marked hyperglycemia strongly enhanced liver glycogen content and labeled glucose incorporation. The fetal liver appears very responsive to acute variations of glycemia. The mechanisms seem to be oriented toward maximal glycogen accumulation.

Animals↗

PubMed2006

Glycogen branches out: new perspectives on the role of glycogen metabolism in the integration of metabolic pathways.

Glycogen is the storage form of carbohydrate for virtually every organism from yeast to primates. Most mammalian tissues store glucose as glycogen, with the major depots located in muscle and liver. The French physiologist Claude Bernard first identified a starch-like substance in liver and muscle and coined the term glycogen, or "sugar former," in the 1850s. During the 150 years since its identification, researchers in the field of glycogen metabolism have made numerous discoveries that are now recognized as significant milestones in biochemistry and cell signaling. Even so, more questions remain, and studies continue to demonstrate the complexity of the regulation of glycogen metabolism. Under classical definitions, the functions of glycogen seem clear: muscle glycogen is degraded to generate ATP during increased energy demand, whereas hepatic glycogen is broken down for release of glucose into the bloodstream to supply other tissues. However, recent findings demonstrate that the roles of glycogen metabolism in energy sensing, integration of metabolic pathways, and coordination of cellular responses to hormonal stimuli are far more complex.

1,4-alpha-Glucan Branching Enzyme↗