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PubMed1984

Phosphorylation of glycogen synthase by the Ca2+- and phospholipid-activated protein kinase (protein kinase C).

The Ca2+- and phospholipid-dependent protein kinase (protein kinase C) has been found to phosphorylate and inactivate glycogen synthase. With muscle glycogen synthase as a substrate, the reaction was stimulated by Ca2+ and by phosphatidylserine. The tumor-promoting phorbol esters 12-O-tetradecanoyl phorbol 13-acetate was also a positive effector, half-maximal activation occurring at 6 nM. Phosphorylation of glycogen synthase, but not histone, was partially inhibited by glycogen, half-maximally at 0.05 mg/ml, probably via a substrate-directed mechanism. The rate of glycogen synthase phosphorylation was approximately half that for histone; the apparent Km for glycogen synthase was 0.25 mg/ml. Protein kinase C also phosphorylated casein, the preferred substrate among the individual caseins being alpha s1-casein. Glycogen synthase was phosphorylated to greater than 1 phosphate/subunit with an accompanying reduction in the -glucose-6-P/+glucose-6-P activity ratio from 0.9 to 0.5. Phosphate was introduced into serine residues in both the NH2-terminal and COOH-terminal CNBr fragments of the enzyme subunit. The two main tryptic phosphopeptides mapped in correspondence with the peptides that contain site 1a and site 2. Lesser phosphorylation in an unidentified peptide was also observed. Rabbit liver and muscle glycogen synthases were phosphorylated at similar rates by protein kinase C. The above results are compatible with a role for protein kinase C in the regulation of glycogen synthase as was suggested by a recent study of intact hepatocytes.

Animals↗

PubMed1981

Activity of enzymes regulating glycogen metabolism in perfused muscle-cuticle sections of Ascaris suum (Nematoda).

A new perfusion system has been developed in which muscle-cuticle sections of Ascaris suum were perfused, enabling study of enzymes in vitro. Using this technique the activity of the regulatory enzymes glycogen synthase and glycogen phosphorylase was determined, and the level of glycogen in the muscle was assessed. During starvation, 98% of glycogen synthase was in the inactive D-form, and 80% of the glycogen phosphorylase activity was in the active a-form. When the ascarid muscle section was perfused with 27 mM glucose, 13.1% of the glycogen synthase was in the active I-form, whereas phosphorylase a-levels dropped to 46% and glycogen was synthesized at a linear rate of 12 mg/g/hr or 1.23 mumoles/min/g muscle-cuticle. ATP levels (3.71 +/- 0.32 mM) remained unchanged over a 4-hr perfusion period with an adenylate energy charge of 0.82. Fructose supported glycogen synthesis, though not as well as glucose. Galactose, mannose, and trehalose did not support glycogen synthesis. The new perfusion system should be useful in future, similar studies on Ascaris.

Animals↗

PubMed1981

Glycogen metabolizing enzymes during starvation and feeding of Ascaris suum maintained in a perfusion chamber.

The glycogen content of muscle was correlated with the activity of glycogen synthase and glycogen phosphorylase from the parasitic roundworm Ascaris suum maintained in vitro. Adult female worms were maintained in the laboratory in a perfusion system during periods of starvation and feeding. During starvation, the levels of glucogen decreased at a rate of 0.1 to 0.2 mumoles/min/g wet weight of muscle-cuticle. During this time, 95% of the glycogen synthase (E.C. 2.4.1.11) was in the active D-form, and 48% of the phosphorylase (E.C. 2.4.1.1) was in the active a-form. Upon feeding, the rate of incorporation of glycosyl residues into glycogen proceeded at a rate of 0.75 to 1.0 mumoles/min/g muscle-cuticle. Glycogen synthase was 22% in the active I-form and phosphorylase a-levels remained virtually unchanged at 41% as compared with the starved worm. Total levels of both enzymes remained constant over the starvation-feeding period with 3.9 units/g phosphorylase and 0.4 units/g glycogen synthase. The apparent Km value for the substrate UDPG for glycogen synthase was 0.22 +/- 0.02 mM. For glycogen phosphorylase the Km value for G-1-P was 1.76 +/- 0.38 mM.

Animals↗

PubMed1996

Insulin action in cultured human myoblasts: contribution of different signalling pathways to regulation of glycogen synthesis.

A key metabolic action of insulin is the stimulation of non-oxidative glucose utilization in skeletal muscle, by increasing both glucose uptake and glycogen synthesis. The molecular mechanism underlying this process has been investigated using a variety of experimental systems. We report here the use of cultured human myoblasts to study insulin control of glycogen synthesis in humans. In these cells insulin stimulates glycogen synthesis approx. 2.2-fold, associated with a similar activation of glycogen synthase (GS) which occurs within 5-10 min of the addition of insulin. Insulin also causes inactivation of glycogen synthase kinase-3 (GSK-3) and activation of protein kinase B, both processes being sufficiently rapid to account for the effects of insulin on GS. Activation by insulin of the protein kinases p70s6K, p90s6K and extracellular signal-regulated kinase 2 (ERK2) is observed, but is significantly slower than the activation of GS. Selective inhibitors of the p70s6K pathway (rapamycin), the ERK2/p90s6K pathway (PD98059) and phosphatidylinositol 3-kinase (wortmannin) have been used to probe the contribution of these components to insulin signalling in human muscle. Wortmannin blocks activation of both glycogen synthesis and GS and inactivation of GSK-3. PD98059 is without effect on these events, while rapamycin is without effect on inactivation of GSK-3 but partially blocks activation of glycogen synthesis and GS. Taken together, these findings suggest that protein kinase B is responsible for the inactivation of GSK-3, but that an additional rapamycin-sensitive mechanism may contribute to the activation of GS and stimulation of glycogen synthesis.

Androstadienes↗

PubMed2000

Determination of yeast glycogen content by individual cell spectroscopy using image analysis.

A rapid technique has been developed to determine the glycogen content of yeast on an individual cell basis using a combination of image analysis technology and staining of yeast cells with an I(2):KI solution. Changes in mean cellular glycogen content during alcoholic fermentation have been reported using this technique. The glycogen content of stored brewer's yeast is heterogeneous compared to freshly propagated yeast which have a more uniform distribution of glycogen. Analysis of the distribution of yeast glycogen during fermentation indicates that a fraction of yeast cells do not dissimilate glycogen. Therefore, conventional analysis of the mean glycogen content of yeast used to inoculate fermentations is of limited use, unless information regarding the proportion of cells which utilize glycogen is known. Analysis of the distribution of glycogen within a yeast population can serve as a useful indicator of yeast quality.

Aerobiosis↗

PubMed1984

Distribution of glycogen in the floor plate of the chick spinal cord during development.

The present study was undertaken to characterize the structural changes and the glycogen distribution in the floor plate of the developing chick spinal cord. The floor plate consisted of ventricular zone by stage 19 (staged according to Hamburger and Hamilton, 1951). The marginal zone of this plate could be distinguished as a narrow border at stage 21. It increased progressively in thickness and was the same thickness as the ventricular zone at stage 26. It increased again in thickness from stage 38 onward. Glycogen appeared and subsequently disappeared in the floor plate of the chick spinal cord during development. Little, if any, glycogen appeared in the midportion of the floor plate at stage 19. The floor plate was weakly glycogen positive from the cervical through lumbosacral segments at stage 21. In the floor plate of the lumbosacral enlargement the glycogen staining was the highest and was maximal through stages 34-37. The floor plate of the cervical and thoracic segments except for the cervical enlargement continue to have low concentrations of glycogen. The glycogen staining of the floor plate began to decrease from stage 38, and at the same time neuroglial cells began to migrate into the marginal zone of the floor plate, later than in other regions of the cord. The glycogen staining in the floor plate was barely detectable at stage 40. The accumulation of the glycogen granules in the floor plate was found only in the radial glial cells.

Animals↗

PubMed1989

Comparison of 3H-galactose and 3H-glucose as precursors of hepatic glycogen in control-fed rats.

Labeling of hepatic glycogen derived from 3H-galactose and 3H-glucose was compared shortly after intravenous injection in control-fed rats. The rats were allowed to accumulate 5-8% glycogen prior to receiving label. Fifteen minutes to 2 hours after labeling, liver was excised and processed for routine light (LM) and electron microscopic (EM) radioautography (RAG) or biochemical analysis. After injection of 3H-galactose, LM-RAGs revealed that the percentage of heavily labeled hepatocytes increased from 37% after 15 minutes to 68% after 1 hour but showed no further increase after 2 hours. alpha-Amylase treatment removed most glycogen and incorporated label; thus few silver grains were observed, indicating little incorporation of label except into glycogen. EM-RAGs demonstrated that most label occurred where glycogen was located. Biochemical analysis showed initially a high blood level of label that rapidly plateaued at a reduced level by 5 minutes. Concomitantly, glycogen labeling determined by liquid scintillation counting reflected the increases observed in the RAGs. After injection of 3H-glucose, LM-RAGs revealed that only 12% of the hepatocytes were heavily labeled at 1 hour and 20% at 2 hours. In tissue treated with alpha-amylase, glycogen was depleted and label was close to background level at each interval observed. EM-RAGs showed most grains associated with glycogen deposits. Biochemically, blood levels of label persisted at a high level for 30 minutes and tissue levels increased slowly over the 2-hour period. This study shows that incorporation from 3H-galactose was more rapid than incorporation of 3H-glucose; however, label derived from both carbohydrates appeared to be incorporated mainly into glycogen.

Animals↗

PubMed1989

Comparative study of nuclear and cytoplasmic glycogen isolated from mutant HD33 ascites cells.

Mutant cells of the HD33 subline of the Ehrlich-Lettré ascites tumor synthesize and store glycogen mainly intranuclearly, when growing in vivo, and exclusively in the cytoplasm, when permanently cultivated as a suspension cell strain. To investigate whether there exist differences between glycogen of nuclear and cytoplasmic origin, the ultrastructure and the biophysical and biochemical properties of glycogen from in vivo and in vitro grown HD33 ascites cells were compared. Pronounced heterogeneity and differences in glycogen particle ultrastructure were evident in situ and after isolation of the native, high-molecular polysaccharide. Nuclear glycogen contains a fraction of heavier molecules (up to 2 X 10(9)) and larger particles (up to 340 nm) which could not be found in the cytoplasmic preparations, which contained only particles smaller than 140 nm. The subparticles of beta-type are similar in both nuclear and cytoplasmic glycogen. The absorption spectra and glucose analysis after degradation with phosphorylase and debranching enzyme indicate that nuclear glycogen has a higher degree of branching, associated with a decrease in the average chain length between the branching points, and shorter external polyglucosidic chains than cytoplasmic glycogen. This is the first report about the analysis and properties of isolated nuclear glycogen.

Animals↗

PubMed1991

Development of the glycogen body of the Japanese quail, Coturnix japonica: II. Observations of electron microscopy.

Transmission electron microscopic observations of the relationships of the cells of the glycogen body and those of nervous tissue in the lumbosacral spinal cord show that one day after hatching, glycogen cells at the lateral margins of the glycogen body lie in close association with elements of the neuropil in the adjacent spinal cord. Glycogen cells and their processes appear to extend into the neuropil, where they contact other glycogen cells, blood vessels, neurons, and neuroglia. Junctional complexes and synapses occur among glycogen cells, astrocytes, and oligodendrocytes. Other indications of specialized activities were surmised by the presence of annulate lamellae in continuity with extensive arrays of smooth endoplasmic reticulum in several glycogen cells. These observations enhance our earlier views that cells of the avian glycogen body are metabolically active in the synthesis and degradation of glycogen for neuronal support and myelination in the central nervous system.

Animals↗

PubMedDate not supplied

In situ 13C NMR quantification of hepatic glycogen.

We report on the 13C NMR visibility of the C-1 glycosidic carbon of alpha-particulate glycogen in perfused rat liver. We used rats fed ad libitum, animals refed after a 48 h fast with a sucrose supplement with or without glucocorticoid treatment, and gsd/gsd rats with a hepatic glycogen storage disease due to phosphorylase kinase deficiency. Thus we studied a wide range of glycogen levels (25-140 mg/g liver). All livers were perfused with 15 mM glucose, to maintain constant glycogen levels. Failure to activate glycogen phosphorylase ensures stable glycogen levels in gsd/gsd livers. Natural abundance 13C NMR signals were calibrated against a phantom containing a fixed amount of glycogen. Accumulated free induction decays were analysed after Fourier transformation by numerical integration, or by direct analysis of the signal in the time domain using a non-iterative method based on singular value decomposition. NMR quantification of the glycogen correlated well with the chemical determination over the whole concentration range. However, the precision (reproducibility) of glycogen determinations (be it by chemical methods or by NMR spectroscopy) may pose problems. Authors should be encouraged to report systematically on the precision of their methods.

Animals↗

PubMed2001

Inactivation and thermal stabilization of glycogenin by linked glycogen.

Glycogen-free but not glycogen-bound glycogenin transglucosylates dodecyl-beta-maltoside. Furthermore, its sugar nucleotide-binding site can be photoaffinity labeled using [beta-(32)P]5-azido-UDP-glucose. Disruption with DMSO of the hydrogen bonds that stabilize the alpha-helical structure of glycogen restored the photoaffinity labeling of the glycogen-bound enzyme but not its transglucosylation activity. The larger size polysaccharide that linked to glycogenin allowed transglucosylation corresponding to that of PG-200, a proteoglycogen species of M(r) 200 kDa. PG-200 showed lower activity and increased activation energy than glycogen-free glycogenin. Heat denaturation of glycogen-free and glycogen-bound glycogenin occurred at 51 and 64 degrees C, respectively. Active glycogenin was recovered after the glycogen-bound form was heated at 60-70 degrees C and immediately cooled. Treatment at 60 degrees C of the glycogen-free enzyme resulted in inactivation. This is the first report describing the inactivation and thermal stabilization of an enzyme by linked polysaccharide.

Acrylamide↗

PubMed1996

Does preconditioning act by glycogen depletion in the isolated rat heart?

Preconditioning hastens the time to onset of ischaemic contracture and increases peak contracture in an isolated perfused rat heart, but improves recovery of function. The preconditioning ischaemic episode is also known to deplete glycogen stores. We tested whether a depletion in glycogen is related to the protection conferred by preconditioning. The isolated Langendorff perfused rat heart, with a left ventricular balloon to record function, was perfused with either glucose 11 mM, acetate 5 mM, or glucose 11 mM + insulin to alter pre-ischaemic glycogen levels prior to 30 min total global ischaemia. In addition, hearts were preconditioned by an episode of 5 min ischaemia and 5 min reperfusion. Time to onset of contracture (TOC-min), peak contracture and recovery of developed pressure after 20 min reperfusion with glucose-containing perfusate (both expressed as percentage pre-ischaemic developed pressure) were measured (n = 9-10). Parallel groups of hearts were clamped at various times for assessment of tissue metabolites. Acetate pre-perfusion reduced glycogen levels compared to glucose hearts, from 16.27 +/- 0.44 to 10.77 +/- 0.96 mumol/g wet wt. TOC was reduced and peak contracture increased, with poor functional recovery. Glucose + insulin pre-perfusion increased glycogen (21.39 +/- 1.08 mumol/g wet wt) with opposite effects on contracture, but functional recovery was still poor. Preconditioning hastened the time to onset of contracture, which could be partially attributed to glycogen depletion. Preconditioning significantly improved functional recovery in glucose hearts, but had little or no effect in the other groups. Thus the protective effect on functional recovery could not be linked to glycogen depletion. Pre-ischaemic glycogen appeared to play a dual role. When low, preconditioning was ineffective, presumably because of lack of production of glycolytic ATP, and severe contracture. When pre-ischaemic glycogen was increased, preconditioning was also relatively ineffective, presumably because of excess accumulation of the metabolites of glycogenolysis.

Acetates↗

PubMed1983

'Insulin-like' effects of lithium ion on isolated rat adipocytes. II. Specific activation of glycogen synthase.

Lithium ion, like insulin, activated adipocyte glycogen synthase with or without glucose in the medium. However, the effect of lithium ion was much greater than that of insulin under both conditions. The lithium-activated glycogen synthase was stable to both Sephadex chromatography and ethanol precipitation of the enzyme, indicating that the effect of lithium ion on glycogen synthase was through covalent modification of the enzyme. Glycogen synthase was significantly activated by lithium ion under conditions where concentrations of cellular ATP were unaffected. The effect of lithium ion on glycogen synthase was rapid and observed at concentrations as low as 1 to 3 mM, reaching a maximum at the concentration of 40 mM. It was thus the most sensitive of all the effects studied (see previous paper). Insulin further stimulated glycogen synthase at low concentrations but not at maximal concentration of lithium ion. Lithium-activated glycogen synthase was inhibited by both epinephrine and dibutyryl cyclic AMP, but was not affected by the removal of extracellular Ca++. Interestingly, lithium ion had no detectable effect on basal pyruvate dehydrogenase as well as on epinephrine-stimulated phosphorylase. The failure of lithium ion to thus mimic insulin actions on pyruvate dehydrogenase and on phosphorylase suggests that the action of lithium ion on glycogen synthase is quite specific and may be mediated by stimulating a phosphatase or by inhibiting a protein kinase acting specifically on glycogen synthase.

Adipose Tissue↗

PubMed1990

Carbohydrate supercompensation and muscle glycogen utilization during exhaustive running in highly trained athletes.

Three female and three male highly trained endurance runners with mean maximal oxygen uptake (VO2max) values of 60.5 and 71.5 ml.kg-1.min-1, respectively, ran to exhaustion at 75%-80% of VO2max on two occasions after an overnight fast. One experiment was performed after a normal diet and training regimen (Norm), the other after a diet and training programme intended to increase muscle glycogen levels (Carb). Muscle glycogen concentration in the gastrocnemius muscle increased by 25% (P less than 0.05) from 581 mmol.kg-1 dry weight, SEM 50 to 722 mmol.kg-1 dry weight, SEM 34 after Carb. Running time to exhaustion, however, was not significantly different in Carb and Norm, 77 min, SEM 13 vs 70 min, SEM 8, respectively. The average glycogen concentration following exhaustive running was 553 mmol.kg-1 dry weight, SEM 70 in Carb and 434 mmol.kg-1 dry weight, SEM 57 in Norm, indicating that in both tests muscle glycogen stores were decreased by about 25%. Periodic acid-Schiff staining for semi-quantitative glycogen determination in individual fibres confirmed that none of the fibres appeared to be glycogen-empty after exhaustive running. The steady-state respiratory exchange ratio was higher in Carb than in Norm (0.92, SEM 0.01 vs 0.89, SEM 0.01; P less than 0.05). Since muscle glycogen utilization was identical in the two tests, the indication of higher utilization of total carbohydrate appears to be related to a higher utilization of liver glycogen. We have concluded that glycogen depletion of the gastrocnemius muscle is unlikely to be the cause of fatigue during exhaustive running at 75%-80% of VO2max in highly trained endurance runners. Furthermore, diet- and training-induced carbohydrate super-compensation does not appear to improve endurance capacity in such individuals.

Adult↗

PubMed1996

Effect of exercise on glycogen metabolism in muscles of triiodothyronine-treated rats.

The aim of the present study was to examine the rate of glycogen mobilization during exercise and the rate of the postexercise glycogen replenishment in different muscle types [white (WG), and red (RG) gastrocnemius, soleus (S) and diaphragm (D)] in rats treated with triiodothyronine (T3, group T). Rats of the control group (C) were treated with saline. The animals were made to run on a treadmill set at 0 degree gradient and at a speed of 1200 m.h-1. The time taken to reach exhaustion in group C was 188 (SD 23) min, whereas in group T, it was only 63 (SD 12) min. The content of glycogen in all muscles of the rats from group T at rest and during exercise was significantly lower than in group C at each corresponding time. At exhaustion, the glycogen content was in WG(C) 34.79 (SD 4.65), (T) 20.10 (SD 4.10); in RG(C) 22.82 (SD 4.66), (T) 16.50 (SD 2.00); in S(C) 14.85 (SD 2.48), (T) 11.90 (SD 2.93); in D(C) 18.18 (SD 3.49), (T) 7.54 (SD 3.36) (mumol of glucosyl units. g-1). The amount of glycogen mobilized during exhausting exercise in RG, S and D was similar in both groups whereas in WG it was much higher in rats of group T than in group C. The concentration of glycogen returned to pre-exercise values in each muscle 3 h after exercise. The net amount of glycogen resynthesized during 3 h of recovery depended on the muscle type. It was in WG(C) 3.30, (T) 18.03; in RG(C) 21.34, (T) 25.88, in S(C) 34.00, (T) 17.68, and in D(C) 17.25, (T) 12.22 mumol of glucosyl units . g-1 (each number represents the difference between the means). It concluded that treatment with T3 markedly affects this exercise-induced metabolism of glycogen in each muscle type. From our study it is suggested that low muscle glycogen content may contribute to a reduction in exercise performance in hyperthyroidism.

Animals↗

PubMed1990

Effects of the administration of angiotensin II on cardiac glycogen metabolism in the rat.

Changes in glycogen metabolism after an intravenous injection of angiotensin II were investigated in the left and right ventricles of the rat heart, as a function of location within the ventricular wall. Hearts were cut into 100-microns thin section, all of which were analysed for glycogen content, glucose incorporation into glycogen and 2-deoxyglucose uptake and phosphorylation after the intravenous injection of 14C-labelled sugar. In control hearts, glycogen levels were uniform across the wall in both ventricles, while the rate of sugar uptake and phosphorylation, and that of glucose incorporation into glycogen, were significantly higher in the subendocardial myocardium of the left ventricular wall. After angiotensin II administration, heart glycogen levels decreased slightly in the left, but not in the right ventricle, while 2-deoxyglucose uptake and phosphorylation, and glucose incorporation into glycogen, increased 2,5- and 5-fold, respectively. With regard to the distribution across the wall of the left ventricle after angiotensin administration, glycogen levels and glucose incorporation into glycogen were uniformly distributed, whereas sugar phosphorylation was still higher in the subendocardium.

Angiotensin II↗

PubMed1988

Regulation of glycogen metabolism in rat respiratory muscles during exercise.

The effect of prolonged exercise on the glycogen level in the respiratory muscles (diaphragm--D, external intercostal--IE and internal--II) has been studied in four groups of rats: 1-control, 2-fasted for 24 h, 3-treated with nicotinic acid and 4-treated with propranolol. There was a sharp reduction in glycogen level in each muscle after 30 min exercise in the control and fasted groups. Exercise till exhaustion further lowered the glycogen level in D in the control group and in IE and II in the fasted group. In the fasted group, the level of glycogen in each muscle, at rest, and after 30 min exercise, and in IE and II muscles after exercise till exhaustion was lower than in the control group. Nicotinic acid did not affect the glycogen level either at rest or during exercise as compared with the control group. Propranolol increased the glycogen level in the muscles at rest and during 30 min exercise. It partially prevented glycogen mobilization in D and IE and fully in II during exercise till exhaustion. In the control group, 24 and 48 h after exercise till exhaustion, the level of glycogen in each muscle exceeded the resting control value. It is concluded that exercise-induced glycogen metabolism in the respiratory muscles differs in some respects from that in the limb or heart muscles.

Adrenergic beta-Antagonists↗

PubMed1985

Cytochemical studies of a glycogen-sarcoplasmic reticulum complex.

Enzymatically active cardiac sarcoplasmic reticulum (SR) fractions contain glycogen. Previous biochemical and morphological studies indicate that the glycogen particles are membrane associated. In the present study, further evidence for membrane-associated glycogen particles in these cardiac SR fractions is presented: (1) morphological parameters, (2) enzymatic digestion by glucoamylase and alpha-amylase and (3) cytochemical staining by two different methods. Dense granules comparable in size (20-30 nm diameter), electron density and substructure to glycogen particles observed in intact cardiac muscle and in glycogen preparations isolated from skeletal muscle were seen. Most of these glycogen particles were removed by amylase digestion except for glycogen particles closely adhering to vesicle membranes. Two different cytochemical techniques (bismuth subnitrate and silver proteinate) revealed a positive reaction product over the glycogen particles. These findings provide further support for the biochemical finding of a structured enzyme complex involving the SR, glycogenolytic enzymes and glycogen.

Animals↗