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PubMed2006

Glycogen content in the cerebral cortex increases with sleep loss in C57BL/6J mice.

We hypothesized that a function of sleep is to replenish brain glycogen stores that become depleted while awake. We have previously tested this hypothesis in three inbred strains of mice by measuring brain glycogen after a 6h sleep deprivation (SD). Unexpectedly, glycogen content in the cerebral cortex did not decrease with SD in two of the strains and was even found to increase in mice of the C57BL/6J (B6) strain. Manipulations that initially induce glycogenolysis can also induce subsequent glycogen synthesis thereby elevating glycogen content beyond baseline. It is thus possible that in B6 mice, cortical glycogen content decreased early during SD and became elevated later in SD. In the present study, we therefore measured changes in brain glycogen over the course of a 6 h SD and during recovery sleep in B6 mice. We found no evidence of a decrease at any time during the SD, instead, cortical glycogen content monotonically increased with time-spent-awake and, when sleep was allowed, started to revert to control levels. Such a time-course is opposite to the one predicted by our initial hypothesis. These results demonstrate that glycogen synthesis can be achieved during prolonged wakefulness to the extent that it outweighs glycogenolysis. Maintaining this energy store seems thus not to be functionally related to sleep in this strain.

Analysis of Variance↗

PubMed1997

Glycogen utilization and ischemic injury in the isolated rat heart.

INTRODUCTION: Fasting increases myocardial glycogen content and has been shown to limit injury and improve recovery following no-flow ischaemia in the isolated heart. However, the protective role of glycogen loading per se in fed animals has been questioned by data in preconditioned animals showing that reduced glycogenolysis may be protective prior to no-flow ischemia. Therefore, we hypothesized that fasting protects the globally ischemic heart by mechanisms separate from glycogen loading. METHODS: Isolated hearts from rats fasted for 24 h were retrogradely perfused using glucose substrate and subjected to 20 min of global no-flow ischemia. Fed rats were identically perfused either under control conditions (glucose substrate) or with an intervention chosen to increase tissue glycogen (glucose plus insulin, [insulin]) prior to ischemia. Functional recovery and creatine kinase (CK) release were measured during reperfusion. Nuclear magnetic resonance spectroscopy was used to measure intracellular pH, phosphorylated glycolytic intermediates and high-energy phosphates, while the lactate and pyruvate contents of the hearts were measured prior to and at the end of ischemia. RESULTS: Heart from fasted animals had significantly increased glycogen content prior to ischemia (76.6 +/- 2 vs. 40.9 +/- 3 mumol glu/gdw in control hearts, P < 0.05) as did hearts exposed to insulin (88.6 +/- 10 mumol glu/gdw), but only hearts from fasted animals had greater glycogen utilization during ischemia. Hearts from fasted animals also had lower levels of lactate relative to pyruvate (L/P) under baseline conditions and, on reperfusion, reduced CK release (fasted: 183 +/- 48 versus control: 756 +/- 56 IU/gdw, P < 0.05). Conversely, insulin hearts had increased CK release (1831 +/- 190 IU/gdw, P < 0.001 vs control) and worse functional and metabolic recovery on reperfusion. Compared to the insulin hearts, hearts from fasted animals had both less acidosis and less rapid depletion of ATP during ischemia, as well as lower accumulation of glycolytic intermediates. CONCLUSION: Fasting protects the heart from ischemic injury and is associated with a lower L/P ratio and increased glycogen utilization during ischemia. In contrast, increasing glycogen content in hearts from fed animals using insulin limits glycogen utilization, increases ischemic injury, and impairs both functional and metabolic recovery under conditions of 20 min of global no-flow ischemia.

Animals↗

PubMed1988

A minimal model of liver glycogen metabolism; feasibility for predicting flux rates.

A minimal model of glycogen metabolism can allow the estimation of the flux rates in the glycogen pathway from the time course of the intermediates in the pathway, measured during substrate administration and hormonal stimulation. The comprehensive model of El-Refai & Bergman (Am. J. Physiol. 231, 1608, 1976) consisting of six compartments and 26 non-estimable parameters has successfully accounted for the responses of hepatic glycogenic intermediates in response to a glucose load in hepatocytes (Katz et al., J. biol. Chem. 253, 4530, 1978), in perfused liver (Nordlie et al., J. biol. Chem. 255, 1834, 1980) and during refeeding in vivo (Van DeWerve & Jeanrenaud, Am. J. Physiol. 247, E271, 1984). The comprehensive model is here reduced to a minimal model, consisting of five compartments representing extracellular and intracellular glucose, glucose-phosphate, uridine diphosphate glucose (UDPG), glycogen, and five parameters estimated from the hepatic response to a given stimulus. Estimation of these parameters requires the measurement of the net hepatic glucose balance, the net gluconeogenic flux, and the time course of glycogenic intermediates responding to a hormone or substrate stimulus. The hepatic glycogenolytic response predicted by the comprehensive model in response to an increase in glucagon is closely fitted by the minimal model. When Gaussian distributed random error was added, 0-5% SD in the glucose and glycogen compartments and 0-10% SD in the glucose-phosphate and UDPG compartments, the hepatic response predicted by the minimal model was virtually free of the added error, and the model parameters were found to be within 30% of their true values. When the minimal model was used to interpret the experimental response to an increase in glucose concentration it predicted that: (1) glucokinase can phosphorylate glucose at rates similar to maximal rates of net glycogen synthesis; (2) futile cycling at the glycogen/glucose-1-phosphate level can limit glycogen synthesis; and (3) glucose-6-phosphatase inhibition by glucose has a significant role in net glycogen synthesis.

Animals↗

PubMed1998

In vivo quantification of glucose uptake and conversion to glycogen in individual muscles of the rat following exercise.

Glycogen depletion is thought to be a potent stimulus for the substantially increased glucose fluxes observed in skeletal muscle following exercise. The aim of this study was to establish the relationships between the glycogen mass and the rates of glucose uptake (Rg') and glucose incorporation into glycogen (Rgly) in individual muscles of conscious adult Wistar rats following moderate nonexhausting treadmill exercise (15 m/min at a 10 degree slope for 45 minutes, approximately 65% VO2max). Muscle glycogen content was determined at 0, 20, 45, 90, or 135 minutes following exercise and compared with Rg' and Rgly measurements at matched times. Muscle types varied in the rate of glycogen resynthesis. Glycogen depots of glycolytic muscle (white gastrocnemius) were still significantly (P < .01) lower than preexercise levels after 135 minutes; red oxidative muscles (soleus and red gastrocnemius) were essentially repleted by 90 minutes. Immediately following exercise, Rg' and Rgly in red gastrocnemius and soleus were 42 +/- 4 and 42 +/- 5 and 36 +/- 2 and 33 +/- 7 micromol/(min . 100 g), greater than the rates induced by maximal insulin stimulation in previous studies. In red muscles, there was a strong inverse relationship between Rgly and tissue glycogen content, consistent with a dominant role for the glycogen mass in the regulation of glycogen resynthesis.

Animals↗

PubMed1997

Meal-induced changes in hepatic glycogen of fasted rats.

Hepatic metabolism of glucose and other nutrients influences feeding behavior. The present study was conducted to confirm prandial decreases in hepatic glycogen concentrations following a short-term fast. Male Sprague-Dawley rats were fasted 6-12 h during the light phase before having access to chow for one or two 20-min meals at the beginning of the dark phase. Plasma glucose and insulin concentrations in hepatic and portal venous blood and hepatic glycogen concentrations prior to and at the end of each meal were compared. Glucose concentration in the hepatic vein was greater than that in the portal vein prior to the meals but not at the end of the meal. Insulin levels were higher in the portal vein than the hepatic vein pre- and postprandially. Hepatic glycogen concentrations increased after each meal in younger (2-month-old) rats but not older (6-month-old) rats. Fasting levels of hepatic glycogen were lower in the younger rats than the older rats; however, the increase in hepatic glycogen was not due to differences in baseline glycogen concentrations at the start of the meal. The reported prandial decreases in hepatic glycogen of fasted rats were not apparent in this study. Because of the difference between 2- and 6-month-old rats in periprandial hepatic glycogen metabolism after a short-term fast, the age of the animal needs to be considered if the dynamics of liver glycogen metabolism are to be incorporated into a model of food intake regulation.

Age Factors↗

PubMed1996

Glycosomes--the organelles of glycogen metabolism.

This article reviews the data concerning the electron microscopical interpretation of glycogen. It demonstrates that glycogen in the cell is associated with the enzymes involved in its metabolism and that the glycogen-protein complex forms morphologically distinct cell organelles called glycosomes. Glycogen can be visualized in the electron microscope (EM) by histochemical procedures, or by negative staining, but it does not react with heavy metals such as uranium and lead. The protein component of glycosomes, stainable by heavy metals, appears in EM as 20-30 nm granules. While biochemical findings have long indicated the association of glycogen and protein in the cell, morphological interpretation traditionally defined the protein component of glycosomes as particles of glycogen. Accordingly, the term alpha or beta particles, introduced to define particles of glycogen, became subsequently applied to the protein component visible in sections stained by heavy metals. The history of microscopic research reveals the conditions which led to such interpretation. Morphological analysis of the reaction of glycosomes to the acids shows that glycosomes deposited free in the cytosol (lyoglycosomes) are acid labile, whereas the others (desmoglycosomes), intimately associated with different cellular structures, are acid-resistant. These 2 groups correspond to lyo- and desmoglycogen distinguished in early biochemical studies on the basis of their different resistance to the cold trichloroacetic acid. The theory of glycosomes provides a new paradigm which clarifies numerous unexplained data in the microscopic literature on glycogen, and opens a vast field for the research on the cellular metabolism of glycogen, with the use of modern molecular and cellular biology techniques.

Animals↗

PubMed2003

The 13CO2 breath test for liver glycogen oxidation after 3-day labeling of the liver with a naturally 13C-enriched diet.

OBJECTIVE: When naturally (13)C-enriched carbohydrate is used to label hepatic glycogen, (13)C-liver glycogen oxidation can be monitored subsequently by measuring the (13)C enrichment of breath CO(2) during a sedentary fast. In our previous breath test studies, we used a 1-d labeling protocol to enrich liver glycogen. Others found that after 3 d of labeling the liver glycogen (13)C enrichment is identical to the dietary carbohydrate (13)C enrichment. METHODS: We compared a diet protocol in which naturally (13)C-enriched carbohydrate was given for 3 d before the breath test with our previously applied 1-d labeling design. The (13)CO(2) breath test was combined with indirect calorimetry. The results were compared with those from our previous studies. In addition, we compared liver glycogen oxidation rates with those from our present technique and different techniques as used in other published studies. RESULTS: Six healthy volunteers were included in this study. The (13)C enrichment of breath CO(2) at plateau excretion level did not differ after 1 or 3 d on a labeling diet. However, the end of plateau time tended to be later after the 3-d diet, 14.3 h versus 12.5 to 13.5 h postprandially in the 1-d labeling studies. Also, the return to baseline time was later in the 3-d study, at 25.8 h versus 19.0 to 23.2 h postprandially after 1 d of labeling. The liver glycogen oxidation rate was similar in both techniques until 17 h postprandially. After this time the 3-d labeling protocol showed a higher level of liver glycogen oxidation. CONCLUSION: The results indicated that the labeling of liver glycogen is slightly less complete after 1 d on a (13)C-enriched diet as compared with 3-d labeling. Our (13)C breath test results compared rather well with studies from the literature using the (13)C-NMR technique, the D(2)O technique, or the (13)CO(2) breath method to measure liver glycogen oxidation.

Adult↗

PubMed1999

NMR of glycogen in exercise.

Natural-abundance 13C NMR spectroscopy is a non-invasive technique that enables in vivo assessments of muscle and/or liver glycogen concentrations. Over the last several years, 13C NMR has been developed and used to obtain information about human glycogen metabolism with diet and exercise. Since NMR is non-invasive, more data points are available over a specified time course, dramatically improving the time resolution. This improved time resolution has enabled the documentation of subtleties of muscle glycogen re-synthesis following severe glycogen depletion that were not previously observed. Muscle and liver glycogen concentrations have been tracked in several different human populations under conditions that include: (1) muscle glycogen recovery from intense localized exercise with normal insulin and with insulin suppressed; (2) muscle glycogen recovery in an insulin-resistant population; (3) muscle glycogen depletion during prolonged low-intensity exercise; (4) effect of a mixed meal on postprandial muscle and liver glycogen synthesis. The present review focuses on basic 13C NMR and gives results from selected studies.

Exercise↗

PubMed2002

Manipulations in glycogen metabolism and the failure to influence infarct size in the ischaemic rabbit heart.

BACKGROUND AND OBJECTIVE: Myocardial ischaemic preconditioning is characterized by a reduction in the rate of glycolysis. Brief myocardial ischaemia also reduces the glycogen content of the heart. The first objective was to determine whether augmenting glucose oxidation by activation of the pyruvate dehydrogenase complex would prevent the infarct limitation of ischaemic preconditioning. The second part of the study evaluates whether glycogen depletion before ischaemia mimics the infarct-limiting effect of ischaemic preconditioning. METHODS: Dichloroacetate (300 + 150 mg kg(-1)), an activator of the pyruvate dehydrogenase complex, was administered intravenously in the anaesthetized open-chest rabbit. All animals underwent 45 min of regional ischaemia and 3 h of reperfusion. Ischaemic preconditiong was elicited by 5 min of coronary occlusion. Control rabbits, those with ischaemic preconditioning with no dichloroacetate, received a saline vehicle. An isolated perfused rabbit heart model was employed to test the second hypothesis. Hearts were depleted of glycogen by perfusing them with a substrate-free buffer. Infarction was assessed by triphenyl tetrazolium chloride and area at risk determined with fluorescent particles. RESULTS: (a) Pyruvate dehydrogenase complex activation experiments. Treatment with dichloroacetate alone did not alter infarct size (58 +/- 7% control vs. 60 +/- 5% dichloroacetate). Addition of dichloroacetate did not attenuate the infarct-limiting effect of ischaemic preconditioning as evidenced by a similar reduction in infarct size in the ischaemic preconditioning group (22 +/- 5%) and in the ischaemic preconditioning + dichloroacetate group (27 +/- 7%). (b) Glycogen depletion experiments. Compared with control hearts with a normal glycogen content (4.84 +/- 0.15 mg g(-1) wet weight), glycogen depleted and ischaemic preconditioning hearts had reduced glycogen content before ischaemia (2.15 +/- 0.26, 1.62 +/- 0.17 mg g(-1) wet weight, respectively; P < 0.01). Glycogen depletion did not reduce infarct size: 25.0 +/- 4.5% cf. 27.9 +/- 3.4% in the control group. However, ischaemic preconditioning resulted in a significant reduction of infarct size (11.5 +/- 2.3% vs. 27.9 +/- 3.4% control; P < 0.01). CONCLUSIONS: Augmentation of oxidative glycolysis by dichloroacetate in in situ rabbit hearts does not alter the effect of ischaemic preconditioning, and glycogen depletion in the isolated rabbit heart does not influence infarct size after subsequent coronary occlusion.

Analysis of Variance↗

PubMed1976

Uridine 5'-(5-thio-alpha-D-glucopyranosyl pyrophosphate): chemical synthesis and activation of rat liver glycogen synthetase.

Uridine 5'-(5-thio-alpha-D-glucopyranosyl pyrophosphate), UDPTG, appears to be a potent activator of rat liver glycogen synthetase a even though it is not a substrate. At 1.0 mM, UDPTG causes over 400% activation of glycogen synthetase a activity. Activation by UDPTG is accompanied by normalization of the otherwise sigmoidal kinetics for UDPG with glycogen synthetase a and a decrease in the apparent Km for UDPG from approximately 2.0 to 0.62 mM. UDPTG inhibits catalytic activity at higher concentrations. At the concentrations examined, UDPTG has no effect on glycogen synthetase b activity. The use of glycogen synthetase free from glycogen synthetase b phosphatase and the selective inhibition of glycogen synthetase b phosphatase by 100 mM NaF-indicate that conversion of synthetase b to a is not responsible for the activation. Moreover, the use of the colorimetric assay for glycogen synthetase activity precludes effects of UDPTG on glycogen phosphorylase activity. UDPTG, chemically synthesized in 60% yield, is characterized by chromatographic and electrophoretic procedures, by its uv spectra, and by analysis of products after chemical and enzymatic hydrolysis.

Animals↗

PubMed2003

Normal hepatic glycogen storage after fasting and feeding in children and adolescents with type 1 diabetes.

OBJECTIVE: Hypoglycemia is the most important acute complication in patients with type 1 diabetes. Liver glycogen is an important storage form of glucose and thus important for maintaining glucose homeostasis. To test the hypothesis whether abnormal storage of glycogen in the liver is contributing to the risk of hypoglycemia in type 1 diabetic children and adolescents, liver glycogen was measured. STUDY DESIGN: Hepatic glycogen concentrations were measured in 19 type 1 diabetic children and adolescents as well as in 19 age-matched controls, following overnight fasting and 4 h after two standardized meals. Hepatic glycogen was assessed by natural abundance 13C nuclear magnetic resonance spectroscopy (MRS). RESULTS: Mean (+/- SEM) fasting hepatic glycogen concentrations measured in arbitrary units (au) were similar in type 1 diabetic subjects and controls (4.98 +/- 0.36 vs. 4.48 +/- 0.33 au; p = 0.31). Both groups presented with an increase in liver glycogen concentrations 4 h after the standardized meals (diabetic subjects 5.70 +/- 0.37 au, p = 0.01; controls 5.78 +/- 0.47 au, p < 0.01). Hepatic glycogen accumulation after feeding was 19.1% in diabetic children and adolescents compared with 35.8% in controls, but this difference did not reach significance. CONCLUSION: In children and adolescents with moderately controlled type 1 diabetes, hepatic glycogen stores after fasting and feeding are comparable to those of matched controls.

Adolescent↗

PubMed1983

The alpha particulate liver glycogen. A morphometric approach to the kinetics of its synthesis and degradation.

Electron micrographs of rat hepatocytes with a glycogen content between 0.36 and 2.55% (w/w) were submitted to morphometrical analysis. From the number and size of glycogen profiles, the distribution of radius and volume of glycogen alpha particles were computed. The 7-fold difference in glycogen content was accompanied by an only 1.8-fold increase in the mean volume of the particles while their number increased by a factor of 4. On the basis of these observations, it is proposed that the population of glycogen particles can be divided in two groups. The first one is made of growing particles, still associated with glycogen synthase; they are the only particles present at low glycogen concentration and their number is limited. Application of a simple mathematical model allows to estimate their number in hepatocytes as 49 X 10(12) particles . ml-1. The second group is made of glycogen particles which have reached their maximal size and the number of which is in principle unlimited. The maximal particle size is estimated to be 0.36 X 10(-15) ml, corresponding to an average molecular weight of 178 X 10(6). The average molecular weight of glycogen, as measured from the actual size of the particles, varied from 89 X 10(6) to 161 X 10(6).

Animals↗

PubMed1987

Epidermal growth factor counteracts the glycogenic effect of insulin in parenchymal hepatocyte cultures.

Rat parenchymal hepatocytes in monolayer culture were used to study the metabolic effects of epidermal growth factor (EGF) and insulin on ketogenesis, gluconeogenesis and glycogen metabolism. EGF, unlike insulin, did not inhibit ketogenesis from palmitate or gluconeogenesis from pyruvate in hepatocyte cultures. It also had no effect on these pathways in the presence of insulin. In contrast, EGF potently counteracted the stimulation of [14C]pyruvate incorporation into glycogen by insulin, and also glycogen deposition from both gluconeogenic precursors and glucose. The EGF concentration causing half-maximal effect was about 0.1 nM. The anti-glycogenic effect of EGF was observed after both long-term (24 h) and short-term (1 h) exposure to EGF, and was more marked in the presence of insulin than in its absence. EGF did not displace bound insulin, suggesting that it neither competes for the insulin receptor nor affects the affinity of the receptor for insulin. EGF did not alter cellular cyclic AMP; and inhibition of cyclic AMP phosphodiesterase activity did not prevent the anti-glycogenic effect of EGF. In liver-derived dividing epithelial cells, Hep-G2 cells and fibroblasts, which have no capacity for gluconeogenesis, EGF did not counteract the stimulatory effect of insulin on [14C]glucose incorporation into glycogen, and in the epithelial cells EGF increased [14C]glucose incorporation into glycogen. The counter-effect of EGF on the glycogenic action of insulin in parenchymal hepatocytes may be due to a direct effect on glycogen metabolism or to an interaction with the post-receptor events in insulin action.

3',5'-Cyclic-AMP Phosphodiesterases↗

PubMed1988

Enhancement of glycogen concentrations in primary cultures of rat hepatocytes exposed to glucose and fructose.

Glycogen synthesis in isolated hepatocytes can occur from glucose both by a direct mechanism and by an indirect process in which glucose is first metabolized to C3 intermediates before use for glycogenesis via gluconeogenesis. We studied the incorporation into glycogen of glucose and the gluconeogenic substrate, fructose, in primary cultures of hepatocytes from fasted rats. In the presence of insulin, both glucose and fructose promoted net deposition of glycogen; however, fructose carbon was incorporated into glycogen to a greater extent than that from glucose. When glucose and fructose were administered simultaneously, the glycogenic utilization of glucose was stimulated 2-3-fold, and that of fructose was increased by about 50%. At constant hexose concentrations, the total incorporation of carbon, and the total accumulation of glycogen mass, from glucose and fructose when present together exceeded that from either substrate alone. Fructose did not change the relative proportion of glucose carbon incorporated into glycogen via the indirect (gluconeogenic) mechanism. The synergism of glucose and fructose in glycogen synthesis in isolated rat hepatocytes in primary culture appears to result from a decrease in the rate of degradation of newly deposited glycogen, owing to (i) decreased amount of phosphorylase a mediated by glucose and (ii) noncovalent inhibition of residual phosphorylase activity by some intermediate arising from the metabolism of fructose, presumably fructose 1-phosphate.

Animals↗

PubMed1993

The contribution of pyruvate cycling to loss of [6-3H]glucose during conversion of glucose to glycogen in hepatocytes: effects of insulin, glucose and acinar origin of hepatocytes.

1. During conversion of [6-3H,U-14C]glucose to glycogen in liver, loss of 6-3H can occur either by cycling via pyruvate (between glycolysis and gluconeogenesis) or by other mechanisms. We used mercaptopicolinate, an inhibitor of phosphoenolpyruvate carboxykinase, to determine the extent to which pyruvate cycling contributes to loss of 6-3H during glucose conversion to glycogen in hepatocytes. 2. Mercaptopicolinate increased the 3H/14C ratio in glycogen during incubation of rat, guinea pig, pig and human hepatocytes with [6-3H,U-14C]glucose. The increase in the 3H/14C ratio in glycogen caused by mercaptopicolinate was greater in periportal than in perivenous rat hepatocytes, indicating that cycling of glucose via pyruvate is more prominent in cells with a higher gluconeogenic relative to glycolytic capacity. 3. The effect of mercaptopicolinate on the 3H/14C ratio in glycogen was observed both in the absence and in the presence of insulin, indicating that stimulation of glycogen synthesis by insulin is not associated with inhibition of pyruvate cycling. In rat and guinea pig but not in pig hepatocytes, the effects of mercaptopicolinate on the 3H/14C ratio in glycogen were greater at 10-15 mM glucose than at 30 mM glucose, suggesting diminished cycling via pyruvate at high glucose concentrations. 4. Insulin increased the loss of 6-3H during stimulation of conversion of glucose to glycogen in hepatocytes from all species. This was due in part to an increase in pyruvate cycling and in part to other mechanisms that are not inhibited by mercaptopicolinate. 5. These results suggest that pyruvate cycling is a significant, but not exclusive, component of the loss of 6-3H in the hepatocyte during glucose conversion to glycogen. The extent of pyruvate cycling is dependent on the acinar origin of the hepatocytes and on the glucose concentration and presence of insulin.

Aged↗

PubMed1998

Specific features of glycogen metabolism in the liver.

Although the general pathways of glycogen synthesis and glycogenolysis are identical in all tissues, the enzymes involved are uniquely adapted to the specific role of glycogen in different cell types. In liver, where glycogen is stored as a reserve of glucose for extrahepatic tissues, the glycogen-metabolizing enzymes have properties that enable the liver to act as a sensor of blood glucose and to store or mobilize glycogen according to the peripheral needs. The prime effector of hepatic glycogen deposition is glucose, which blocks glycogenolysis and promotes glycogen synthesis in various ways. Other glycogenic stimuli for the liver are insulin, glucocorticoids, parasympathetic (vagus) nerve impulses and gluconeogenic precursors such as fructose and amino acids. The phosphorolysis of glycogen is mainly mediated by glucagon and by the orthosympathetic neurotransmitters noradrenaline and ATP. Many glycogenolytic stimuli, e.g. adenosine, nucleotides and NO, also act indirectly, via secretion of eicosanoids from non-parenchymal cells. Effectors often initiate glycogenolysis cooperatively through different mechanisms.

Amino Acids↗

PubMed1986

Study on the effect of a high fat diet on diaphragm and liver glycogen and glycerides in the rat.

The present work was undertaken to study the effect of nutritional obesity induced by a high fat diet on the consumption of glycogen and glycerides in rat liver and diaphragm. Groups of rats were fed for five weeks from weaning either a fat-rich-carbohydrate (CHO)-poor diet, or a CHO-rich-fat-poor diet. Basal plasma glucose and free fatty acids (FFA) were significantly increased in the animals adapted to the fat-rich diet. Half of the rats were submitted to a 48-h fast. After fast, basal plasma glucose and immunoreactive insulin (IRI) fell significantly, whereas plasma FFA levels were higher than in the group fed the CHO-rich-fat-poor diet. In the liver, glycogen concentration fell in both groups after fast, with a glycogen breakdown of 1930 +/- 244 mumole glycogen glucose/liver in the fat-fed group vs 4636 +/- 216 mumole/liver in the CHO-fed group. Glycerides fell by 750 +/- 68 mumole glyceride glycerol/liver in the fat-fed rats while remaining unchanged (increased by 82 +/- 57 mumole/liver) in the CHO-fed group. In the diaphragm glycogen concentration also fell in both groups, with a glycogen breakdown of 6.0 +/- 0.3 mumole glycogen glucose/g wet tissue in the fat-fed rats vs 15.2 +/- 1.4 mumole/g wet tissue in the CHO-fed animals. Glycerides fell by 23.1 +/- 4.0 mumole/g wet diaphragm in the CHO-fed animals. The lower breakdown of glycogen in both liver and diaphragm of fat-fed rats demonstrates a decreased utilization of glycogen during fast, with energy consumption originating in larger part from triglycerides.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1984

Synthesis and degradation of labelled glycogen pools in preimplantation mouse embryos during short periods of in vitro culture.

The incorporation and turnover of glucose carbon by mouse embryos during short periods of in vitro culture were studied using [U-14C]glucose as marker. Particular attention was given to the synthesis and degradation of the acid-soluble and acid-insoluble glycogen pools. During a 5-h culture period, incorporation into all fractions isolated increased during development from the 1-cell to the early blastocyst stage. During maturation of the blastocyst, incorporation into acid-insoluble glycogen fell whilst that into acid-soluble glycogen continued to rise linearly over this 24 h period. At the late blastocyst stage over 80% of total glucose carbon accumulated was in this latter fraction. The decrease in acid-insoluble glycogen observed above was found to occur as a sudden change between 96 and 104 h post-hCG. The turnover of glucose carbon incorporated into the glycogen pools was studied using pulse-chase culture techniques. The results indicate that the considerable amounts of glycogen accumulated at the later stages of preimplantation development cannot act as a major energy source in vitro except in the absence of energy substrates. Under these conditions of energy starvation, however, the breakdown of acid-insoluble glycogen is inhibited. The findings show that the late preimplantation embryo accumulates large amounts of acid-soluble glycogen in vitro due to increased rate of synthesis and low rate of degradation. It is suggested that the falling levels of glycogen reported in the uterine embryo are most likely a result of environment factors other than the availability of energy substrates.

Animals↗