Disorders of Muscle Glycogen Metabolism

2013 ◽  
pp. 254-264 ◽  
Author(s):  
John Vissing
1992 ◽  
Vol 267 (35) ◽  
pp. 25129-25134 ◽  
Author(s):  
A.M. Gómez-Foix ◽  
W.S. Coats ◽  
S Baqué ◽  
T Alam ◽  
R.D. Gerard ◽  
...  

2004 ◽  
Vol 378 (3) ◽  
pp. 1073-1077 ◽  
Author(s):  
Carlos LERÍN ◽  
Eulàlia MONTELL ◽  
Teresa NOLASCO ◽  
Mar GARCÍA-ROCHA ◽  
Joan J. GUINOVART ◽  
...  

Pharmacological inhibition of liver GP (glycogen phosphorylase), which is currently being studied as a treatment for Type II (non-insulin-dependent) diabetes, may affect muscle glycogen metabolism. In the present study, we analysed the effects of the GP inhibitor CP-91149 on non-engineered or GP-overexpressing cultured human muscle cells. We found that CP-91149 treatment decreased muscle GP activity by (1) converting the phosphorylated AMP-independent a form into the dephosphorylated AMP-dependent b form and (2) inhibiting GP a activity and AMP-mediated GP b activation. Dephosphorylation of GP was exerted, irrespective of incubation of the cells with glucose, whereas inhibition of its activity was synergic with glucose. As expected, CP-91149 impaired the glycogenolysis induced by glucose deprivation. CP-91149 also promoted the dephosphorylation and activation of GS (glycogen synthase) in non-engineered or GP-overexpressing cultured human muscle cells, but exclusively in glucose-deprived cells. However, this inhibitor did not activate GS in glucose-deprived but glycogen-replete cells overexpressing PTG (protein targeting to glycogen), thus suggesting that glycogen inhibits the CP-91149-mediated activation of GS. Consistently, CP-91149 promoted glycogen resynthesis, but not its overaccumulation. Hence, treatment with CP-91149 impairs muscle glycogen breakdown, but enhances its recovery, which may be useful for the treatment of Type II (insulin-dependent) diabetes.


2001 ◽  
Vol 52 (7) ◽  
pp. 723 ◽  
Author(s):  
G. E. Gardner ◽  
R. H. Jacob ◽  
D. W. Pethick

This study was a series of experiments designed to test the influence of supplemental magnesium oxide (MgO) on muscle glycogen concentration in sheep exposed to stress (exercise) and the commercial slaughter process, and to test the effectiveness of this supplement in the commercial scenario. In Expt 1, Merino wethers maintained on a mixed ration (metabolisable energy 11 MJ/kg and crude protein 16.3% in DM) were supplemented with MgO at the rate of 0%, 0.5%, or 1% of their ration for 10 days prior to a single bout of exercise and for 10 days prior to slaughter at a commercial abattoir. The exercise regimen consisted of 4 intervals of 15 min, with muscle biopsies taken by biopsy drill from the m. semimembranosis (SM) and m. semitendinosis (ST) pre-exercise and immediately post-exercise, and at 36 and 72 h post-exercise. Muscle biopsies were also taken 1 week prior to slaughter from the SM and ST, with further samples taken approximately 30 min post-slaughter. Ultimate pH (pHu) of the SM, ST, and m. longissimus dorsi (LD) was measured 48 h after slaughter. Sheep supplemented with MgO lost less muscle glycogen in the ST during exercise, and repleted more muscle glycogen in the SM during the post-exercise repletion phase, than unsupplemented sheep. The supplemented animals also had higher muscle glycogen concentrations in the ST at slaughter. In Expt 2, MgO was administered to Merino wether lambs for 4 days prior to slaughter in the form of a water-borne slurry at a rate equivalent to 1% of their ration. This treatment resulted in significantly reduced muscle glycogen concentrations in both the SM and ST at slaughter. In Expts 3–5, MgO was used as an ‘in-feed’ supplement in the commercial scenario. In each case, slaughter-weight Merino lambs were supplemented with MgO at the rate of 1% of their ration for 4 days prior to commercial slaughter. Positive responses were seen in 2 of the 3 experiments, with increased glycogen concentrations and a reduced pHu. The animals that demonstrated no response to MgO had the lowest pHu after slaughter, suggesting a minimal stress load, thus providing very little scope for an effect of the MgO supplement. We conclude that MgO can reduce the effects of exercise, leading to a subsequent reduction in glycogen loss, and an increase in the rate of glycogen repletion in skeletal muscle following exercise. The results support MgO supplementation as a viable option for reducing the stress associated with commercial slaughter.


Cells ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 883
Author(s):  
Marta Migocka-Patrzałek ◽  
Magdalena Elias

Glycogen phosphorylase (PG) is a key enzyme taking part in the first step of glycogenolysis. Muscle glycogen phosphorylase (PYGM) differs from other PG isoforms in expression pattern and biochemical properties. The main role of PYGM is providing sufficient energy for muscle contraction. However, it is expressed in tissues other than muscle, such as the brain, lymphoid tissues, and blood. PYGM is important not only in glycogen metabolism, but also in such diverse processes as the insulin and glucagon signaling pathway, insulin resistance, necroptosis, immune response, and phototransduction. PYGM is implicated in several pathological states, such as muscle glycogen phosphorylase deficiency (McArdle disease), schizophrenia, and cancer. Here we attempt to analyze the available data regarding the protein partners of PYGM to shed light on its possible interactions and functions. We also underline the potential for zebrafish to become a convenient and applicable model to study PYGM functions, especially because of its unique features that can complement data obtained from other approaches.


1995 ◽  
Vol 25 (9) ◽  
pp. 693-698 ◽  
Author(s):  
C. SCHALIN-JÄNTTI ◽  
E. LAURILA ◽  
M. LÖFMAN ◽  
L. C. GROOP

2014 ◽  
Vol 54 (10) ◽  
pp. 1575 ◽  
Author(s):  
G. E. Gardner ◽  
P. McGilchrist ◽  
D. W. Pethick

The biochemistry of glycogen metabolism is well characterised, having been extensively studied in laboratory rodents and humans, and from this stems the bulk of our knowledge regarding the metabolism of glycogen in ruminants. With respect to intermediary metabolism, the key tissues include the liver and muscle. The liver glycogen depot plays a central role in intermediary metabolism, storing and mobilising glycogen during the fed and fasted metabolic states, with these responses modulated during pregnancy, lactation, and exercise. Alternatively, the muscle glycogen depot is particularly important for local energy homeostasis, and is likely to be less important as a key post-prandial sink for blood glucose given the reduced absorption of glucose from the gut in ruminant animals. Yet similar to the liver, this depot is also in a constant state of turnover, with the muscle glycogen concentration at any point in time a reflection of the rates of glycogen synthesis and degradation. Muscle glycogen metabolism attracts particular attention given its importance for post-mortem acidification of muscle tissue, with a shortage at slaughter leading to dark cutting meat. Simplistically the concentration of muscle glycogen at slaughter is a function of two key factors, the on-farm starting levels of glycogen minus the amount depleted during the pre-slaughter phase. On-farm concentrations of muscle glycogen are largely a reflection of metabolisable energy intake driving increased rates of muscle glycogen synthesis. Compared with simple-stomached species the rate of glycogen synthesis within ruminants is relatively low. Yet there also appears to be differences between sheep and cattle when fed diets of similar metabolisable energy, with cattle repleting muscle glycogen more slowly after depletion through exercise. While metabolisable energy intake is the key driver, genetic and age-related factors have also been shown to influence glycogen repletion. The amount of muscle glycogen depleted during the pre-slaughter phase is largely associated with stress and adrenaline release, and several recent studies have characterised the importance of factors such as exercise, age and genetics which modulate this stress response. This paper presents a summary of recent experiments in both cattle and sheep that highlight current developments in the understanding of this trait.


2019 ◽  
pp. 17-24
Author(s):  
Daphna Atar-Zwillenberg ◽  
Michael Atar ◽  
Gianni Morson ◽  
Udo Spornitz

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.


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