Effect of hypercorticism on regulation of skeletal muscle glycogen metabolism by epinephrine

1992 ◽  
Vol 262 (4) ◽  
pp. E434-E439 ◽  
Author(s):  
L. Coderre ◽  
A. K. Srivastava ◽  
J. L. Chiasson
Keyword(s):  
Skeletal Muscle ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Activity Ratio ◽  
Glycogen Synthase ◽  
Glycogen Metabolism ◽  
Dexamethasone Treatment ◽  
Fed State ◽  
Glycogen Concentration ◽  
Glycogen Synthase Activity

The effect of hypercorticism on the regulation of glycogen metabolism by epinephrine was examined in skeletal muscles using a hindlimb perfusion technique. Rats were injected with either saline or dexamethasone (0.4 mg.kg-1.day-1) for 14 days and were studied in the fed and fasted (24 h) states under saline or epinephrine (10(-7) M) treatment. In the fed state, dexamethasone administration did not affect basal glycogen concentration but decreased glycogen synthase activity ratio in white and red gastrocnemius muscles. Epinephrine failed to decrease glycogen content despite the expected activation of glycogen phosphorylase in the fed dexamethasone-treated rats. Dexamethasone treatment resulted in a threefold increase in the level of muscle adenosine, a phosphorylase a inhibitor. In control rats, fasting was associated with a decrease in muscle glycogen concentration (P less than 0.01) and with an increase in the glycogen synthase activity ratio. Dexamethasone treatment, however, totally abolished both the decreased muscle glycogen content and glycogen synthase activation observed in fasting controls. In the dexamethasone-treated group, fasting restored the glycogenolytic effect of epinephrine. Interestingly, it was associated with decreased muscle adenosine concentrations. These data indicate that, in the fed state, dexamethasone treatment inhibits skeletal muscle glycogenolysis in response to epinephrine despite phosphorylase activation and glycogen synthase inactivation. It is suggested that this abnormality could be due to the inhibition of phosphorylase a by increased muscle adenosine levels.

Effect of hypercorticism on regulation of skeletal muscle glycogen metabolism by insulin

1992 ◽  
Vol 262 (4) ◽  
pp. E427-E433 ◽  
Author(s):  
L. Coderre ◽  
A. K. Srivastava ◽  
J. L. Chiasson
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Content ◽  
Activity Ratio ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Glycogen Metabolism ◽  
Dexamethasone Treatment ◽  
Muscle Glycogen Content ◽  
Glycogen Synthase Activity ◽  
Muscle Glycogen Concentration

The effects of hypercorticism on the regulation of glycogen metabolism by insulin in skeletal muscles was examined by using the hindlimb perfusion technique. Rats were injected daily with either saline or dexamethasone (0.4 mg.kg-1.day-1) for 14 days and were studied in the fed or fasted (24 h) state under saline or insulin (1 mU/ml) treatment. In fed controls, insulin resulted in glycogen synthase activation and in enhanced glycogen synthesis. In dexamethasone-treated animals, basal muscle glycogen concentration remained normal, but glycogen synthase activity ratio was decreased in white and red gastrocnemius and plantaris muscles. Furthermore, insulin failed to activate glycogen synthase and glycogen synthesis. In the controls, fasting was associated with decreased glycogen concentrations and with increased glycogen synthase activity ratio in all four groups of muscles (P less than 0.01). Dexamethasone treatment, however, completely abolished the decrease in muscle glycogen content as well as the augmented glycogen synthase activity ratio associated with fasting. Insulin infusion stimulated glycogen synthesis in fasted controls but not in dexamethasone-treated rats. These data therefore indicate that dexamethasone treatment inhibits the stimulatory effect of insulin on glycogen synthase activity and on glycogen synthesis. Furthermore, hypercorticism suppresses the decrease in muscle glycogen content associated with fasting.

Insulin regulation of skeletal muscle glycogen metabolism

1980 ◽  
Vol 239 (1) ◽  
pp. E69-E74 ◽  
Author(s):  
J. L. Chiasson ◽  
M. R. Dietz ◽  
H. Shikama ◽  
M. Wootten ◽  
J. H. Exton
Keyword(s):  
Skeletal Muscle ◽  
Activity Ratio ◽  
Glycogen Synthase ◽  
Glycogen Metabolism ◽  
Effective Concentration ◽  
Threefold Increase ◽  
Glucose Clearance ◽  
Maximal Activation ◽  
Glycogen Synthase Activity

Using the perfused rat hindlimb preparation, the role of insulin in the regulation of glycogen metabolism in voluntary skeletal muscle has been characterized. A maximally effective concentration of insulin (1 mU/ml) caused a threefold increase in glucose clearance by 5 min. However, the -glucose-6-P/+glucose-6-P activity ratio of glycogen synthase was not significantly increased before 20 min. Insulin concentrations as low as 0.1 mU/ml significantly modified the glycogen synthase activity ratio and the half-maximal activation constant (A0.5) for glucose-6-P at 30 min, but had no effect on tissue cAMP. These changes were not dependent on the presence of glucose and were not modified by fasting. These results indicate that high physiological concentrations of insulin activate glycogen synthase in voluntary skeletal muscle and that this effect is independent of changes in glucose uptake or tissue cyclic AMP.

scholarly journals Dietary whey protein increases liver and skeletal muscle glycogen levels in exercise-trained rats

2005 ◽  
Vol 93 (4) ◽  
pp. 439-445 ◽  
Author(s):  
Masashi Morifuji ◽  
Kensuke Sakai ◽  
Chiaki Sanbongi ◽  
Katsumi Sugiura
Keyword(s):  
Skeletal Muscle ◽  
Whey Protein ◽  
Muscle Glycogen ◽  
Dietary Protein ◽  
Glycogen Content ◽  
Glycogen Synthase ◽  
Casein Diet ◽  
Skeletal Muscle Glycogen ◽  
Protein Group ◽  
Glycogen Synthase Activity

We investigated the effect of different types of dietary protein on glycogen content in liver and skeletal muscle of exercise-trained rats. Twenty-four male Sprague-Dawley rats (approximately 100 g; n 6 per group) were divided into sedentary or exercise-trained groups with each group being fed either casein or whey protein as the source of dietary protein. Rats in the exercised groups were trained during 2 weeks using swimming exercise for 120 min/d, 6 d/week. Exercise training resulted in an increase in the skeletal muscle glycogen content. Furthermore, the whey protein group significantly increased the skeletal muscle glycogen content compared with the casein group. The increase in glycogen content in liver was significantly greater in rats fed the whey protein diet compared with those fed the casein diet. We also found that the whey protein diet increased the activity of liver glucokinase, whereas it decreased the activities of 6-phosphofructokinase and pyruvate kinase compared with the casein diet. However, hepatic total glycogen synthase activity and mRNA expression were similar with the two diets. In the skeletal muscle, whey protein decreased only 6-phosphofructokinase activity compared with casein. Total glycogen synthase activity in the skeletal muscle in the whey protein group was significantly higher than that in the casein group. The present study is the first to demonstrate that a diet based on whey protein may increase glycogen content in liver and skeletal muscle of exercise-trained rats. We also observed that whey protein regulated glycogen metabolism in these two tissues by different mechanisms.

Time course of insulin sensitivity and skeletal muscle glycogen synthase activity after a single bout of exercise in horses

2007 ◽  
Vol 103 (3) ◽  
pp. 1063-1069 ◽  
Author(s):  
Shannon E. Pratt ◽  
Raymond J. Geor ◽  
Lawrence L. Spriet ◽  
L. Jill McCutcheon
Keyword(s):  
Skeletal Muscle ◽  
Insulin Sensitivity ◽  
Muscle Glycogen ◽  
Time Course ◽  
Glycogen Content ◽  
Activity Ratio ◽  
Glycogen Synthase ◽  
Muscle Glycogen Content ◽  
Skeletal Muscle Glycogen ◽  
Single Bout

The time course of insulin sensitivity, skeletal muscle glycogen and GLUT4 content, and glycogen synthase (GS) activity after a single bout of intense exercise was examined in eight horses. On separate days, a euglycemic-hyperinsulinemic clamp (EHC) was undertaken at 0.5, 4, or 24 h after exercise or after 48 h of rest [control (Con)]. There was no increase in mean glucose infusion rate (GIR) with exercise (0.5-, 4-, and 24-h trials), and GIR was significantly decreased at 0.5 h postexercise (GIR: 8.6 ± 2.7, 6.7 ± 2.0, 9.0 ± 2.0, and 10.6 ± 2.2 mg·kg−1·min−1 for Con and at 0.5, 4, and 24 h, respectively). Before each EHC, muscle glycogen content (mmol glucosyl units/kg dry muscle) was higher ( P < 0.05) for Con (565 ± 102) than for other treatments (317 ± 84, 362 ± 79, and 382 ± 74 for 0.5, 4, and 24 h, respectively) and muscle GLUT4 content was unchanged. Pre-EHC active-to-total GS activity ratio was higher ( P < 0.05) at 0.5, 4, and 24 h after exercise than in Con. Post-EHC active GS and GS activity ratio were higher ( P < 0.05) in Con and at 24 h. There was a significant inverse correlation ( r = −0.43, P = 0.02) between glycogen content and GS activity ratio but no relationship between GS activity and GIR. The lack of increase in insulin sensitivity, determined by EHC, after exercise that resulted in a significant reduction in muscle glycogen content is consistent with the slow rate of muscle glycogen resynthesis observed in equine studies.

Insulin promotes glycogen synthesis in the absence of GSK3 phosphorylation in skeletal muscle

2008 ◽  
Vol 294 (1) ◽  
pp. E28-E35 ◽  
Author(s):  
Michale Bouskila ◽  
Michael F. Hirshman ◽  
Jørgen Jensen ◽  
Laurie J. Goodyear ◽  
Kei Sakamoto
Keyword(s):  
Skeletal Muscle ◽  
Glucose Uptake ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Wild Type ◽  
Muscle Glycogen Synthesis ◽  
Mutant Forms

Insulin promotes dephosphorylation and activation of glycogen synthase (GS) by inactivating glycogen synthase kinase (GSK) 3 through phosphorylation. Insulin also promotes glucose uptake and glucose 6-phosphate (G-6- P) production, which allosterically activates GS. The relative importance of these two regulatory mechanisms in the activation of GS in vivo is unknown. The aim of this study was to investigate if dephosphorylation of GS mediated via GSK3 is required for normal glycogen synthesis in skeletal muscle with insulin. We employed GSK3 knockin mice in which wild-type GSK3α and -β genes are replaced with mutant forms (GSK3α/βS21A/S21A/S9A/S9A), which are nonresponsive to insulin. Although insulin failed to promote dephosphorylation and activation of GS in GSK3α/βS21A/S21A/S9A/S9Amice, glycogen content in different muscles from these mice was similar compared with wild-type mice. Basal and epinephrine-stimulated activity of muscle glycogen phosphorylase was comparable between wild-type and GSK3 knockin mice. Incubation of isolated soleus muscle in Krebs buffer containing 5.5 mM glucose in the presence or absence of insulin revealed that the levels of G-6- P, the rate of [14C]glucose incorporation into glycogen, and an increase in total glycogen content were similar between wild-type and GSK3 knockin mice. Injection of glucose containing 2-deoxy-[3H]glucose and [14C]glucose also resulted in similar rates of muscle glucose uptake and glycogen synthesis in vivo between wild-type and GSK3 knockin mice. These results suggest that insulin-mediated inhibition of GSK3 is not a rate-limiting step in muscle glycogen synthesis in mice. This suggests that allosteric regulation of GS by G-6- P may play a key role in insulin-stimulated muscle glycogen synthesis in vivo.

Increased concentrations of glycogen synthase protein in skeletal muscle of patients with NIDDM

1995 ◽  
Vol 269 (1) ◽  
pp. E27-E32 ◽  
Author(s):  
M. Lofman ◽  
H. Yki-Jarvinen ◽  
M. Parkkonen ◽  
J. Lindstrom ◽  
L. Koranyi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glucose Metabolism ◽  
Protein Concentration ◽  
Glycogen Synthase ◽  
Glycogen Metabolism ◽  
Dependent Diabetes Mellitus ◽  
Euglycemic Hyperinsulinemic Clamp ◽  
Control Subjects ◽  
Significant Difference ◽  
Glycogen Synthase Activity

To examine whether changes in the glycogen synthase protein concentration contribute to impaired insulin-stimulated glycogen metabolism in patients with noninsulin-dependent diabetes mellitus (NIDDM), muscle biopsies were taken before and after a 4-h euglycemic hyperinsulinemic clamp to measure glycogen synthase activity and glycogen synthase protein concentrations in 14 patients with NIDDM and in 17 control subjects. Nonoxidative glucose metabolism was reduced by 64% in patients with NIDDM compared with control subjects and correlated with insulin-stimulated glycogen synthase activity (r = 0.55, P < 0.05). The concentration of glycogen synthase protein in skeletal muscle was higher in patients with NIDDM than in control subjects (6.75 +/- 0.88 vs. 4.41 +/- 0.50 counts.min-1.micrograms protein-1, P < 0.05), whereas there was no significant difference in glycogen synthase mRNA concentration between the two groups. The glycogen synthase protein concentration correlated inversely with the rate of nonoxidative glucose metabolism (r = -0.63, P < 0.05). These findings indicate that the amount of glycogen synthase protein is increased in skeletal muscle of patients with NIDDM. The increase in the glycogen synthase protein may serve to compensate for a functional defect in the activation of the enzyme by insulin.

Liver and peripheral tissue glycogen metabolism in obese mice: effect of a mixed meal

1993 ◽  
Vol 265 (5) ◽  
pp. E743-E751
Author(s):  
C. Chen ◽  
P. F. Williams ◽  
I. D. Caterson
Keyword(s):  
Skeletal Muscle ◽  
Adipose Tissue ◽  
Cardiac Muscle ◽  
White Adipose Tissue ◽  
Glycogen Content ◽  
Glycogen Synthase ◽  
Glycogen Metabolism ◽  
Glycogen Storage ◽  
Obese Mice ◽  
Entire Study

Glycogen metabolism in the liver, skeletal muscle, cardiac muscle, and white adipose tissue was studied in gold thioglucose (GTG) obese mice after fasting and during refeeding. Prolonged (48 h) fasted control and GTG mice were refed with standard laboratory diet for 24 h. During fasting and refeeding, the changes in glycogen content and the activity of glycogen synthase I and R and phosphorylase alpha in the liver were similar in lean and GTG mice. However, the glycogen storage in the livers from GTG mice was always greater than that in lean animals. In GTG mice the activity of liver glycogen synthase I and R was significantly higher than that in lean animals 3 and 6 h after refeeding. The activity of liver phosphorylase alpha in GTG mice was higher than that in lean mice after refeeding. There were no significant differences in the glycogen content of white adipose tissue, cardiac muscle, and skeletal muscle from lean and GTG mice during the entire study. The results of this study suggest that increased glycogen storage in the liver is a major alteration in nonoxidative glucose metabolism and contributes to the development of insulin resistance and glucose intolerance in GTG obese mice.

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