Control of Glycogen Synthesis by Glucose, Glycogen, and Insulin in Cultured Human Muscle Cells

Halse, Reza; Bonavaud, Sylvie; Armstrong, Jane L.; McCormack, James G.; Yeaman, Stephen J.

doi:10.2337/diabetes.50.4.720

Cited by 53 publications

(51 citation statements)

References 39 publications

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“…Glucose withdrawal from myoblasts for 5 h caused a 1.6-fold increase in the rate of 2-deoxyglucose uptake, as compared with cells maintained in glucose-containing media. This is consistent with an earlier work (18). The basal rate of 2-deoxyglucose uptake was unaffected by the presence of CP-91149 during glucose deprivation; however, a slight decrease was observed in the rate of uptake following glucose-deprivation (644.7…”

Section: Resultssupporting

confidence: 92%

“…The ability of CP-91149 to affect intracellular glycogen levels was assessed in human myoblasts in culture (Table 1). Incubation of myoblasts in the absence of glucose for 2 h caused an ϳ25% decrease in intracellular glycogen concentrations, consistent with an earlier work (18). This decrease was essentially blocked by 10 and 100 mol/l CP-91149, indicating that this compound can also inhibit the human muscle isoform of glycogen phosphorylase.…”

Section: Resultssupporting

confidence: 90%

“…Activation of GS by glucose following time-dependent decrease in cellular glycogen in response to glucose deprivation has been reported in human muscle cells in culture (18), suggesting that induced changes in cellular glycogen content might be responsible for alterations in the activity of GS. However, it was unclear whether changes in the activity state of GS were a direct result of alterations in the concentration of cellular glycogen or of other metabolic consequences of glucose deprivation.…”

Section: Resultsmentioning

confidence: 89%

“…Following readdition of glucose, a dramatic and sustained increase in GS activity is observed, which is independent of GSK3 inactivation. Indeed, the mechanism leading to GS activation in this model is independent of that utilized by insulin (18).…”

mentioning

confidence: 87%

“…Another possibility is that decreased cellular glycogen content may directly lead to GS activation. We have recently developed a model system in vitro using cultured human muscle, in which glycogen depletion is achieved by glucose deprivation (18). Following readdition of glucose, a dramatic and sustained increase in GS activity is observed, which is independent of GSK3 inactivation.…”

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confidence: 99%

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Regulation of Glycogen Synthase by Glucose and Glycogen

Halse

Fryer²,

McCormack³

et al. 2003

Diabetes

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We report here use of human myoblasts in culture to study the relationships between cellular glycogen concentrations and the activities of glycogen synthase (GS) and AMP-activated protein kinase (AMPK). Incubation of cells for 2 h in the absence of glucose led to a 25% decrease in glycogen content and a significant decrease in the fractional activity of GS. This was accompanied by stimulation of both the ␣1 and ␣2 isoforms of AMPK, without significant alterations in the ratios of adenine nucleotides. When glucose was added to glycogen-depleted cells, a rapid and substantial increase in GS activity was accompanied by inactivation of AMPK back to basal values. Inclusion of the glycogen phosphorylase inhibitor, CP-91149, prevented the loss of glycogen during glucose deprivation but not the activation of AMPK. However, in the absence of prior glycogen breakdown, glucose treatment failed to activate GS above control values, indicating the crucial role of glycogen content. Activation of AMPK by either 5-aminoimidazole-4-carboxamide 1-␤-D-ribofuranoside (AICAR) or hydrogen peroxide was also associated with a decrease in the activity ratio of GS. AICAR treatment had no effect on total cellular glycogen content but led to a modest increase in glucose uptake. These data support a role for AMPK in both stimulating glucose uptake and inhibiting GS in intact cells, thus promoting glucose flux through glycolysis. Diabetes 52:9 -15, 2003

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Section: Resultssupporting

confidence: 92%

Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 89%

mentioning

confidence: 87%

mentioning

confidence: 99%

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Regulation of Glycogen Synthase by Glucose and Glycogen

Halse

Fryer²,

McCormack³

et al. 2003

Diabetes

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Current Awareness

2001

Diabetes Metabolism Res

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In order to keep subscribers up‐to‐date with the latest developments in their field, John Wiley & Sons are providing a current awareness service in each issue of the journal. The bibliography contains newly published material in the field of diabetes/metabolism. Each bibliography is divided into 17 sections: 1 Books, Reviews & Symposia; 2 General; 3 Genetics; 4 Epidemiology; 5 Immunology; 6 Prediction; 7 Prevention; 8 Intervention: a) General; b) Pharmacology; 9 Pathology: a) General; b) Cardiovascular; c) Neurological; d) Renal; 10 Endocrinology & Metabolism; 11 Nutrition; 12 Animal Studies; 13 Techniques. Within each section, articles are listed in alphabetical order with respect to author (9 Weeks journals ‐ Search completed at 30th May 2001)

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Role of glycogen content in insulin resistance in human muscle cells

Litherland

Morris

Walker

et al. 2006

Journal Cellular Physiology

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We have used primary human muscle cell cultures to investigate the role of glycogen loading in cellular insulin resistance. Insulin pre-treatment for 2 h markedly impaired insulin signaling, as assessed by protein kinase B (PKB) phosphorylation. In contrast, insulin-dependent glycogen synthesis, glycogen synthase (GS) activation, and GS sites 3 de-phosphorylation were impaired only after 5 h of insulin pre-treatment, whereas 2-deoxyglucose transport was only decreased after 18 h pre-treatment. Insulin-resistant glycogen synthesis was associated closely with maximal glycogen loading. Both glucose limitation and 5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranoside (AICAR) treatment during insulin pre-treatment curtailed glycogen accumulation, and concomitantly restored insulin-sensitive glycogen synthesis and GS activation, although GS de-phosphorylation and PKB phosphorylation remained impaired. Conversely, glycogen super-compensation diminished insulin-sensitive glycogen synthesis and GS activity. Insulin acutely promoted GS translocation to particulate subcellular fractions; this was abolished by insulin pre-treatment, as was GS dephosphorylation therein. Limiting glycogen accumulation during insulin pre-treatment re-instated GS dephosphorylation in particulate fractions, whereas glycogen super-compensation prevented insulin-stimulated GS translocation and dephosphorylation. Our data suggest that diminished insulin signaling alone is insufficient to impair glucose disposal, and indicate a role for glycogen accumulation in inducing insulin resistance in human muscle cells.

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Control of Glycogen Synthesis by Glucose, Glycogen, and Insulin in Cultured Human Muscle Cells

Cited by 53 publications

References 39 publications

Regulation of Glycogen Synthase by Glucose and Glycogen

Regulation of Glycogen Synthase by Glucose and Glycogen

Current Awareness

Role of glycogen content in insulin resistance in human muscle cells

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