Effect of muscle glycogen content on glucose uptake following exercise

Fell, R. D.; Terblanché, S.E.; Ivy, John L.; Young, John C.; Holloszy, John O.

doi:10.1152/jappl.1982.52.2.434

Cited by 110 publications

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“…14 CO 2 production from [U- 14 C]glucose mainly reflects CO 2 derived from the decarboxylation of glucose in the pentose phosphate pathway and in the pyruvate dehydrogenase step in the pathway of fatty acid synthesis. Because lipid synthesis was stimulated in these cells, we used [6][7][8][9][10][11][12][13][14] C]glucose to determine whether the overexpression of myophosphorylase also stimulated glucose oxidation. We found that there was no difference in the Glucose Uptake and Phosphorylation-The effect of phosphorylase dosage on the uptake and phosphorylation of the nonmetabolizable glucose analogue 2-deoxyglucose was studied (Table III).…”

Section: Resultsmentioning

confidence: 99%

“…The system accounting for such effects appears to be located at a post-receptor level, because exercise does not affect the amount of insulin receptors or insulin-stimulated kinase activity (9,10). Breakdown of glycogen stores (11)(12)(13) or the activation of glycogen synthase (9) have been suggested as possible mediators of this phenomenon. On the other hand, even though these studies are consistent with the fact that glucose uptake is limited by glucose metabolism, other studies suggest that it is glucose transport that limits glucose uptake (14,15).…”

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confidence: 99%

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Overexpression of Muscle Glycogen Phosphorylase in Cultured Human Muscle Fibers Causes Increased Glucose Consumption and Nonoxidative Disposal

Baqué¹,

Guinovart

Gómèz-Foix

1996

Journal of Biological Chemistry

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The effect of increased expression of glycogen phosphorylase on glucose metabolism in human muscle was examined in primary cultured fibers transduced with recombinant adenovirus AdCMV-MGP encoding muscle glycogen phosphorylase. Increments of 20-fold in total enzyme activity and of 14-fold of the active form of the enzyme were associated with a 30% reduction in basal glycogen levels. Total glycogen synthase activity was doubled in AdCMV-MGP-transduced cells even though the activity ratio was decreased. Incubation with forskolin, which inactivated glycogen synthase and activated glycogen phosphorylase, induced greater net glycogenolysis in engineered cells. In unstimulated fibers, lactate production was three times higher in AdCMV-MGP fibers as compared with controls, despite similar rates of glycogenolysis. In transduced fibers incubated with 2-deoxyglucose, the level of 2-deoxyglucose 6-phosphate was about 8-fold elevated over the control even though hexokinase activity was unmodified in AdCMV-MGP fibers. Overexpression of glycogen phosphorylase also led to enhancement of [U- CO 2 formation from [6-14 C]glucose was unmodified, in AdCMV-MGP fibers. Our data show that in human skeletal muscle cells in culture, the increase in glycogen phosphorylase activity is able to up-regulate glycogen synthase activity indicating the enhancement of glycogen turnover. We suggest that the increase in glycogen phosphorylase and, thereby, in glycogen metabolism, is sufficient to enhance glucose uptake in the muscle cell. Glucose taken up by engineered muscle cells is essentially disposed of through nonoxidative metabolism and converted into lactate and lipid.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

Overexpression of Muscle Glycogen Phosphorylase in Cultured Human Muscle Fibers Causes Increased Glucose Consumption and Nonoxidative Disposal

Baqué¹,

Guinovart

Gómèz-Foix

1996

Journal of Biological Chemistry

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“…Glucose-induced insulin resistance, also referred to as "glucose toxicity," has been studied in a number of experimental models. These include rats infused with high concentrations of glucose (4 -6), perfused rat hind limb muscles (7)(8)(9)(10), isolated muscles incubated in vitro (11,12), primary cultures of rat adipocytes (13)(14)(15), and muscles of transgenic mice overexpressing GLUT1 (16,17).…”

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confidence: 99%

“…One is that accumulation of large amounts of glycogen, as a result of glucose flooding into the cell, causes insulin resistance (7,11,18), possibly as a consequence of association of GLUT4-containing vesicles with glycogen particles (19,20). A second hypothesis is that glucose toxicity is mediated by activation of protein kinase C (5,21,22) resulting in increased serine and threonine phosphorylation of the insulin receptor, with a decrease in insulin stimulation of insulin receptor tyrosine kinase (21,(23)(24)(25).…”

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confidence: 99%

Development of Glucose-induced Insulin Resistance in Muscle Requires Protein Synthesis

Kawanaka

Han

Gao

et al. 2001

Journal of Biological Chemistry

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Muscles and fat cells develop insulin resistance when exposed to high concentrations of glucose and insulin. We used an isolated muscle preparation incubated with high levels of glucose and insulin to further evaluate how glucose-induced insulin resistance (GIIR) is mediated. Incubation with 2 milliunits/ml insulin and 36 mM glucose for 5 h resulted in an ϳ50% decrease in insulinstimulated muscle glucose transport. The decrease in insulin responsiveness of glucose transport induced by glucose was not due to impaired insulin signaling, as insulin-stimulated phosphatidylinositol 3-kinase activity and protein kinase B phosphorylation were not reduced. It has been hypothesized that entry of glucose into the hexosamine biosynthetic pathway with accumulation of UDP-N-acetylhexosamines (UDP-HexNAcs) mediates GIIR. However, inhibition of the rate-limiting enzyme GFAT (glutamine:fructose-6-phosphate amidotransferase) did not protect against GIIR despite a marked reduction of UDP-HexNAcs. The mRNA synthesis inhibitor actinomycin D and the protein synthesis inhibitor cycloheximide both completely protected against GIIR despite the massive increases in UDP-HexNAcs and glycogen that resulted from increased glucose entry. Activation of AMP-activated protein kinase also protected against GIIR. These results provide evidence that GIIR can occur in muscle without increased accumulation of hexosamine pathway end products, that neither high glycogen concentration nor impaired insulin signaling is responsible for GIIR, and that synthesis of a protein with a short half-life mediates GIIR. They also suggest that dephosphorylation of a transcription factor may be involved in the induction of GIIR.

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“…In the Gdepleted hearts, the lower preischemic glycogen is almost exhausted after the initial 10 min of LFI and this leads to a stimulation of GLUT4 translocation and glucose uptake. Similarly, exercise-induced stimulation of glucose uptake in skeletal muscles is greater when glycogen content is low and unable to supply endogenous substrate for glycolysis (6,14).…”

Section: Discussionmentioning

confidence: 99%

Ischemia-induced activation of AMPK does not increase glucose uptake in glycogen-replete isolated working rat hearts

Omar¹,

Fraser²,

Clanachan³

2008

American Journal of Physiology-Heart and Circulatory Physiology

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Omar MA, Fraser H, Clanachan AS. Ischemia-induced activation of AMPK does not increase glucose uptake in glycogenreplete isolated working rat hearts. Am J Physiol Heart Circ Physiol 294: H1266-H1273, 2008. First published January 4, 2008 doi:10.1152/ajpheart.01087.2007.-Alterations in myocardial glucose metabolism are a key determinant of ischemia-induced depression of left ventricular mechanical function. Since myocardial glycogen is an important source of endogenous glucose, we compared the effects of ischemia on glucose uptake and utilization in isolated working rat hearts in which glycogen content was either replete (G replete, 114 mol/g dry wt) or partially depleted (G depleted, 71 mol/g dry wt). The effects of low-flow ischemia (LFI, 0.5 ml/min) on glucose uptake, glycogen turnover (glycogenolysis and glycogen synthesis), glycolysis, adenosine 5Ј-monophosphate-activated protein kinase (AMPK) activity, and GLUT4 translocation were measured. Relative to preischemic values, LFI caused a time-dependent reduction in glycogen content in both G-replete and G-depleted groups due to an acceleration of glycogenolysis (by 12-fold and 6-fold, respectively). In G-replete hearts, LFI (15 min) decreased glucose uptake (by 59%) and did not affect GLUT4 translocation. In G-depleted hearts, LFI also decreased initially glucose uptake (by 90%) and glycogen synthesis, but after 15 min, when glycogenolysis slowed due to exhaustion of glycogen content, glucose uptake increased (by 31%) in association with an increase in GLUT4 translocation. After 60 min of LFI, glucose uptake, glycogenolysis, and glycolysis recovered to near-preischemic values in both groups. LFI increased AMPK activity in a time-dependent manner in both groups (by 6-fold and 4-fold, respectively). Thus, when glycogen stores are replete before ischemia, ischemia-induced AMPK activation is not sufficient to increase glucose uptake. Under these conditions, an acceleration of glycogen degradation provides sufficient endogenous substrate for glycolysis during ischemia. low-flow ischemia; glucose uptake; glycogen metabolism; glucose metabolism; adenosine-5Ј-monophosphate-activated protein kinase UNDER AEROBIC CONDITIONS, ϳ95% of the energy requirement of cardiac muscle is derived from the mitochondrial oxidation of fatty acids and carbohydrates, whereas the remainder is provided by glycolysis. However, during ischemia, oxygen (O 2 ) deprivation inhibits oxidative metabolism and glycolysis becomes a major source of myocardial ATP production (44). Thus myocardial carbohydrate availability and metabolism are critical determinants of ischemic injury and postischemic left ventricular (LV) mechanical function.Glucose transport, the first step of myocardial glucose utilization, involves the facilitated diffusion of glucose across the sarcolemmal membrane. The rate of glucose transport is determined by the transmembrane concentration gradient of glucose as well as the abundance and affinity of glucose transporter proteins, GLUT1 and GLUT4 (27). Following transport, gluco...

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Effect of muscle glycogen content on glucose uptake following exercise

Cited by 110 publications

References 0 publications

Overexpression of Muscle Glycogen Phosphorylase in Cultured Human Muscle Fibers Causes Increased Glucose Consumption and Nonoxidative Disposal

Overexpression of Muscle Glycogen Phosphorylase in Cultured Human Muscle Fibers Causes Increased Glucose Consumption and Nonoxidative Disposal

Development of Glucose-induced Insulin Resistance in Muscle Requires Protein Synthesis

Ischemia-induced activation of AMPK does not increase glucose uptake in glycogen-replete isolated working rat hearts

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