Regulation of GLUT4 protein expression and glycogen storage after prolonged exercise

Kuo, Chia‐Hua; Browning, Karen S.; Ivy, John L.

doi:10.1046/j.1365-201x.1999.00489.x

Cited by 74 publications

(85 citation statements)

References 39 publications

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“…The similar level of expression and activation of insulin-signaling components and GLUT4 protein in the face of the different insulin sensitivity in rested and exercised muscle shows that increased GLUT4 protein expression is not a prerequisite for increased insulin sensitivity of glucose uptake, as recently suggested (40,41). In addition, the findings raise the possibility that exercise modulates insulin-signaling components further "downstream."…”

Section: Discussionsupporting

confidence: 60%

“…Protein expression. Studies performed in rodent skeletal muscle have indicated that GLUT4 mRNA and protein expression are rapidly increased after intensive exercise (40,41). By immunoblotting, the insulin receptor (1.00 ± 0.10 vs. 1.11 ± 0.17), IRS-1 (2.68 ± 0.67 vs. 2.26 ± 0.62), p85 (6.3 ± 1.2 vs. 5.7 ± 0.8), Akt (0.20 ± 0.03 vs. 0.24 ± 0.03), and GLUT4 (4.4 ± 0.6 vs. 5.4 ± 0.5) protein expression were not significantly different between the rested and exercised muscle (data are means ± SE, n = 7).…”

Section: R E S U Lt Smentioning

confidence: 99%

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Insulin signaling and insulin sensitivity after exercise in human skeletal muscle.

Wojtaszewski

Hansen²,

Gade³

et al. 2000

Diabetes

315

288

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Muscle glucose uptake, glycogen synthase activity, and insulin signaling were investigated in response to a physiological hyperinsulinemic (600 p m o l / l ) -e u g l y c e m i c clamp in young healthy subjects. Four hours before the clamp, the subjects performed one-legged exercise for 1 h. In the exercised leg, insulin more rapidly activated glucose uptake (half activation time [t 1 / 2 ] = 11 vs. 3 4 min) and glycogen synthase activity (t 1 / 2 = 8 vs. 17 min), and the magnitude of increase was two-to fourfold higher compared with the rested leg. However, prior exercise did not result in a greater or more rapid increase in insulin-induced receptor tyrosine kinase ( I RTK) activity (t 1 / 2 = 50 min), serine phosphorylation of Akt (t 1 / 2 = 1-2 min), or serine phosphorylation of glycogen synthase kinase-3 (GSK-3) (t 1 / 2 = 1-2 min) or in a larger or more rapid decrease in GSK-3 activity (t 1 / 2 = 3-8 min). Thirty minutes after cessation of insulin infusion, glucose uptake, glycogen synthase a c t i v i t y, and signaling events were partially reversed in both the rested and the exercised leg. We conclude the following: 1) physiological hyperinsulinemia induces sustained activation of insulin-signaling molecules in human skeletal muscle; 2) the more distal insulinsignaling components (Akt, GSK-3) are activated much more rapidly than the proximal signaling molecules (1). In human skeletal muscle, the effects of exercise per se on muscle glucose transport are relatively short-lived (2-4 h), whereas the enhanced sensitivity for glucose transport activation by insulin has been observed >48 h after an exercise bout in human subjects (3-5). In rat skeletal muscle, it has been demonstrated that there is a marked increase in insulin sensitivity for both glucose transport and glycogen synthase activation after exercise (2,6). These changes facilitate glycogen resynthesis, and they may be the mechanism by which muscle glycogen storage is increased above pre-exercise values, known as "supercompensation" (7,8). Whether prior exercise also increases the sensitivity for glycogen synthase activation by insulin in human skeletal muscle is unknown.We have previously hypothesized that an upregulation of insulin signaling is involved in the increased insulin sensitivity after exercise (9). However, if humans are subjected to physiological hyperinsulinemia or if rat muscles are incubated in the presence of insulin 3-4 h after exercise, insulin receptor tyrosine kinase (IRTK) a c t i v i t y, insulin receptor substrate 1 (IRS-1) tyrosine phosphorylation, and phosphatidylinositol (PI) 3-kinase activity are not enhanced in skeletal muscle (9,10). This suggests that exercise may modulate insulin signaling further downstream or affect processes directly involved in glucose transporter translocation and activation.Signaling involving D-3 phosphorylated inositol lipids, generated by the action of PI 3-kinases, has been suggested to lead to the metabolic effects of insulin, including the activation of glucose transport and glycogen sy...

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Section: Discussionsupporting

confidence: 60%

Section: R E S U Lt Smentioning

confidence: 99%

Insulin signaling and insulin sensitivity after exercise in human skeletal muscle.

Wojtaszewski

Hansen²,

Gade³

et al. 2000

Diabetes

315

288

View full text Add to dashboard Cite

show abstract

“…When carbohydrate is available, those polysome-associated GLUT4 mRNAs could be physically protected from intracellular degradation machinery and retained in order to be reutilized in translational cycle during the recovery period. In this study, GLUT4 protein level in human skeletal muscle was not altered by both LGI and HGI diets, suggesting that the increases in GLUT4 protein by post-exercise high-carbohydrate diets may take longer in humans than in rats (Kuo et al, 1999a).…”

Section: Discussionmentioning

confidence: 78%

“…In humans, GLUT4 mRNA levels can be increased rapidly after a single bout of prolonged exercise (Kraniou et al, 2006), and downregulated by a high-carbohydrate diet (Cheng et al, 2005). In the rat skeletal muscle, post-exercise carbohydrate supplementation can induce a protracted GLUT4 protein increase for several hours, whereas GLUT4 mRNA transiently downregulates below baseline in 90 min (Kuo et al, 1999a).…”

Section: Introductionmentioning

confidence: 99%

Effect of dietary glycemic index on substrate transporter gene expression in human skeletal muscle after exercise

et al. 2009

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Background/Objectives: Skeletal muscle plays important role in the regulation of whole-body metabolism. In skeletal muscle, uptakes of glucose and fatty acid from circulation are facilitated by transmembrane substrate transporters GLUT4 and FAT/ CD36, respectively. The aim of this study was to determine the effect of dietary glycemic index (GI) on GLUT4 and FAT/CD36 gene expressions in human skeletal muscle after a single bout of exercise. Subjects/Methods: Eight male subjects completed a 60-min cycling exercise at 75% maximal oxygen consumption (VO 2 max ), and were immediately fed an isocaloric meal containing either high-GI (HGI) or low-GI (LGI) diets, with similar proportions of carbohydrate, fat and protein in a crossover design. Muscle samples from deep vastus lateralis were taken by needle biopsy immediately after exercise and 3 h after exercise. Results: After exercise, the HGI diet produced significantly greater glucose and insulin responses compared with the LGI diet, as indicated by the greater area under the curves. Both diets resulted in rapid reductions in plasma fatty acid and glycerol below fasting level. GLUT4 mRNA was downregulated by both HGI and LGI diets to a comparable extent, whereas GLUT4 protein levels were not changed during this short period. FAT/CD36 mRNA and protein levels were substantially decreased with the HGI diet below baseline, but not with the LGI diet. Conclusion: This study found a significant dietary GI effect on post-exercise FAT/CD36 gene expression in human skeletal muscle. This result implicates that the differences in dietary GI are sufficient to alter fat metabolism.

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“…With the decrease in LDH-B and the increase in LDH-A, the shift to glycolytic metabolism in the soleus following functional overload would allow energy to be produced rapidly. Changes in muscle loading also alters the muscle's overall glycolytic capacity, which can be regulated pretranslationally (19,28). LDH enzymatic activity was also altered at the onset of disuse.…”

Section: Discussionmentioning

confidence: 99%

Lactate dehydrogenase expression at the onset of altered loading in rat soleus muscle

Washington

Reecy²,

Thompson³

et al. 2004

Journal of Applied Physiology

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dehydrogenase expression at the onset of altered loading in rat soleus muscle. J Appl Physiol 97: 1424 -1430, 2004; 10.1152/japplphysiol.00222.2004.-Both functional overload and hindlimb disuse induce significant energy-dependent remodeling of skeletal muscle. Lactate dehydrogenase (LDH), an important enzyme involved in anaerobic glycolysis, catalyzes the interconversion of lactate and pyruvate critical for meeting rapid high-energy demands. The purpose of this study was to determine rat soleus LDH-A and -B isoform expression, mRNA abundance, and enzymatic activity at the onset of increased or decreased loading in the rat soleus muscle. The soleus muscles from male Sprague-Dawley rats were functionally overloaded for up to 3 days by a modified synergist ablation or subjected to disuse by hindlimb suspension for 3 days. LDH mRNA concentration was determined by Northern blotting, LDH protein isoenzyme composition was determined by zymogram analysis, and LDH enzymatic activity was determined spectrophotometrically. LDH-A mRNA abundance increased by 372%, and LDH-B mRNA abundance decreased by 43 and 31% after 24 h and 3 days of functional overload, respectively, compared with that in control rats. LDH protein expression demonstrated a shift by decreasing LDH-B isoforms and increasing LDH-A isoforms. LDH-B activity decreased 80% after 3 days of functional overload. Additionally, LDH-A activity increased by 234% following 3 days of hindlimb suspension. However, neither LDH-A or LDH-B mRNA abundance was affected following 3 days of hindlimb suspension. In summary, the onset of altered loading induced a differential expression of LDH-A and -B in the rat soleus muscle, favoring rapid energy production. Long-term altered loading is associated with myofiber conversion; however, the rapid changes in LDH at the onset of altered loading may be involved in other physiological processes.atrophy; hypertrophy; disuse; hindlimb suspension; glycolytic enzymes THE LOADING DEMANDS PLACED on skeletal muscle can dramatically affect fiber cross-sectional area, phenotype, and metabolic profile (14,30,40). These adaptations are specific to the type of loading stimulus applied. Contractile and metabolic properties of skeletal muscle are linked during myofiber conversion, as evidenced by the fact that metabolic enzyme activity and gene expression are related to the new functional demands placed on that muscle. An overall shift in muscle phenotype will occur after an extended period of altered loading; however, a brief period of altered loading is also a powerful stimulus for changes to skeletal muscle that can regulate several processes associated with muscle remodeling. Functionally overloading the rat soleus muscle for 3 days alters gene expression for immune function, inflammation, and cell cycle regulation (9). Brief periods of muscle unloading initiate signaling that decreases muscle mass that includes a decrease in protein synthesis (26) and satellite cell proliferation (11).Increasing or decreasing muscle loading for extended period...

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Regulation of GLUT4 protein expression and glycogen storage after prolonged exercise

Cited by 74 publications

References 39 publications

Insulin signaling and insulin sensitivity after exercise in human skeletal muscle.

Insulin signaling and insulin sensitivity after exercise in human skeletal muscle.

Effect of dietary glycemic index on substrate transporter gene expression in human skeletal muscle after exercise

Lactate dehydrogenase expression at the onset of altered loading in rat soleus muscle

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