scholarly journals Effects of exercise on GLUT-4 and glycogenin gene expression in human skeletal muscle

2000 ◽  
Vol 88 (2) ◽  
pp. 794-796 ◽  
Author(s):  
Yorgos Kraniou ◽  
David Cameron-Smith ◽  
Marie Misso ◽  
Greg Collier ◽  
Mark Hargreaves
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Oxygen Consumption ◽  
Human Skeletal Muscle ◽  
Glycogen Synthesis ◽  
Cycle Ergometer ◽  
Peak Oxygen Consumption ◽  
Hexokinase Ii ◽  
Glut 4 ◽  
Single Bout

To investigate the effect of exercise on GLUT-4, hexokinase, and glycogenin gene expression in human skeletal muscle, 10 untrained subjects (6 women and 4 men, 21.4 ± 1.2 yr, 66.3 ± 5.0 kg, peak oxygen consumption = 2.30 ± 0.19 l/min) exercised for 60 min on a cycle ergometer at a power output requiring 73 ± 4% peak oxygen consumption. Muscle samples were obtained by needle biopsy before, immediately after, and 3 h after exercise. Gene expression was quantified, relative to 29S ribosomal protein cDNA, by RT-PCR. GLUT-4 gene expression was increased immediately after exercise (1.7 ± 0.4 vs. 0.9 ± 0.3 arbitrary units; P < 0.05) and remained significantly higher than baseline 3 h after the end of exercise (2.2 ± 0.4 vs. 0.9 ± 0.3 arbitrary units; P < 0.05). Hexokinase II gene expression was significantly higher than the resting value 3 h after the end of exercise (2.9 ± 0.4 vs. 1.3 ± 0.3 arbitrary units; P < 0.05). Exercise increased glycogenin mRNA more than twofold (2.8 ± 0.6 vs. 1.2 ± 0.2 arbitrary units; P < 0.05) 3 h after the end of exercise. For the first time, we report that a single bout of exercise is sufficient to cause upregulation of GLUT-4 and glycogenin gene expression in human skeletal muscle. Whether these increases, together with the associated increase in hexokinase II gene expression, lead to increased expression of these key proteins in skeletal muscle and contribute to the enhanced skeletal muscle glucose uptake, glycogen synthesis, and insulin action observed following exercise remains to be determined.

Rat skeletal muscle hexokinase II mRNA and activity are increased by a single bout of acute exercise

1994 ◽  
Vol 266 (2) ◽  
pp. E171-E178 ◽  
Author(s):  
R. M. O'Doherty ◽  
D. P. Bracy ◽  
H. Osawa ◽  
D. H. Wasserman ◽  
D. K. Granner
Keyword(s):  
Skeletal Muscle ◽  
Acute Exercise ◽  
Recovery Period ◽  
Exhaustive Exercise ◽  
Male Rats ◽  
Hexokinase Ii ◽  
Glut 4 ◽  
Heat Stable ◽  
Single Bout

This study addresses the potential role of skeletal muscle hexokinase (HK) II in the regulation of glucose uptake and metabolism in vivo. Male rats undertook a single bout of treadmill exercise and were then killed immediately or after a predetermined recovery period. Three muscles [soleus (Sol), gastrocnemius/plantaris (Gc), and white vastus] were excised, and HK II mRNA, GLUT-4 mRNA, total HK (HK I and HK II) and heat-stable HK (predominantly HK I) activities were assessed. Three hours after the cessation of a single bout of exhaustive exercise, HK II mRNA was significantly increased in all three muscles. Ninety or thirty minutes of exercise, with a 3-h recovery, increased Gc HK II mRNA to the same extent as exhaustive exercise, but 15 min of exercise had no effect. Gc HK II mRNA continued to increase up to 8 h after the cessation of 90 min of exercise but returned to basal by 24 h postexercise. In contrast to HK II mRNA, Gc GLUT-4 mRNA was unchanged at 0, 3, 8, and 24 h after the cessation of 90 min of exercise. Total HK activity was significantly increased in Sol and Gc, 8 and 24 h after the cessation of 90 min of exercise. Heat-stable HK activity was unchanged in all three muscles. The increase in total HK activity, inferred to be an increase of HK II, may be important in the persistence of the postexercise increase in insulin action.

Seven days of exercise increase GLUT-4 protein content in human skeletal muscle

1995 ◽  
Vol 79 (6) ◽  
pp. 1936-1938 ◽  
Author(s):  
J. A. Houmard ◽  
M. S. Hickey ◽  
G. L. Tyndall ◽  
K. E. Gavigan ◽  
G. L. Dohm
Keyword(s):  
Skeletal Muscle ◽  
Exercise Training ◽  
Protein Content ◽  
Human Skeletal Muscle ◽  
Glucose Transporter ◽  
Vastus Lateralis ◽  
Cycle Ergometer ◽  
Maximal Heart Rate ◽  
Short Term ◽  
Glut 4

Insulin-responsive glucose transporter (GLUT-4) content increases by 1.8-fold in skeletal muscle with 14 wk of exercise training [Houmard et al. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E896-E901, 1993]. The purpose of this study was to determine whether more short-term training (7 days) increases GLUT-4 protein content in human skeletal muscle. Seven sedentary men [25.0 +/- 1.1 (SE) yr, 44.1 +/- 2.2 ml.kg-1.min-1 maximal O2 uptake, 14.9 +/- 2.1% body fat] were examined before and after 7 days of cycle ergometer training (1 h/day, 76 +/- 2% maximal heart rate). Needle biopsy samples from the vastus lateralis were used to determine GLUT-4 protein content. Muscle GLUT-4 increased (P < 0.05) by an average of 2.8 +/- 0.5-fold with 7 days of training. GLUT-4 content in skeletal muscle thus increases substantially with short-term exercise training.

Regulation of hexokinase II and glycogen synthase mRNA, protein, and activity in human muscle

1995 ◽  
Vol 269 (4) ◽  
pp. E701-E708 ◽  
Author(s):  
L. J. Mandarino ◽  
R. L. Printz ◽  
K. A. Cusi ◽  
P. Kinchington ◽  
R. M. O'Doherty ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Insulin Infusion ◽  
Glycogen Synthase ◽  
Normal Subjects ◽  
Hexokinase Ii ◽  
Glut 4 ◽  
Before And After ◽  
Muscle Biopsies

Insulin regulates the activity of key enzymes of glucose metabolism in skeletal muscle by altering transcription or translation or by producing activity-altering modifications of preexisting enzyme molecules. Because of the small size of percutaneous muscle biopsies, these phenomena have been difficult to study in humans. This study was performed to determine how physiological hyperinsulinemia regulates the activities of hexokinase (HK), glycogen synthase (GS), and GLUT-4 in human skeletal muscle in vivo. We determined mRNA abundance, protein content, and activities for these proteins in muscle biopsies before and after a hyperinsulinemic clamp in normal subjects. HK I, HK II, GS, and GLUT-4 were expressed in muscle. HK II accounted for 80% of total HK activity and was increased by insulin from a basal value of 2.11 +/- 0.26 to 3.35 +/- 0.47 pmol.min-1.mg protein-1 (P < 0.05); HK I activity was unaffected. Insulin increased GS activity from 3.85 +/- 0.82 to 6.06 +/- 0.49 nmol.min-1.mg-1 (P < 0.01). HK II mRNA was increased 3.3 +/- 1.3-fold (P < 0.05) by insulin infusion. HK I, GS, and GLUT-4 mRNA and protein were unaffected. Because insulin infusion increased HK II but not GS mRNA, we conclude that HK II and GS may be regulated by insulin by different mechanisms in human skeletal muscle.

scholarly journals Metabolic and molecular changes associated with the increased skeletal muscle insulin action 24–48 h after exercise in young and old humans

2018 ◽  
Vol 46 (1) ◽  
pp. 111-118 ◽  
Author(s):  
Francis B. Stephens ◽  
Kostas Tsintzas
Keyword(s):  
Skeletal Muscle ◽  
Insulin Sensitivity ◽  
Insulin Action ◽  
Glucose Transporter ◽  
Glycogen Synthesis ◽  
Older Individuals ◽  
Hexokinase Ii ◽  
Molecular Changes ◽  
Single Bout ◽  
Muscle Insulin Action

The molecular and metabolic mechanisms underlying the increase in insulin sensitivity (i.e. increased insulin-stimulated skeletal muscle glucose uptake, phosphorylation and storage as glycogen) observed from 12 to 48 h following a single bout of exercise in humans remain unresolved. Moreover, whether these mechanisms differ with age is unclear. It is well established that a single bout of exercise increases the translocation of the glucose transporter, GLUT4, to the plasma membrane. Previous research using unilateral limb muscle contraction models in combination with hyperinsulinaemia has demonstrated that the increase in insulin sensitivity and glycogen synthesis 24 h after exercise is also associated with an increase in hexokinase II (HKII) mRNA and protein content, suggesting an increase in the capacity of the muscle to phosphorylate glucose and divert it towards glycogen synthesis. Interestingly, this response is altered in older individuals for up to 48 h post exercise and is associated with molecular changes in skeletal muscle tissue that are indicative of reduced lipid oxidation, increased lipogenesis, increased inflammation and a relative inflexibility of changes in intramyocellular lipid (IMCL) content. Reduced insulin sensitivity (insulin resistance) is generally related to IMCL content, particularly in the subsarcolemmal (SSL) region, and both are associated with increasing age. Recent research has demonstrated that ageing per se appears to cause an exacerbated lipolytic response to exercise that may result in SSL IMCL accumulation. Further research is required to determine if increased IMCL content affects HKII expression in the days after exercise in older individuals, and the effect of this on skeletal muscle insulin action.

Unchanged [3H]ouabain binding site content but reduced Na+-K+ pump α2-protein abundance in skeletal muscle in older adults

2012 ◽  
Vol 113 (10) ◽  
pp. 1505-1511 ◽  
Author(s):  
Michael J. McKenna ◽  
Ben D. Perry ◽  
Fabio R. Serpiello ◽  
Marissa K. Caldow ◽  
Pazit Levinger ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Oxygen Consumption ◽  
Binding Site ◽  
Total Content ◽  
Peak Oxygen Consumption ◽  
Vastus Lateralis Muscle ◽  
Protein Abundance ◽  
Membrane Excitability ◽  
Ouabain Binding

Aging is associated with reduced muscle mass, weakness, and increased fatigability. In skeletal muscle, the Na+-K+ pump (NKA) is important in regulating Na+-K+ gradients, membrane excitability, and thus contractility, but the effects of aging on muscle NKA are unclear. We investigated whether aging is linked with reduced muscle NKA by contrasting muscle NKA isoform gene expression and protein abundance, and NKA total content in 17 Elderly (66.8 ± 6.4 yr, mean ± SD) and 16 Young adults (23.9 ± 2.2 yr). Participants underwent peak oxygen consumption assessment and a vastus lateralis muscle biopsy, which was analyzed for NKA α1-, α2-, α3-, β1-, β2-, and β3-isoform gene expression (real-time RT-PCR), protein abundance (immunoblotting), and NKA total content ([3H]ouabain binding sites). The Elderly had lower peak oxygen consumption (−36.7%, P = 0.000), strength (−36.3%, P = 0.001), NKA α2- (−24.4%, 11.9 ± 4.4 vs. 9.0 ± 2.7 arbitrary units, P = 0.049), and NKA β3-protein abundance (−23.0%, P = 0.041) than Young. The β3-mRNA was higher in Elderly compared with Young ( P = 0.011). No differences were observed between groups for other NKA isoform mRNA or protein abundance, or for [3H]ouabain binding site content. Thus skeletal muscle in elderly individuals was characterized by decreased NKA α2- and β3-protein abundance, but unchanged α1 abundance and [3H]ouabain binding. The latter was likely caused by reduced α2 abundance with aging, preventing an otherwise higher [3H]ouabain binding that might occur with a greater membrane density in smaller muscle fibers. Further study is required to verify reduced muscle NKA α2 with aging and possible contributions to impaired exercise capability and daily living activities.

Global and targeted gene expression and protein content in skeletal muscle of young men following short-term creatine monohydrate supplementation

2008 ◽  
Vol 32 (2) ◽  
pp. 219-228 ◽  
Author(s):  
Adeel Safdar ◽  
Nicholas J. Yardley ◽  
Rodney Snow ◽  
Simon Melov ◽  
Mark A. Tarnopolsky
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Mrna Expression ◽  
Protein Content ◽  
Cellular Response ◽  
Glycogen Synthesis ◽  
Creatine Monohydrate ◽  
Fat Free Mass ◽  
Cell Swelling ◽  
Short Term

Creatine monohydrate (CrM) supplementation has been shown to increase fat-free mass and muscle power output possibly via cell swelling. Little is known about the cellular response to CrM. We investigated the effect of short-term CrM supplementation on global and targeted mRNA expression and protein content in human skeletal muscle. In a randomized, placebo-controlled, crossover, double-blind design, 12 young, healthy, nonobese men were supplemented with either a placebo (PL) or CrM (loading phase, 20 g/day × 3 days; maintenance phase, 5 g/day × 7 days) for 10 days. Following a 28-day washout period, subjects were put on the alternate supplementation for 10 days. Muscle biopsies of the vastus lateralis were obtained and were assessed for mRNA expression (cDNA microarrays + real-time PCR) and protein content (Kinetworks KPKS 1.0 Protein Kinase screen). CrM supplementation significantly increased fat-free mass, total body water, and body weight of the participants ( P < 0.05). Also, CrM supplementation significantly upregulated (1.3- to 5.0-fold) the mRNA content of genes and protein content of kinases involved in osmosensing and signal transduction, cytoskeleton remodeling, protein and glycogen synthesis regulation, satellite cell proliferation and differentiation, DNA replication and repair, RNA transcription control, and cell survival. We are the first to report this large-scale gene expression in the skeletal muscle with short-term CrM supplementation, a response that suggests changes in cellular osmolarity.

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