Exercise Induces Isoform-Specific Increase in 5′AMP-Activated Protein Kinase Activity in Human Skeletal Muscle

2000 ◽  
Vol 273 (3) ◽  
pp. 1150-1155 ◽  
Author(s):  
Nobuharu Fujii ◽  
Tatsuya Hayashi ◽  
Michael F. Hirshman ◽  
Jeremy T. Smith ◽  
Susan A. Habinowski ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Human Skeletal Muscle ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Specific Increase ◽  
Amp Activated Protein Kinase

scholarly journals Metformin Increases AMP-Activated Protein Kinase Activity in Skeletal Muscle of Subjects With Type 2 Diabetes

Diabetes ◽  
2002 ◽  
Vol 51 (7) ◽  
pp. 2074-2081 ◽  
Author(s):  
N. Musi ◽  
M. F. Hirshman ◽  
J. Nygren ◽  
M. Svanfeldt ◽  
P. Bavenholm ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Skeletal Muscle ◽  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Amp Activated Protein Kinase

5′-AMP-activated protein kinase activity and protein expression are regulated by endurance training in human skeletal muscle

2004 ◽  
Vol 286 (3) ◽  
pp. E411-E417 ◽  
Author(s):  
Christian Frøsig ◽  
Sebastian B. Jørgensen ◽  
D. Grahame Hardie ◽  
Erik A. Richter ◽  
Jørgen F. P. Wojtaszewski
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Exercise Training ◽  
Protein Content ◽  
Endurance Training ◽  
Human Skeletal Muscle ◽  
Protein Kinase Activity ◽  
Local Contraction ◽  
Ampk Activity ◽  
Amp Activated Protein Kinase

The 5′-AMP-activated protein kinase (AMPK) is proposed to be involved in signaling pathways leading to adaptations in skeletal muscle in response to both a single exercise bout and exercise training. This study investigated the effect of endurance training on protein content of catalytic (α1, α2) and regulatory (β1, β2 and γ1, γ2, γ3) subunit isoforms of AMPK as well as on basal AMPK activity in human skeletal muscle. Eight healthy young men performed supervised one-legged knee extensor endurance training for 3 wk. Muscle biopsies were obtained before and 15 h after training in both legs. In response to training the protein content of α1, β2 and γ1 increased in the trained leg by 41, 34, and 26%, respectively (α1 and β2 P < 0.005, γ1 P < 0.05). In contrast, the protein content of the regulatory γ3-isoform decreased by 62% in the trained leg ( P = 0.01), whereas no effect of training was seen for α2, β1, and γ2. AMPK activity associated with the α1- and the α2-isoforms increased in the trained leg by 94 and 49%, respectively (both P < 0.005). In agreement with these observations, phosphorylation of α-AMPK-(Thr172) and of the AMPK target acetyl-CoA carboxylase-β(Ser221) increased by 74 and 180%, respectively (both P < 0.001). Essentially similar results were obtained in four additional subjects studied 55 h after training. This study demonstrates that protein content and basal AMPK activity in human skeletal muscle are highly susceptible to endurance exercise training. Except for the increase in γ1 protein, all observed adaptations to training could be ascribed to local contraction-induced mechanisms, since they did not occur in the contralateral untrained muscle.

5′-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle

2003 ◽  
Vol 94 (2) ◽  
pp. 631-641 ◽  
Author(s):  
Jakob N. Nielsen ◽  
Kirsty J. W. Mustard ◽  
Drew A. Graham ◽  
Haiyan Yu ◽  
Christopher S. MacDonald ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Exercise Training ◽  
Human Skeletal Muscle ◽  
Protein Kinase Activity ◽  
Trained Subjects ◽  
Protein Levels ◽  
Ampk Activity ◽  
Amp Activated Protein Kinase ◽  
Sedentary Subjects

5′-AMP-activated protein kinase (AMPK) has been proposed to be a pivotal factor in cellular responses to both acute exercise and exercise training. To investigate whether protein levels and gene expression of catalytic (α1, α2) and regulatory (β1, β2, γ1, γ2, γ3) AMPK subunits and exercise-induced AMPK activity are influenced by exercise training status, muscle biopsies were obtained from seven endurance exercise-trained and seven sedentary young healthy men. The α1- and α2-AMPK mRNA contents in trained subjects were both 117 ± 2% of that in sedentary subjects (not significant), whereas mRNA for γ3 was 61 ± 1% of that in sedentary subjects (not significant). The level of α1-AMPK protein in trained subjects was 185 ± 34% of that in sedentary subjects ( P < 0.05), whereas the levels of the remaining subunits (α2, β1, β2, γ1, γ2, γ3) were similar in trained and sedentary subjects. At the end of 20 min of cycle exercise at 80% of peak O2 uptake, the increase in phosphorylation of α-AMPK (Thr172) was blunted in the trained group (138 ± 38% above rest) compared with the sedentary group (353 ± 63% above rest) ( P < 0.05). Acetyl CoA-carboxylase β-phosphorylation (Ser221), which is a marker for in vivo AMPK activity, was increased by exercise in both groups but to a lower level in trained subjects (32 ± 5 arbitrary units) than in sedentary controls (45 ± 1 arbitrary units) ( P < 0.01). In conclusion, trained human skeletal muscle has increased α1-AMPK protein levels and blunted AMPK activation during exercise.

scholarly journals 5′-AMP-activated protein kinase activity is elevated early during primary brain tumor development in the rat

2010 ◽  
Vol 128 (9) ◽  
pp. 2230-2239 ◽  
Author(s):  
Taichang Jang ◽  
Joy M. Calaoagan ◽  
Eunice Kwon ◽  
Steven Samuelsson ◽  
Lawrence Recht ◽  
...  
Keyword(s):  
Brain Tumor ◽  
Protein Kinase ◽  
Kinase Activity ◽  
Tumor Development ◽  
Primary Brain Tumor ◽  
Protein Kinase Activity ◽  
Amp Activated Protein Kinase
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