Oral glucose ingestion attenuates exercise-induced activation of 5′-AMP-activated protein kinase in human skeletal muscle

2006 ◽  
Vol 342 (3) ◽  
pp. 949-955 ◽  
Author(s):  
Thorbjorn C.A. Akerstrom ◽  
Jesper B. Birk ◽  
Ditte K. Klein ◽  
Christian Erikstrup ◽  
Peter Plomgaard ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Human Skeletal Muscle ◽  
Oral Glucose ◽  
Glucose Ingestion ◽  
Exercise Induced ◽  
Amp Activated Protein Kinase

Exercise and MEF2–HDAC interactions

2007 ◽  
Vol 32 (5) ◽  
pp. 852-856 ◽  
Author(s):  
Sean L. McGee
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Nuclear Export ◽  
Energy Homeostasis ◽  
Whole Body ◽  
Positive Health ◽  
Exercise Induced ◽  
Amp Activated Protein Kinase ◽  
Body Energy ◽  
Skeletal Muscle Adaptations

Exercise increases the metabolic capacity of skeletal muscle, which improves whole-body energy homeostasis and contributes to the positive health benefits of exercise. This is, in part, mediated by increases in the expression of a number of metabolic enzymes, regulated largely at the level of transcription. At a molecular level, many of these genes are regulated by the class II histone deacetylase (HDAC) family of transcriptional repressors, in particular HDAC5, through their interaction with myocyte enhancer factor 2 transcription factors. HDAC5 kinases, including 5′-AMP-activated protein kinase and protein kinase D, appear to regulate skeletal muscle metabolic gene transcription by inactivating HDAC5 and inducing HDAC5 nuclear export. These mechanisms appear to participate in exercise-induced gene expression and could be important for skeletal muscle adaptations to exercise.

scholarly journals Exercise-Induced Protein Kinase C Isoform-Specific Activation in Human Skeletal Muscle

Diabetes ◽  
2003 ◽  
Vol 53 (1) ◽  
pp. 21-24 ◽  
Author(s):  
S. Perrini ◽  
J. Henriksson ◽  
J. R. Zierath ◽  
U. Widegren
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Skeletal Muscle ◽  
Kinase C ◽  
Exercise Induced

GLUCOSE INGESTION ATTENUATES THE EXERCISE-INDUCED INCREASE IN PDK4 mRNA IN HUMAN SKELETAL MUSCLE

2003 ◽  
Vol 35 (Supplement 1) ◽  
pp. S196
Author(s):  
M Hargreaves ◽  
L J. Cluberton ◽  
S L McGee ◽  
R M. Murphy
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Glucose Ingestion ◽  
Exercise Induced

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.

scholarly journals AMP-Activated Protein Kinase Is Not Down-Regulated in Human Skeletal Muscle of Obese Females

2004 ◽  
Vol 89 (9) ◽  
pp. 4575-4580 ◽  
Author(s):  
Gregory R. Steinberg ◽  
Angela C. Smith ◽  
Bryce J. W. van Denderen ◽  
Zhiping Chen ◽  
Sid Murthy ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Human Skeletal Muscle ◽  
Amp Activated Protein Kinase

scholarly journals Role of Angptl4/Fiaf in exercise-induced skeletal muscle AMPK activation

2018 ◽  
Vol 125 (3) ◽  
pp. 715-722 ◽  
Author(s):  
Hyukki Chang ◽  
Obin Kwon ◽  
Mi-Seon Shin ◽  
Gil Myoung Kang ◽  
Yea Hyun Leem ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Muscle Cells ◽  
Oxidative Capacity ◽  
Skeletal Muscle Cells ◽  
C2c12 Myotubes ◽  
Ampk Activation ◽  
Expression Levels ◽  
Exercise Induced ◽  
Amp Activated Protein Kinase

Angiopoietin-like protein 4 (Angptl4)/fasting-induced adipose factor (Fiaf) expression levels are increased by exercise in skeletal muscle. We have previously shown that Angptl4 regulates food intake and energy expenditure via modulation of hypothalamic AMP-activated protein kinase (AMPK) activity. AMPK is an important signaling molecule that integrates skeletal muscle metabolism during exercise. Therefore, we investigated the involvement of Angptl4 in exercise-induced AMPK activation in skeletal muscle. Angptl4 protein and mRNA expression levels were significantly increased in the gastrocnemius and soleus muscles of mice following a 50-min running bout. Treatment of C2C12 myotubes with Angptl4 increased phosphorylation of AMPK and acetyl-CoA carboxylase (ACC), which were markers of AMPK activation, and the mitochondrial maximum respiratory capacity. Treadmill exercise increased AMPK and ACC phosphorylation in the gastrocnemius of normal mice; this phosphorylation increase was attenuated in mice lacking Angptl4. Endurance to swimming and hanging was also reduced in Angptl4 knockout mice. Taken together, our current data demonstrate that exercise-induced upregulation of skeletal muscle Angptl4 is critical for AMPK activation and exercise tolerance. These findings unveil a new role for skeletal muscle Angptl4 in exercise physiology. NEW & NOTEWORTHY 1) Angiopoietin-like protein 4 (Angptl4) treatment activates AMP-activated protein kinase (AMPK) signaling in skeletal muscle cells. 2) Angptl4 increases the maximum mitochondrial oxidative capacity through AMPK activation in skeletal muscle cells. 3) Lack of Angptl4 mitigates exercise-induced skeletal muscle AMPK activation. 4) Angptl4-deficient mice show a lower endurance to exercise.

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