scholarly journals Role of 5′AMP‐activated protein kinase in glycogen synthase activity and glucose utilization: insights from patients with McArdle's disease

2002 ◽  
Vol 541 (3) ◽  
pp. 979-989 ◽  
Author(s):  
Jakob N. Nielsen ◽  
Jørgen F. P. Wojtaszewski ◽  
Ronald G. Haller ◽  
D. Grahame Hardie ◽  
Bruce E. Kemp ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Glucose Utilization ◽  
Glycogen Synthase ◽  
Mcardle's Disease ◽  
Mcardle’S Disease ◽  
Amp Activated Protein Kinase ◽  
Glycogen Synthase Activity

Transgenic models – a scientific tool to understand exercise-induced metabolism: the regulatory role of AMPK (5′-AMP-activated protein kinase) in glucose transport and glycogen synthase activity in skeletal muscle

2003 ◽  
Vol 31 (6) ◽  
pp. 1290-1294 ◽  
Author(s):  
J.F.P. Wojtaszewski ◽  
J.N. Nielsen ◽  
S.B. Jørgensen ◽  
C. Frøsig ◽  
J.B. Birk ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Glucose Transport ◽  
Glycogen Synthase ◽  
Muscle Metabolism ◽  
Regulatory Role ◽  
Amp Activated Protein Kinase ◽  
Glycogen Synthase Activity

The AMPK (5´AMP-activated protein kinase) is becoming recognized as a critical regulator of energy metabolism. However, many of these effects in muscle metabolism have been ascribed to AMPK based on the use of the unspecific activator AICAR (5-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside). Using mouse models in which AMPK activity has been specifically blocked (kinase dead) or knocked out we and others have been able to conduct studies gaining more conclusive data on the role of AMPK in muscle metabolism. In this mini-review focus is on AMPK and its regulatory role for glucose transport and GS (glycogen synthase) activity in skeletal muscle, indicating that AMPK is a GS kinase in vivo which might influence GS activity during exercise and that AMPK is involved in AICAR/hypoxia-induced glucose transport but not or only partially in contraction-stimulated glucose transport.

Decreased insulin action in skeletal muscle from patients with McArdle's disease

2002 ◽  
Vol 282 (6) ◽  
pp. E1267-E1275 ◽  
Author(s):  
Jakob N. Nielsen ◽  
John Vissing ◽  
Jørgen F. P. Wojtaszewski ◽  
Ronald G. Haller ◽  
Najma Begum ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glucose Tolerance ◽  
Muscle Glycogen ◽  
Insulin Action ◽  
Glycogen Synthase ◽  
Oral Glucose ◽  
Mcardle's Disease ◽  
Mcardle’S Disease ◽  
The Difference ◽  
Glycogen Synthase Activity

Insulin action is decreased by high muscle glycogen concentrations in skeletal muscle. Patients with McArdle's disease have chronic high muscle glycogen levels and might therefore be at risk of developing insulin resistance. In this study, six patients with McArdle's disease and six matched control subjects were subjected to an oral glucose tolerance test and a euglycemic-hyperinsulinemic clamp. The muscle glycogen concentration was 103 ± 45% higher in McArdle patients than in controls. Four of six McArdle patients, but none of the controls, had impaired glucose tolerance. The insulin-stimulated glucose utilization and the insulin-stimulated increase in glycogen synthase activity during the clamp were significantly lower in the patients than in controls (51.3 ± 6.0 vs. 72.6 ± 13.1 μmol · min−1 · kg lean body mass−1, P < 0.05, and 53 ± 15 vs. 79 ± 9%, P < 0.05, n = 6, respectively). The difference in insulin-stimulated glycogen synthase activity between the pairs was significantly correlated ( r = 0.96, P < 0.002) with the difference in muscle glycogen level. The insulin-stimulated increase in Akt phosphorylation was smaller in the McArdle patients than in controls (45 ± 13 vs. 76 ± 13%, P < 0.05, respectively), whereas basal and insulin-stimulated glycogen synthase kinase 3α and protein phosphatase-1 activities were similar in the two groups. Furthermore, the ability of insulin to decrease and increase fat and carbohydrate oxidation, respectively, was blunted in the patients. In conclusion, these data show that patients with McArdle's glycogen storage disease are insulin resistant in terms of glucose uptake, glycogen synthase activation, and alterations in fuel oxidation. The data further suggest that skeletal muscle glycogen levels play an important role in the regulation of insulin-stimulated glycogen synthase activity.

scholarly journals The role of AMP-activated protein kinase in quercetin-induced apoptosis of HL-60 cells

2014 ◽  
Vol 46 (5) ◽  
pp. 394-400 ◽  
Author(s):  
J. Xiao ◽  
G. Niu ◽  
S. Yin ◽  
S. Xie ◽  
Y. Li ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Induced Apoptosis ◽  
Amp Activated Protein Kinase

Role of the AMP-activated protein kinase in regulating fatty acid metabolism during exerciseThis paper is one of a selection of papers published in this Special Issue, entitled 14th International Biochemistry of Exercise Conference – Muscles as Molecular and Metabolic Machines, and has undergone the Journal’s usual peer review process.

2009 ◽  
Vol 34 (3) ◽  
pp. 315-322 ◽  
Author(s):  
Gregory R. Steinberg
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acids ◽  
Adipose Tissue ◽  
Fatty Acid ◽  
Protein Kinase ◽  
Fatty Acid Metabolism ◽  
Acid Metabolism ◽  
Moderate Intensity ◽  
Amp Activated Protein Kinase

During moderate-intensity exercise, fatty acids are the predominant substrate for working skeletal muscle. The release of fatty acids from adipose tissue stores, combined with the ability of skeletal muscle to actively fine tune the gradient between fatty acid and carbohydrate metabolism, depending on substrate availability and energetic demands, requires a coordinated system of metabolic control. Over the past decade, since the discovery that AMP-activated protein kinase (AMPK) was increased in accordance with exercise intensity, there has been significant interest in the proposed role of this ancient stress-sensing kinase as a critical integrative switch controlling metabolic responses during exercise. In this review, studies examining the role of AMPK as a regulator of fatty acid metabolism in both adipose tissue and skeletal muscle during exercise will be discussed. Exercise induces activation of AMPK in adipocytes and regulates triglyceride hydrolysis and esterfication through phosphorylation of hormone sensitive lipase (HSL) and glycerol-3-phosphate acyl-transferase, respectively. In skeletal muscle, exercise-induced activation of AMPK is associated with increases in fatty acid uptake, phosphorylation of HSL, and increased fatty acid oxidation, which is thought to occur via the acetyl-CoA carboxylase-malony-CoA-CPT-1 signalling axis. Despite the importance of AMPK in regulating fatty acid metabolism under resting conditions, recent evidence from transgenic models of AMPK deficiency suggest that alternative signalling pathways may also be important for the control of fatty acid metabolism during exercise.

scholarly journals Regulation of Glycogen Synthase by Glucose and Glycogen: A Possible Role for AMP-Activated Protein Kinase

Diabetes ◽  
2003 ◽  
Vol 52 (1) ◽  
pp. 9-15 ◽  
Author(s):  
R. Halse ◽  
L. G.D. Fryer ◽  
J. G. McCormack ◽  
D. Carling ◽  
S. J. Yeaman
Keyword(s):  
Protein Kinase ◽  
Glycogen Synthase ◽  
Amp Activated Protein Kinase

Muscle pain in myophosphorylase deficiency (McArdle’s disease): The role of gender, genotype, and pain-related coping

Pain ◽  
2006 ◽  
Vol 124 (3) ◽  
pp. 295-304 ◽  
Author(s):  
Oliver Rommel ◽  
Rudolf A. Kley ◽  
Gabriele Dekomien ◽  
Jörg T. Epplen ◽  
Matthias Vorgerd ◽  
...  
Keyword(s):  
Muscle Pain ◽  
Mcardle's Disease ◽  
Mcardle’S Disease

The emerging role of AMP-activated protein kinase in cholestatic liver diseases

2017 ◽  
Vol 125 ◽  
pp. 105-113 ◽  
Author(s):  
Xiaojiaoyang Li ◽  
Runping Liu ◽  
Luyong Zhang ◽  
Zhenzhou Jiang
Keyword(s):  
Protein Kinase ◽  
Liver Diseases ◽  
Amp Activated Protein Kinase

scholarly journals Beneficial Role of Erythrocyte Adenosine A2B Receptor–Mediated AMP-Activated Protein Kinase Activation in High-Altitude Hypoxia

Circulation ◽  
2016 ◽  
Vol 134 (5) ◽  
pp. 405-421 ◽  
Author(s):  
Hong Liu ◽  
Yujin Zhang ◽  
Hongyu Wu ◽  
Angelo D’Alessandro ◽  
Gennady G. Yegutkin ◽  
...  
Keyword(s):  
Protein Kinase ◽  
High Altitude ◽  
Altitude Hypoxia ◽  
Kinase Activation ◽  
Beneficial Role ◽  
Protein Kinase Activation ◽  
A2b Receptor ◽  
Amp Activated Protein Kinase ◽  
Adenosine A2b
Sign in / Sign up

Export Citation Format

Share Document