Methodological Aspects of Measuring Human Skeletal Muscle Electrolyte Content and Ouabain Binding Capacity

1998 ◽  
Vol 260 (2) ◽  
pp. 218-222 ◽  
Author(s):  
M.Stig Djurhuus ◽  
Niels A.H. Klitgaard ◽  
Claus Tveskov ◽  
Klavs Madsen ◽  
Bernadette Guldager ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Binding Capacity ◽  
Ouabain Binding ◽  
Electrolyte Content ◽  
Methodological Aspects

Extrarenal potassium adaptation: role of skeletal muscle

1986 ◽  
Vol 251 (2) ◽  
pp. F313-F318 ◽  
Author(s):  
J. D. Blachley ◽  
B. P. Crider ◽  
J. H. Johnson
Keyword(s):  
Skeletal Muscle ◽  
Binding Capacity ◽  
Lethal Dose ◽  
Plasma Potassium ◽  
Potassium Salts ◽  
Ouabain Binding ◽  
High Potassium ◽  
Potassium Adaptation

Following the ingestion of a high-potassium-content diet for only a few days, the plasma potassium of rats rises only modestly in response to a previously lethal dose of potassium salts. This acquired tolerance, termed potassium adaptation, is principally the result of increased capacity to excrete potassium into the urine. However, a substantial portion of the acute potassium dose is not immediately excreted and is apparently translocated into cells. Previous studies have failed to show an increase in the content of potassium of a variety of tissues from such animals. Using 86Rb as a potassium analogue, we have shown that the skeletal muscle of potassium-adapted rats takes up significantly greater amounts of potassium in vivo in response to an acute challenge than does that of control animals. Furthermore, the same animals exhibit greater efflux of 86Rb following the termination of the acute infusion. We have also shown that the Na+-K+-ATPase activity and ouabain-binding capacity of skeletal muscle microsomes are increased by the process of potassium adaptation. We conclude that skeletal muscle is an important participant in potassium adaptation and acts to temporarily buffer acute increases in the extracellular concentration of potassium.

Physiological and methodological aspects of rate of force development assessment in human skeletal muscle

2017 ◽  
Vol 38 (5) ◽  
pp. 743-762 ◽  
Author(s):  
David Rodríguez-Rosell ◽  
Fernando Pareja-Blanco ◽  
Per Aagaard ◽  
Juan José González-Badillo
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Rate Of Force Development ◽  
Force Development ◽  
Development Assessment ◽  
Methodological Aspects

Malleability of human skeletal muscle Na+-K+-ATPase pump with short-term training

2004 ◽  
Vol 97 (1) ◽  
pp. 143-148 ◽  
Author(s):  
H. J. Green ◽  
D. J. Barr ◽  
J. R. Fowles ◽  
S. D. Sandiford ◽  
J. Ouyang
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Aerobic Power ◽  
Vastus Lateralis ◽  
Peak Oxygen Consumption ◽  
Rapid Adaptation ◽  
Ouabain Binding ◽  
Short Term ◽  
Power Peak ◽  
Phosphatase Assay

To investigate the hypothesis that short-term submaximal training would result in changes in Na+-K+-ATPase content, activity, and isoform distribution in skeletal muscle, seven healthy, untrained men [peak aerobic power (peak oxygen consumption; V̇o2 peak) = 45.6 ml·kg−1·min−1 (SE 5.4)] cycled for 2 h/day at 60–65% V̇o2 peak for 6 days. Muscle tissue, sampled from the vastus lateralis before training (0 days) and after 3 and 6 days of training and analyzed for Na+-K+-ATPase content, as assessed by the vanadate facilitated [3H]ouabain-binding technique, was increased ( P < 0.05) at 3 days (294 ± 8.6 pmol/g wet wt) and 6 days (308 ± 15 pmol/g wet wt) of training compared with 0 days (272 ± 9.7 pmol/g wet wt). Maximal Na+-K+-ATPase activity as evaluated by the 3- O-methylfluorescein phosphatase assay was increased ( P < 0.05) by 6 days (53.4 ± 5.9 nmol·h−1·mg protein−1) but not by 3 days (35.9 ± 4.5 nmol·h−1·mg protein−1) compared with 0 days (37.8 ± 3.7 nmol·h−1·mg protein−1) of training. Relative isoform distribution, measured by Western blot techniques, indicated increases ( P < 0.05) in α2-content by 3 days and β1-content by 6 days of training. These results indicate that prolonged aerobic exercise represents a potent stimulus for the rapid adaptation of Na+-K+-ATPase content, isoform, and activity characteristics.

scholarly journals The effect of exercise and insulin on AS160 phosphorylation and 14-3-3 binding capacity in human skeletal muscle

2008 ◽  
Vol 294 (2) ◽  
pp. E401-E407 ◽  
Author(s):  
Kirsten F. Howlett ◽  
Alicia Mathews ◽  
Andrew Garnham ◽  
Kei Sakamoto
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Acute Exercise ◽  
Binding Capacity ◽  
Sensitivity Index ◽  
Akt Phosphorylation ◽  
Prior Exercise ◽  
Single Bout ◽  
Before And After ◽  
Amp Activated Protein Kinase

AS160 is an Akt substrate of 160 kDa implicated in the regulation of both insulin- and contraction-mediated GLUT4 translocation and glucose uptake. The effects of aerobic exercise and subsequent insulin stimulation on AS160 phosphorylation and the binding capacity of 14-3-3, a novel protein involved in the dissociation of AS160 from GLUT4 vesicles, in human skeletal muscle are unknown. Hyperinsulinemic-euglycemic clamps were performed on seven men at rest and immediately and 3 h after a single bout of cycling exercise. Skeletal muscle biopsies were taken before and after the clamps. The insulin sensitivity index calculated during the final 30 min of the clamp was 8.0 ± 0.8, 9.1 ± 0.5, and 9.2 ± 0.8 for the rest, postexercise, and 3-h postexercise trials, respectively. AS160 phosphorylation increased immediately after exercise and remained elevated 3 h after exercise. In contrast, the 14-3-3 binding capacity of AS160 and phosphorylation of Akt and AMP-activated protein kinase were only increased immediately after exercise. Insulin increased AS160 phosphorylation and 14-3-3 binding capacity and insulin receptor substrate-1 and Akt phosphorylation, but the response to insulin was not enhanced by prior exercise. In conclusion, the 14-3-3 binding capacity of AS160 is increased immediately after acute exercise in human skeletal muscle, but this is not maintained 3 h after exercise completion despite sustained AS160 phosphorylation. Insulin increases AS160 phosphorylation and 14-3-3 binding capacity, but prior exercise does not appear to enhance the response to insulin.

scholarly journals Exercise-induced TBC1D1 Ser237 phosphorylation and 14-3-3 protein binding capacity in human skeletal muscle

2010 ◽  
Vol 588 (22) ◽  
pp. 4539-4548 ◽  
Author(s):  
Christian Frøsig ◽  
Christian Pehmøller ◽  
Jesper B. Birk ◽  
Erik A. Richter ◽  
Jørgen F. P. Wojtaszewski
Keyword(s):  
Skeletal Muscle ◽  
Protein Binding ◽  
Human Skeletal Muscle ◽  
Binding Capacity ◽  
Protein Binding Capacity ◽  
Exercise Induced

Estimation of stability of [3H]-ouabain binding site concentration in rat and human skeletal muscle post mortem

1985 ◽  
Vol 45 (2) ◽  
pp. 139-144 ◽  
Author(s):  
AAGE NØRGAARD ◽  
Keld Kjeldsen ◽  
Jim STENFATT Larsen ◽  
Christian Grønhøj Larsen ◽  
Frederik Grønhøj Larsen
Keyword(s):  
Skeletal Muscle ◽  
Binding Site ◽  
Human Skeletal Muscle ◽  
Post Mortem ◽  
Ouabain Binding
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