System for measuring isolated rat soleus muscle belly response to tetanic stimulation

2000 ◽  
Vol 439 (S1) ◽  
pp. r173-r174
Author(s):  
Anton Koren ◽  
Roman Blenkuš
Keyword(s):  
Soleus Muscle ◽  
Tetanic Stimulation ◽  
Muscle Belly ◽  
Rat Soleus Muscle ◽  
Isolated Rat

On the role of 5-hydroxytryptamine in the peripheral action of fenfluramine: studies with the isolated rat soleus muscle

1990 ◽  
Vol 39 (5) ◽  
pp. 965-968 ◽  
Author(s):  
Shlomo Sasson ◽  
Baruch Kunievsky ◽  
Christine Nathan ◽  
Erol Ceras
Keyword(s):  
Soleus Muscle ◽  
Rat Soleus Muscle ◽  
Peripheral Action ◽  
Isolated Rat

Mechanism of insulin-induced activation of Na(+)-K(+)-ATPase in isolated rat soleus muscle

1991 ◽  
Vol 261 (2) ◽  
pp. C224-C230 ◽  
Author(s):  
E. Weil ◽  
S. Sasson ◽  
Y. Gutman
Keyword(s):  
Soleus Muscle ◽  
Time Course ◽  
Maximal Effect ◽  
Dependent Manner ◽  
Insulin Stimulation ◽  
K Uptake ◽  
Sequence Of Events ◽  
Rat Soleus Muscle ◽  
Isolated Rat ◽  
Stimulation Of

Insulin augments Na(+)-K(+)-ATPase activity in skeletal muscles. It has been proposed that the sequence of events is activation of Na(+)-H+ antiporter, increased intracellular Na+ concentration ( [Na+]i), and stimulation of Na(+)-K+ pump. We have used isolated rat soleus muscles to test this hypothesis. Insulin increased the ouabain-suppressible K+ uptake in a dose- and time-dependent manner. The maximal effect was observed at 50-100 mU/ml insulin. Stimulation of K+ uptake was accompanied by increased specific [3H]ouabain binding and lowered [Na+]i. The ionophore monensin, which promotes Na(+)-H+ exchange, also increased the rate of ouabain-suppressible K+ uptake in soleus muscle, with a maximal effect obtained at 10-100 microM ionophore. However, this increase was accompanied by an elevation of [Na+]i. In the presence of 10-100 microM monensin, addition of 100 mU/ml insulin further increased K+ uptake but reduced [Na+]i. The effect on K+ uptake was additive. Ouabain (10(-3) M) completely suppressed the effect of insulin on [Na+]i. Insulin had no effect on the magnitude or the time course of insulin stimulation of K+ uptake. Thus equal stimulation of Na(+)-K(+)-ATPase by insulin was observed when [Na+]i was elevated (under monensin) or lowered (under amiloride). These data suggest that activation of Na(+)-K(+)-ATPase in soleus muscle by insulin is not secondary to stimulation of Na(+)-H+ antiporter.

The importance of limitations in aerobic metabolism, glycolysis, and membrane excitability for the development of high-frequency fatigue in isolated rat soleus muscle

2007 ◽  
Vol 292 (5) ◽  
pp. R2001-R2011 ◽  
Author(s):  
K. T. Murphy ◽  
T. Clausen
Keyword(s):  
Soleus Muscle ◽  
High Frequency ◽  
Receptor Agonist ◽  
Aerobic Metabolism ◽  
Membrane Excitability ◽  
M Wave ◽  
Force Transducers ◽  
Rat Soleus Muscle ◽  
Isolated Rat

We investigated the role of limitations in aerobic metabolism, glycolysis, and membrane excitability for development of high-frequency fatigue in isolated rat soleus muscle. Muscles mounted on force transducers were incubated in buffer bubbled with 5% CO2 and either 95% O2 (oxygenated) or 95% N2 (anoxic) and stimulated at 60 Hz continuously for 30–120 s or intermittently for 120 s. Cyanide (2 mM) and 2-deoxyglucose (10 mM) were used to inhibit aerobic metabolism and both glycolysis and aerobic metabolism, respectively. Excitability was reduced by carbacholine (10 μM), a nicotinic ACh receptor agonist, or ouabain (10 μM), an Na+-K+ pump inhibitor. Membrane excitability was measured by recording M waves. Intracellular Na+ and K+ contents and membrane potentials were measured by flame photometry and microelectrodes, respectively. During 120 s of continuous stimulation, oxygenated and anoxic muscles showed the same force loss. In oxygenated muscles, cyanide did not alter force loss for up to 90 s, whereas 2-deoxyglucose increased force loss (by 19–69%; P < 0.01) from 14 s of stimulation. In oxygenated muscles, 60 s of stimulation reduced force, M wave area, and amplitude by 70–90% ( P < 0.001). Carbacholine or ouabain increased intracellular Na+ content ( P < 0.001), induced a 7- to 8-mV membrane depolarization ( P < 0.001), and accelerated the rate of force loss (by 250–414%) during 30 s of stimulation ( P < 0.001). Similar effects were seen with intermittent stimulation. In conclusion, limitations in glycolysis and subsequently also in aerobic metabolism, as well as membrane excitability but not aerobic metabolism alone, appear to play an important role in the development of high-frequency fatigue in isolated rat soleus muscle.

Short-term measurement of D-xylose uptake by isolated rat soleus muscle

1976 ◽  
Vol 4 (4) ◽  
pp. 223-237 ◽  
Author(s):  
Ian G. Sloan ◽  
Gary P. Korbl ◽  
Michael K. Gould
Keyword(s):  
Soleus Muscle ◽  
Short Term ◽  
Xylose Uptake ◽  
Rat Soleus Muscle ◽  
Isolated Rat

Total and myofibrillar protein degradation in isolated soleus muscles after exercise

1989 ◽  
Vol 257 (1) ◽  
pp. E1-E5 ◽  
Author(s):  
G. J. Kasperek ◽  
R. D. Snider
Keyword(s):  
Protein Degradation ◽  
Soleus Muscle ◽  
Exercise Duration ◽  
Myofibrillar Protein ◽  
Rat Soleus Muscle ◽  
Exercise Induced ◽  
Isolated Rat

The effect of exercise on the rate of total and myofibrillar protein degradation was determined by measuring the rate of release of tyrosine and 3-methylhistidine, respectively, from isolated rat soleus muscle strips after exercise. The rate of tyrosine release was 30–50% greater from the muscles of the exercised rats, whereas the rate of 3-methylhistidine release was unchanged. Thus the exercise-induced increase in the rate of protein degradation is due to increased breakdown of nonmyofibrillar proteins. The rate of protein degradation increases as a function of exercise duration and rapidly returns to the preexercise level during recovery. The exercise-induced increase in the rate of protein degradation is not inhibited by chloroquine. Together these observations suggest that the increase in the rate of protein degradation observed immediately after exercise is due to the breakdown of nonmyofibrillar proteins and occurs via the nonlysosomal pathway of protein degradation.

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