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.

Intracellular Na+ and K+ activities during insulin stimulation of rat soleus muscle

1982 ◽  
Vol 242 (3) ◽  
pp. E193-E200
Author(s):  
R. J. Stark ◽  
J. O'Doherty
Keyword(s):  
Membrane Potential ◽  
Soleus Muscle ◽  
Intracellular Sodium ◽  
Resting Membrane Potential ◽  
Insulin Stimulation ◽  
Subsequent Increase ◽  
Extracellular Glucose ◽  
Rat Soleus Muscle ◽  
Sodium And Potassium ◽  
Stimulation Of

The action of insulin on the resting membrane potential (Em) and intracellular sodium and potassium activities (aNa, aK) of rat soleus muscle fibers was determined by direct intracellular measurements of aNa, aK, and Em using Na-selective, K-selective, and conventional microelectrodes. The use of these microelectrodes allowed us to continuously monitor these parameters in the same fiber. Although we were able to accurately measure aNa and aK and continuously monitor their levels throughout periods of insulin stimulation of up to 20 min duration, we were unable to detect any significant change in Em, aNa, or aK. Varying the concentration of insulin or extracellular glucose failed to alter our observations. These results indicate that the action of insulin on the sarcolemma and subsequent increase in glucose transport must result from some mechanism independent of a change in membrane potential or intracellular sodium or potassium activity.

Excretion in the house cricket: stimulation of rectal reabsorption by homogenates of the corpus cardiacum

1993 ◽  
Vol 185 (1) ◽  
pp. 305-323 ◽  
Author(s):  
J. H. Spring ◽  
S. A. Albarwani
Keyword(s):  
Time Course ◽  
Chloride Transport ◽  
Malpighian Tubule ◽  
Acheta Domesticus ◽  
Rectal Absorption ◽  
K Uptake ◽  
House Cricket ◽  
Tubule Fluid ◽  
Stimulation Of

1. We describe an in vitro perfused preparation of Acheta domesticus rectum which allows direct comparison of Malpighian tubule secretion and rectal absorption under identical conditions. Rectal absorption is stimulated four- to sixfold by corpora cardiaca (CC) homogenates and the stimulated rate is sufficiently rapid to account for all the fluid secreted by the tubules. 2. The time course for increased fluid absorption is similar to that required to stimulate electrogenic chloride transport in locusts and grasshoppers. Chloride is rapidly absorbed by the rectum under all conditions, along with lesser amounts of Na+ and K+. Unlike the situation in locusts, K+ uptake is unaffected by CC homogenates and the stimulated absorbate is NaCl-rich, similar in composition to the NaCl-rich tubule fluid produced under stimulated conditions. The absorbate is always slightly hypo-osmotic to the perfusate, reaching a maximum differential of approximately 15 mosmol l-1 following CC stimulation. 3. The antidiuretic factor that reduces tubule secretion does not promote fluid reabsorption by the rectum.

Excitation-induced activation of the Na(+)-K+ pump in rat skeletal muscle

1994 ◽  
Vol 266 (4) ◽  
pp. C925-C934 ◽  
Author(s):  
M. E. Everts ◽  
T. Clausen
Keyword(s):  
Soleus Muscle ◽  
Contractile Activity ◽  
Activation Mechanism ◽  
Rat Skeletal Muscle ◽  
Ouabain Binding ◽  
Direct Stimulation ◽  
Rat Soleus Muscle ◽  
Fold Stimulation ◽  
86Rb Influx ◽  
Stimulation Of

The stimulating effect of excitation on the Na(+)-K+ pump was characterized in measurements of 22Na efflux, intracellular Na+ content, 86Rb influx, and [3H]ouabain binding in isolated rat soleus muscle. Direct stimulation (10 V, 1 ms, 2 Hz) rapidly increased 22Na efflux and 86Rb influx about twofold. These effects were blocked by tetracaine and ouabain, were not associated with any significant increase in intracellular Na+, and could not be attributed to a rise in extracellular K+. The stimulation of 22Na efflux was unaffected by tubocurarine, dantrolene, trifluoperazine, or bumetanide. Stimulation at 2 Hz increased the rate of [3H]ouabain binding by approximately 120% within 1 min, indicating an early specific activation of the Na(+)-K+ pump. Stimulation at 60 Hz for 10 s increased intracellular Na+ content by 58%. Reextrusion of Na+ was complete in 2 min and could be prevented by ouabain (10(-4) M) or by cooling to 0 degrees C. It is concluded that, in rat soleus muscle, excitation leads to a rapid and pronounced (up to 15-fold) stimulation of the Na(+)-K+ pump, even at modest increases in intracellular Na+. This activation mechanism may be essential for the maintenance of transmembrane Na(+)-K+ gradients and prompt recovery of excitability during contractile activity.

scholarly journals Insulin stimulation of pyruvate dehydrogenase in adipocytes involves two distinct signalling pathways

2003 ◽  
Vol 369 (2) ◽  
pp. 351-356 ◽  
Author(s):  
Sam A. JOHNSON ◽  
Richard M. DENTON
Keyword(s):  
Pyruvate Dehydrogenase ◽  
Mitogen Activated Protein Kinase ◽  
Signalling Pathways ◽  
Maximal Effect ◽  
Insulin Stimulation ◽  
Rat Adipocytes ◽  
Extracellular Signal ◽  
Mitogen Activated Protein ◽  
Phosphoinositide 3 Kinase ◽  
Stimulation Of

In isolated rat adipocytes, the insulin stimulation of pyruvate dehydrogenase can be partially inhibited by inhibitors of PI3K (phosphoinositide 3-kinase) and MEK1/2 (mitogen-activated protein kinase/extracellular signal-regulated kinase kinase). In combination, U0126 and wortmannin completely block the insulin stimulation of pyruvate dehydrogenase. It is concluded that the effect of insulin on pyruvate dehydrogenase in rat adipocytes involves two distinct signalling pathways: one is sensitive to wortmannin and the other to U0126. The synthetic phosphoinositolglycan PIG41 can activate pyruvate dehydrogenase but the activation is only approx. 30% of the maximal effect of insulin. This modest activation can be completely blocked by wortmannin alone, suggesting that PIG41 acts through only one of the pathways leading to the activation of pyruvate dehydrogenase.

scholarly journals Osmotic and phorbol ester-induced activation of Na+/H+ exchange: possible role of protein phosphorylation in lymphocyte volume regulation.

1985 ◽  
Vol 101 (1) ◽  
pp. 269-276 ◽  
Author(s):  
S Grinstein ◽  
S Cohen ◽  
J D Goetz ◽  
A Rothstein
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Time Course ◽  
Phorbol Esters ◽  
Underlying Mechanism ◽  
Atp Depletion ◽  
Sequence Of Events ◽  
Kinase C ◽  
Stimulation Of

The Na+/H+ antiport is stimulated by 12-O-tetradecanoylphorbol-13, acetate (TPA) and other phorbol esters in rat thymic lymphocytes. Mediation by protein kinase C is suggested by three findings: (a) 1-oleoyl-2-acetylglycerol also activated the antiport; (b) trifluoperazine, an inhibitor of protein kinase C, blocked the stimulation of Na+/H+ exchange; and (c) activation of countertransport was accompanied by increased phosphorylation of specific membrane proteins. The Na+/H+ antiport is also activated by osmotic cell shrinking. The time course, extent, and reversibility of the osmotically induced and phorbol ester-induced responses are similar. Moreover, the responses are not additive and they are equally susceptible to inhibition by trifluoperazine, N-ethylmaleimide, and ATP depletion. The extensive analogies between the TPA and osmotically induced effects suggested a common underlying mechanism, possibly activation of a protein kinase. It is conceivable that osmotic shrinkage initiates the following sequence of events: stimulation of protein kinase(s) followed by activation of the Na+/H+ antiport, resulting in cytoplasmic alkalinization. The Na+ taken up through the antiport, together with the HCO3- and Cl- accumulated in the cells as a result of the cytoplasmic alkalinization, would be followed by osmotically obliged water. This series of events could underlie the phenomenon of regulatory volume increase.

scholarly journals Mucin release and calcium fluxes in isolated rat submandibular acini

1984 ◽  
Vol 224 (2) ◽  
pp. 473-481 ◽  
Author(s):  
M A McPherson ◽  
R L Dormer
Keyword(s):  
Time Course ◽  
Dose Dependence ◽  
Trypan Blue Exclusion ◽  
Mechanical Dispersion ◽  
Intracellular Calcium Mobilization ◽  
Submandibular Acini ◽  
Mucin Release ◽  
Net Release ◽  
Isolated Rat ◽  
Stimulation Of

A method is described for preparing isolated rat submandibular acini by collagenase digestion followed by mechanical dispersion. As assessed by Trypan Blue exclusion, phase contrast microscopy, ATP content and release of mucins and lactate dehydrogenase, the acini are morphologically and functionally intact. Secretory function of isolated acini was similar to that of intact tissue in terms of time-course, dose dependence and degree of stimulation of mucin release by adrenergic secretagogues. Mucin release was increased to the same extent (approx. 3-4-fold) by either isoproterenol or noradrenaline at a maximally effective concentration (10 microM). Stimulation of mucin release by isoproterenol (10 microM), noradrenaline (10 microM) or adrenaline (10 microM) was inhibited by propranolol (30 microM) but not by phentolamine (30 microM). Isoproterenol (10 microM) increased both 45Ca2+ uptake and efflux from the acini, which was shown to represent a net release of calcium. However, there was a delay (approx. 10 min) in onset of stimulation of 45Ca2+ mobilization which was not apparent in isoproterenol stimulation of mucin release. Our results indicate that increases in intracellular calcium mobilization in response to a beta-adrenergic secretagogue do not trigger mucin secretion from rat submandibular acini.

scholarly journals Translocation of the brain-type glucose transporter largely accounts for insulin stimulation of glucose transport in BC3H-1 myocytes

1990 ◽  
Vol 269 (3) ◽  
pp. 597-601 ◽  
Author(s):  
D M Calderhead ◽  
K Kitagawa ◽  
G E Lienhard ◽  
G W Gould
Keyword(s):  
Glucose Transport ◽  
Glucose Transporter ◽  
Fold Increase ◽  
The Other ◽  
Insulin Stimulation ◽  
Glut 1 ◽  
Glut 4 ◽  
Rat Soleus Muscle ◽  
The Brain ◽  
Stimulation Of

Insulin-stimulated glucose transport was examined in BC3H-1 myocytes. Insulin treatment lead to a 2.7 +/- 0.3-fold increase in the rate of deoxyglucose transport and, under the same conditions, a 2.1 +/- 0.1-fold increase in the amount of the brain-type glucose transporter (GLUT 1) at the cell surface. It has been shown that some insulin-responsive tissues express a second, immunologically distinct, transporter, namely GLUT 4. We report here that BC3H-1 myocytes and C2 and G8 myotubes express only GLUT 1; in contrast, rat soleus muscle and heart express 3-4 times higher levels of GLUT 4 than GLUT 1. Thus translocation of GLUT 1 can account for most, if not all, of the insulin stimulation of glucose transport in BC3H-1 myocytes. On the other, hand, neither BC3H-1 myocytes nor the other muscle-cell lines are adequate as models for the study of insulin regulation of glucose transport in muscle tissue.

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