Journal of Applied Physiology AJP: Heart and Circulatory Physiology
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J Appl Physiol 93: 1457-1465, 2002. First published July 5, 2002; doi:10.1152/japplphysiol.00440.2002
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Vol. 93, Issue 4, 1457-1465, October 2002

Exercise effects on muscle beta -adrenergic signaling for MAPK-dependent NKCC activity are rapid and persistent

Aidar R. Gosmanov, Nicholas C. Nordtvedt, Richard Brown, and Donald B. Thomason

Department of Physiology, College of Medicine, University of Tennessee Health Science Center, Memphis, Tennessee 38163

This study investigated exercise adaptation of signaling mechanisms that control Na+-K+-2Cl- cotransporter (NKCC) activity in rat skeletal muscle. An acute bout of exercise increased total and NKCC-mediated 86Rb influx. Inhibition of extracellular signal-regulated kinase (ERK) activation abolished the exercise-induced NKCC upregulation. Treadmill training (20 m/min, 20% grade, 30 min/day, 5 days/wk) stimulated total 86Rb influx and increased NKCC activity in the soleus muscle after 2 wk and in the plantaris muscle after 4 wk. Exercise-induced NKCC activity was associated with a 1.4- to 2-fold increase in ERK phosphorylation. Isoproterenol, which activates ERK and NKCC in sedentary muscle, caused a remarkable inhibition of the exercise-induced NKCC activity. Furthermore, isoproterenol inhibition of exercise-induced NKCC activity was accompanied with decreased ERK phosphorylation in the plantaris muscle. Akt (protein kinase B) phosphorylation on both Thr308 and Ser473, which activates Akt and inhibits NKCC activity in sedentary muscle, was stimulated by acute and chronic exercise. This Akt activation was unaffected by isoproterenol. These results indicate an immediate and persistent exercise adaptation of the signal pathways that participate in the control of potassium transport.

potassium transport; extracellular signal-regulated kinase; mitogen-activated protein kinase; Akt; p38; endurance exercise


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