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Am J Physiol Cell Physiol 275: C826-C831, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 3, C826-C831, September 1998

Mechanism of depression in cardiac sarcolemmal Na+-K+-ATPase by hypochlorous acid

Kiminori Kato, Qiming Shao, Vijayan Elimban, Anton Lukas, and Naranjan S. Dhalla

Institute of Cardiovascular Sciences, St. Boniface General Hospital Research Centre, and Department of Physiology, Faculty of Medicine, University of Manitoba, Winnipeg, Manitoba, Canada R2H 2A6

Oxidative stress during pathological conditions such as ischemia-reperfusion is known to promote the formation of hypochlorous acid (HOCl) in the heart and to result in depression of cardiac sarcolemmal (SL) Na+-K+-ATPase activity. In this study, we examined the direct effects of HOCl on SL Na+-K+-ATPase from porcine heart. HOCl decreased SL Na+-K+-ATPase activity in a concentration- and time-dependent manner. Characterization of Na+-K+-ATPase activity in the presence of different concentrations of MgATP revealed a decrease in the maximal velocity (Vmax) value, without a change in affinity for MgATP on treatment of SL membranes with 0.1 mM HOCl. The Vmax value of Na+-K+-ATPase, when determined in the presence of different concentrations of Na+, was also decreased, but affinity for Na+ was increased when treated with HOCl. Formation of acylphosphate by SL Na+-K+-ATPase was not affected by HOCl. Scatchard plot analysis of [3H]ouabain binding data indicated no significant change in the affinity or maximum binding capacity value for ouabain binding following treatment of SL membranes with HOCl. Western blot analysis of Na+-K+-ATPase subunits in HOCl-treated SL membranes showed a decrease (34 ± 9% of control) in the beta 1-subunit without any change in the alpha 1- or alpha 2-subunits. These data suggest that the HOCl-induced decrease in SL Na+-K+-ATPase activity may be due to a depression in the beta 1-subunit of the enzyme.

oxidative stress; sarcolemmal sodium-potassium-adenosinetriphosphatase; sarcolemmal ouabain binding; pig heart; sodium-potassium-adenosinetriphosphatase subunits


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