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Am J Physiol Cell Physiol 286: C813-C820, 2004. First published November 19, 2003; doi:10.1152/ajpcell.00389.2003
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MEMBRANE TRANSPORTERS, ION CHANNELS, AND PUMPS

Na+ pump {alpha}2-isoform specifically couples to contractility in vascular smooth muscle: evidence from gene-targeted neonatal mice

Daniel A. Shelly,1 Suiwen He,2 Amy Moseley,2 Craig Weber,3 Michelle Stegemeyer,1 Ronald M. Lynch,3 Jerry Lingrel,2 and Richard J. Paul1

Departments of 1Molecular and Cellular Physiology and 2Molecular Genetics, Biochemistry, and Microbiology, College of Medicine, University of Cincinnati, Ohio 45267-0576; and 3Department of Physiology, College of Medicine, University of Arizona, Tucson, Arizona 85724-5017

Submitted 9 September 2003 ; accepted in final form 15 November 2003

The relative expression of {alpha}1 - and {alpha}2-Na+/K+-ATPase isoforms found in vascular smooth muscle is developmentally regulated and under hormonal and neurogenic control. The physiological roles of these isoforms in vascular function are not known. It has been postulated that the {alpha}1-isoform serves a "housekeeping" role, whereas the {alpha}2-isoform localizes to a subsarcolemmal compartment and modulates contractility. To test this hypothesis, isoform-specific gene-targeted mice in which the mRNA for either the {alpha}1- or the {alpha}2-Na+/K+-ATPase isoform was ablated were utilized. Both of these knockouts, and , are lethal; the latter dies at birth, which allows this neonatal aorta to be studied. Isometric force in -aorta was more sensitive to contractile agonists and less sensitive to the vasodilators forskolin and sodium nitroprusside (SNP) than wild-type (WT) aorta; -aortas had intermediate values. In contrast, neonatal -aorta was similar to WT. Western blot analysis indicated a population of 70% {alpha}1- and 30% {alpha}2-isoforms in the WT. Thus in terms of the total Na+/K+-ATPase protein, the -aorta (at 70%) would be similar to the -aorta (at 65%) but with a dramatically different phenotype. These data suggest that individual {alpha}-isoforms of the Na+/K+-ATPase differ functionally and that the {alpha}2-isoform couples more strongly to activation-relaxation pathways. Three-dimensional image-acquisition and deconvolution analyses suggest that the {alpha}2-isoform is distributed differently than the {alpha}1-isoform. Importantly, these isoforms do not localize to the same regions.

sodium; potassium; ATPase; contraction; transgenic


Address for reprint requests and other correspondence: R. J. Paul, Dept. of Molecular and Cellular Physiology, Univ. of Cincinnati College of Medicine, 231 Albert Sabin Way, Cincinnati, OH 45267-0576 (E-mail: Richard.Paul{at}uc.edu).




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