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Originally published In Press as doi:10.1074/jbc.M002323200 on April 10, 2000

J. Biol. Chem., Vol. 275, Issue 27, 20693-20699, July 7, 2000
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Sperm Motility Is Dependent on a Unique Isoform of the Na,K-ATPase*

Alison L. Woo, Paul F. James, and Jerry B LingrelDagger

From the Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0524

The Na,K-ATPase, a member of the P-type ATPases, is composed of two subunits, alpha  and beta , and is responsible for translocating Na+ out of the cell and K+ into the cell using the energy of hydrolysis of one molecule of ATP. The electrochemical gradient it generates is necessary for many cellular functions, including establishment of the plasma membrane potential and transport of sugars and ions in and out of the cell. Families of isoforms for both the alpha  and beta  subunits have been identified, and specific functional roles for individual isoforms are just beginning to emerge. The alpha 4 isoform is the most recently identified Na,K-ATPase alpha  isoform, and its expression has been found only in testis. Here we show that expression of the alpha 4 isoform in testis is localized to spermatozoa and that inhibition of this isoform alone eliminates sperm motility. These data describe for the first time a biological function for the alpha 4 isoform of the Na,K-ATPase, revealing a critical role for this isoform in sperm motility.

* This work was supported by National Institutes of Health Grants RO1HL28573 and PO1HL41496 (to J. B L.) and Training Grant T32HL07382 (to A. L. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence and reprint requests should be addressed: Dept. of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati College of Medicine, 231 Bethesda Ave., Cincinnati, OH 45267-0524. E-mail: Jerry.Lingrel@uc.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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