Journal
MOLECULAR REPRODUCTION AND DEVELOPMENT
Volume 62, Issue 3, Pages 348-356Publisher
WILEY-LISS
DOI: 10.1002/mrd.90002
Keywords
Na+ pump; ATP1AL2; NHE1; NHE5; sperm motility
Funding
- NHLBI NIH HHS [R01HL28573, T32HL07382, P01HL41496] Funding Source: Medline
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The Na,K-ATPase generates electrochemical gradients that are used to drive the coupled transport of many ions and nutrients across the plasma membrane. The functional enzyme is comprised of an a and P subunit and families of isoforms for both subunits exist. Recent studies in this laboratory have identified a biological role for the Na,K-ATPase alpha4 isoform in sperm motility. Here we further investigate the role of the Na, K-ATPase carrying the a4 isoform, showing again that ouabain eliminates sperm motility, and in addition, that nigericin, a H+/K+ ionophore, and monensin, a H+/Na+ ionophore, reinitiate motility. These data, along with the observation that the K+ ionophore valinomycin has no effect on the motility of ouabain-inhibited sperm, suggest that ouabain may change intracellular H+ levels in a manner that is incompatible with sperm motility. We have also localized NHE1 and NHE5, known regulators of intracellular H+ content, to the same region of the sperm as the Na,K-ATPase a4 isoform. These data highlight the important role of the Na,K-ATPase a4 isoform in regulating intracellular H+ levels, and provide evidence suggesting the involvement of the Na+/H+ exchanger, which is critical for maintaining normal sperm motility.
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