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Originally published In Press as doi:10.1074/jbc.M206284200 on December 19, 2002

J. Biol. Chem., Vol. 278, Issue 9, 7001-7009, February 28, 2003
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Involvement of a Na+/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> Cotransporter in Mouse Sperm Capacitation*

Ignacio A. DemarcoDagger , Felipe Espinosa§, Jennifer EdwardsDagger , Julian SosnikDagger , José Luis de la Vega-Beltrán§, Joel W. Hockensmith, Gregory S. Kopf||**, Alberto Darszon§, and Pablo E. ViscontiDagger Dagger Dagger

From the Dagger  Center for Research in Contraception and Reproductive Health, Department of Cell Biology, and the  Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia 22908, § Universidad Autonoma de Mexico, Cuebnavaca, Mexico, and || Center for Research in Reproduction and Women's Health, University of Pennsylvania, Philadelphia, Pennsylvania 19104

Mammalian sperm are incapable of fertilizing eggs immediately after ejaculation; they acquire fertilization capacity after residing in the female tract for a finite period of time. The physiological changes sperm undergo in the female reproductive tract that render sperm able to fertilize constitute the phenomenon of "sperm capacitation." We have demonstrated that capacitation is associated with an increase in the tyrosine phosphorylation of a subset of proteins and that these events are regulated by an HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>/cAMP-dependent pathway involving protein kinase A. Capacitation is also accompanied by hyperpolarization of the sperm plasma membrane. Here we present evidence that, in addition to its role in the regulation of adenylyl cyclase, HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> has a role in the regulation of plasma membrane potential in mouse sperm. Addition of HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> but not Cl- induces a hyperpolarizing current in mouse sperm plasma membranes. This HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>-dependent hyperpolarization was not observed when Na+ was replaced by the non-permeant cation choline+. Replacement of Na+ by choline+ also inhibited the capacitation-associated increase in protein tyrosine phosphorylation as well as the zona pellucida-induced acrosome reaction. The lack of an increase in protein tyrosine phosphorylation was overcome by the presence of cAMP agonists in the incubation medium. The lack of a hyperpolarizing HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> current and the inhibition of the capacitation-dependent increase in protein tyrosine phosphorylation in the absence of Na+ suggest that a Na+/HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> cotransporter is present in mouse sperm and is coupled to events regulating capacitation.

* This work was supported by National Institutes of Health Grants HD38082 (to P. E. V.), HD06274, and HD22732 (to G. S. K.), by CONACyT, and DGAPA IN201599 (to A. D.), and by the Mellon Foundation.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.

** Present address: Wyeth Ayerst P. O. Box 8299, Philadelphia, PA 19101-8299.

Dagger Dagger To whom correspondence should be addressed: Department of Veterinary and Animal Sciences, Paige Labs, University of Massachusetts, Amherst, MA 01003. E-mail: pevb61@yahoo.com.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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