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Journal of Andrology, Vol. 23, No. 5, September/October 2002
Copyright © American Society of Andrology

Activation of Protein Kinase A During Human Sperm Capacitation and Acrosome Reaction

LINDA LEFIÈVRE*, KULA N. JHA{dagger}, EVE DE LAMIRANDE*, PABLO E. VISCONTI{dagger} AND CLAUDE GAGNON*

From the * Urology Research Laboratory, Royal Victoria Hospital and Faculty of Medicine, McGill University, Montréal, Québec, Canada; and the {dagger} Center for Research in Contraception and Reproductive Health, Department of Cell Biology, University of Virginia, Charlottesville, Virginia.

Correspondence to: Dr Claude Gagnon, Urology Research Laboratories, Room H6.47, Royal Victoria Hospital, 687 Ave des Pins ouest, Montréal, Québec, Canada H3A 1A1 (e-mail: claude.gagnon{at}muhc.mcgill.ca).


Spermatozoa undergo a variety of changes during their life that are prerequisites to their maturation and ability to fertilize eggs. Mammalian sperm capacitation and acrosome reaction are regulated by signal transduction systems involving cyclic adenosine monophosphate (cAMP) as a second messenger. This second messenger acts through the activation of protein kinase A (PKA) and indirectly regulates protein tyrosine phosphorylation. cAMP levels are controlled by a balance of phosphodiesterases (PDEs) and adenylyl cyclase (AC) enzymatic activities, which are responsible for its degradation and production, respectively. The aim of this study was to evaluate the possible relationship between the intracellular levels of cAMP and PDE and PKA activities during human sperm capacitation induced by fetal cord serum ultrafiltrate (FCSu) and acrosome reaction induced by calcium ionophore A23187. We report that PKA activity was higher in capacitating than in noncapacitating spermatozoa and that intracellular levels of cAMP decreased but that PDE activity remained constant during capacitation. The acrosome reaction induced by A23187 was associated with increases in cAMP and PKA activity but not in PDE activity. These results strongly suggest that net cAMP concentration is under the control of AC, since PDE activity is constant during sperm capacitation and the acrosome reaction. Moreover, the results suggest that low levels of cAMP are sufficient for capacitation and PKA activation and/or that the cAMP concentration measured in whole spermatozoa does not reflect the effective intracellular cAMP levels present in specific compartments of these cells.

     Key words: Phosphodiesterases, cyclic adenosine monophosphate, calcium ionophore A23187, signal transduction




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