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Mol. Hum. Reprod. Advance Access published online on October 18, 2006
Molecular Human Reproduction, doi:10.1093/molehr/gal085
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© The Author 2006. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org
Received August 23, 2006
Revised September 11, 2006
Accepted September 18, 2006

Article

Evidence for the involvement of proline-directed serine/threonine phosphorylation in sperm capacitation

K.N. Jha 1 *, A.M. Salicioni 2 *, E. Arcelay 2, O. Chertihin 3, S. Kumari 3, J.C. Herr 3, and P.E. Visconti 4 *

1 Center for Research in Contraceptive and Reproductive Health, Department of Cell Biology, University of Virginia, Charlottesville, VA, USA
2 Department of Veterinary and Animal Sciences, University of Massachusetts, Amherst, MA, USA
3 Center for Research in Contraceptive and Reproductive Health, Department of Cell Biology, University of Virginia, Charlottesville, VA USA
4 Center for Research in Contraceptive and Reproductive Health, Department of Cell Biology, University of Virginia, Charlottesville, VA USA; Department of Veterinary and Animal Sciences, University of Massachusetts, Amherst, MA, USA

* To whom correspondence should be addressed.
P.E. Visconti, E-mail: pvisconti{at}vasci.umass.edu


  Abstract

To become fertilization competent, mammalian sperm undergo changes in the female reproductive tract termed capacitation. Capacitation correlates with an increase in tyrosine phosphorylation; however, less is known about the role of serine/threonine phosphorylation in this process. Proline-directed phosphorylation is one of the major regulatory phosphorylation events in many cellular processes such as cell proliferation and differentiation. Using mitotic phosphoprotein monoclonal-2 (MPM-2) antibody in this study, we observed that several mouse sperm proteins in the range of 70-250 kDa underwent increased serine/threonine-proline phosphorylation during capacitation. In contrast to the time course of tyrosine phosphorylation, proline-directed phosphorylation could be observed at shorter time points of sperm incubation, and it was found to be independent of NaHCO3 and adenosine 3'5'-cyclic monophosphate (cAMP). Similar to the regulation of the increase in tyrosine phosphorylation, cholesterol acceptors such as bovine serum albumin (BSA) or 2-hydroxypropyl-{beta}-cyclodextrin (2-OH-propyl-{beta}-CD) were essential for the regulation of proline-directed phosphorylation in mouse sperm. Furthermore, it was also found to be BSA dependent in human sperm. Among proline-directed kinases, extracellular signal-regulated kinase 1/2 (ERK1/2) is present in mammalian sperm; nevertheless, U0126 and PD098059, two inhibitors of the ERK pathway, did not block this phosphorylation in mouse sperm. In conclusion, capacitation is associated with an increase in proline-directed phosphorylation linked to cholesterol efflux in the sperm.

Keywords: sperm/capacitation/phosphorylation/kinases/MPM-2.

*The authors equally contributed to this work.


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