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Mol. Hum. Reprod. Advance Access originally published online on October 18, 2006
Molecular Human Reproduction 2006 12(12):781-789; 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

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

K.N. Jha1,*, A.M. Salicioni2,*, E. Arcelay2, O. Chertihin1, S. Kumari1, J.C. Herr1 and P.E. Visconti1,2,3

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

3 To whom correspondence should be addressed at: Department of Veterinary and Animal Sciences, University of Massachusetts, 208 Paige Building, 161 Holdsworth Way, Amherst MA 01003, USA. E-mail: pvisconti{at}vasci.umass.edu

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-ß-cyclodextrin (2-OH-propyl-ß-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.

Key words: sperm/capacitation/phosphorylation/kinases/MPM-2

* The authors equally contributed to this work.


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