First published online December 15, 2003
Journal of Cell Science 117, 201e (2004)
© The Company of Biologists Limited
Sperm capacity decreased
Prior to fertilization, spermatozoa must undergo capacitation - a maturation process in which they react to signals in the female reproductive tract and acquire the ability to undergo tyrosine phosphorylation in response to cyclic AMP. Ca2+ is a potential regulator of the process; however, its effects on capacitation and tyrosine phosphorylation are disputed. John Aitken and co-workers now clear up the controversy by demonstrating that Ca2+ negatively regulates this signalling pathway (see p. 211). They confirm the importance of tyrosine phosphorylation for capacitation and show that extracellular Ca2+ reduces its extent in human and mouse spermatozoa. Interestingly, they find that this is associated with reduced ATP levels and can be mimicked by glucose deprivation. Suspecting that Ca2+-dependent ATPases such as the SERCA Ca2+ pump might be involved, the authors go on to demonstrate, using radiolabelled probes, that spermatozoa have many such ATPases. They then show that the SERCA inhibitor thapsigargin also suppresses tyrosine phosphorylation. Their findings thus not only indicate that Ca2+ inhibits tyrosine phosphorylation during capacitation but reveal the importance of ATP-dependent pumps - which could be significant in the context of male infertility, given the known correlation between sperm function and ATP levels.

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Related articles in JCS:
- Analysis of the mechanism by which calcium negatively regulates the tyrosine phosphorylation cascade associated with sperm capacitation
- Mark A. Baker, Louise Hetherington, Heath Ecroyd, Shaun D. Roman, and R. John Aitken
JCS 2004 117: 211-222.
[Abstract]
[Full Text]