Molecular Human Reproduction, Vol. 8, No. 2, 124-135,
February 2002
© 2002 European Society of Human Reproduction and Embryology
Testis and spermatogenesis |
The extracellular signal-regulated kinase (ERK) pathway is involved in human sperm function and modulated by the superoxide anion
Urology Research Laboratory, Royal Victoria Hospital and McGill University, Montréal, Québec, Canada
Our aim was to ascertain the role of the extracellular signal-regulated protein kinase (ERK) pathway in human sperm capacitation induced by fetal cord serum ultrafiltrate (FCSu) and its regulation by the superoxide anion (O2-·). Immunoblotting indicated the presence of Shc, Grb2, Rasp21, Raf and ERK1 and 2 (ERK1/2) in spermatozoa. Grb2, Rasp21, Raf and MEK inhibitors dose-dependently prevented sperm capacitation and protein tyrosine phosphorylation, without modifying sperm O2-· production. Therefore, the whole ERK cascade plays a role in capacitation, downstream of O2-· but upstream of protein tyrosine phosphorylation. Upon incubation with FCSu, the early (5 min) increase in ERK1/2 activity (as shown by double phosphorylation of the Thr-Glu-Tyr motif) was followed by an important decrease over the next 2 h; superoxide dismutase did not change this pattern. The phosphorylation of the Thr-Glu-Tyr motif present in other sperm proteins (16–33 kDa) also increased (5 min incubation with FCSu) and then progressively decreased, and this effect was regulated by O2-·, MEK and cAMP. The phospho-Ser/Thr-Pro content (characteristic of ERK1/2 substrates) of Triton-insoluble proteins (75 and 80 kDa) increased during capacitation and also appeared to be regulated by O2-· and the ERK pathway. Inhibition of ERK1/2 activation reduced lysophosphatidylcholine-induced acrosome reaction and the associated protein tyrosine phosphorylation. These results support a role for the ERK pathway in human sperm function.
acrosome reaction/dual specificity kinase/mitogen-activated protein kinase/signal transduction/tyrosine phosphorylation
1 To whom correspondence should be addressed at: Urology Research Laboratory, H6.47, Royal Victoria Hospital,687 ave des Pins ouest, Montréal, Qué Canada H3A 1A1. E-mail: edelamirande{at}hotmail.com
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