Molecular Human Reproduction, Vol 4, 251-258, Copyright © 1998 by Oxford University Press
M Luconi, C Krausz, T Barni, GB Vannelli, G Forti and E Baldi
Mitogen-activated protein kinases (MAPK), also known as extracellular
signal-regulated kinases (ERKs) are cytoplasmic and nuclear
serine/threonine kinases involved in signal transduction of several
extracellular effectors. Recently, we have demonstrated that ERKs are
present in spermatozoa and are involved in the regulation of the process of
capacitation. We report here the effect of progesterone, a well-known
inducer of the acrosome reaction in mammalian spermatozoa, on the
immunolocalization, phosphorylation and activity of ERKs in capacitated
human spermatozoa. We demonstrated that short-term incubation of
spermatozoa with progesterone induces phosphorylation and activation of
ERKs, resulting in redistribution of the proteins from the post-acrosomal
region to the equatorial segment within the sperm head. To investigate the
role of ERKs on the biological effects of progesterone, we used the MAPK
cascade inhibitor PD098059, which strongly inhibited progesterone-induced
activation of ERK-2. This compound did not inhibit progesterone-induced
acrosome reaction, although it prevented redistribution of the enzyme to
the equatorial region of the sperm head. These results suggest that the two
processes, although temporally related, are independent. In conclusion, we
provide new insight into the signal transduction pathways involved in the
non- genomic action of progesterone in spermatozoa and suggest a possible
involvement of ERKs in the process of fertilization.
JOURNAL ARTICLE
Progesterone stimulates p42 extracellular signal-regulated kinase (p42erk) in human spermatozoa
Dipartimento di Fisiopatologia Clinica, Universita di Firenze, Italy.
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