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Dipartimento di Fisiopatologia Clinica, Unità di Andrologia, Università di Firenze, I-50139 Firenze, Italy
Address all correspondence and requests for reprints to: Elisabetta Baldi, Ph.D., Dipartimento di Fisiopatologia Clinica, Unità di Andrologia, Università di Firenze, Viale Pieraccini 6, I-50139 Florence, Italy. E-mail: e.baldi{at}mednuc2.dfc.unifi.it
The presence of functional nongenomic progesterone (P) receptors in
human spermatozoa has been investigated by equilibrium binding studies
in intact spermatozoa, ligand blot and Western blot analysis of sperm
lysates, as well as determination of the effects of the steroid on
sperm intracellular Ca2+ concentrations. Binding
experiments were performed using
progesterone-11
-glucuronide-[125I]iodotyramine as
tracer. Computer analysis of competition curves using different
steroids as competitors indicated the presence of two distinct binding
sites for P. The high affinity site (Kd in the nanomolar
range) appears to be specific for P, whereas the low affinity one
(Kd in the micromolar range) binds with equal affinity
11ß-hydroxyprogesterone (11ßOHP) and 17-hydroxyprogesterone
(17OHP). A significant correlation exists among affinity constants
(as determined by binding studies) and EC50 values for the
effects of P, 11ßOHP, and 17OHP on intracellular Ca2+
in fura-2-loaded spermatozoa, strongly indicating the involvement of
P-binding sites in the biological effect of the steroid. In particular,
dose-response curves for P were biphasic, with an EC50 in
the nanomolar range and another in the micromolar range. Conversely,
curves for 11ßOHP and 17OHP were monophasic, with an
EC50 just in the micromolar range. Ligand blot analysis of
sperm total lysates performed with peroxidase-conjugated P revealed the
presence of two binding proteins of 54 and 57 kDa that were specific
for P. Indeed, peroxidase-conjugated P binding was blocked by the
simultaneous presence of the unconjugated steroid. Using c262
antibody, which is directed against the P-binding domain of genomic
receptor, we detected two proteins of similar molecular mass (54 and 57
kDa), whereas using antibodies directed against the DNA-binding and
N-terminal domains of the genomic P receptors, the two proteins were
not detected. In addition, p54 and p57 appear to be mostly localized in
sperm membranes and virtually absent in the cytoplasm. The involvement
of these proteins in the biological effects of P is indicated by the
strong inhibitory effect of c262 on P-induced acrosome reaction of
capacitated human spermatozoa.
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