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The Journal of Clinical Endocrinology & Metabolism Vol. 84, No. 5 1670-1678
Copyright © 1999 by The Endocrine Society

Original Studies

Identification and Characterization of a Novel Functional Estrogen Receptor on Human Sperm Membrane That Interferes with Progesterone Effects

Michaela Luconi, Monica Muratori, Gianni Forti and Elisabetta Baldi

Dipartimento di Fisiopatologia Clinica, Unita’ di Andrologia, Università di Firenze, I-50139 Florence, Italy

Address all correspondence and requests for reprints to: Michaela Luconi or Elisabetta Baldi, Dipartimento di Fisiopatologia Clinica, Unità di Andrologia, Università di Firenze, viale Pieraccini 6, I-50139 Florence, Italy. E-mail: m.luconi{at}dfc.unifi.it

The presence of a novel functional estrogen receptor on the human sperm surface has been demonstrated by using different experimental approaches. Ligand blot analysis of sperm lysates, using peroxidase-conjugated estradiol as probe, identified a specific estradiol-binding protein of approximately 29-kDa apparent molecular mass. The same protein band was also revealed by using {alpha}H222 antibody, which is directed against the steroid binding domain of the genomic estrogen receptor. The biological effects of estrogen receptor were investigated by analyzing calcium fluxes, tyrosine phosphorylation, and acrosome reaction (AR) in response to 17ß-estradiol (17ßE2) and by measuring the steroid influence on calcium and AR in responses to progesterone (P), a well-known physiological stimulus for human spermatozoa. Our results demonstrate that 17ßE2 induces a rapid and sustained increase of intracellular calcium concentrations ([Ca2+]i). This effect is totally dependent on the presence of extracellular calcium, because it is completely abolished in a calcium-depleted medium. The dose-response curve for calcium increase to 17ßE2 is biphasic with a first component in the nanomolar range (effective concentration 50 = 0.60 ± 0.12 nmol/L) and a second component in the micromolar range (EC50 = 3.80 ± 0.26 µmol/L). 17ßE2 stimulates tyrosine phosphorylation of several sperm proteins, including the 29-kDa protein band, and determines a reduction of calcium response to P, finally resulting in inhibition of P-stimulated sperm AR. Conversely, no direct effect of 17ßE2 is observed on AR. 17ßE2 effects on calcium are clearly mediated by a membrane receptor, because they are reproduced by the membrane-impermeable conjugate of the hormone BSA-E2 and reduced by sperm preincubation with {alpha}H222 antibody. Taken together, our results clearly show the presence of a functional surface estrogen receptor, of 29 kDa, on human spermatozoa. This receptor may play a role in the modulation of nongenomic action of P in these cells during the process of fertilization.




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