Characterization of a specific estrogen receptor in the oviduct of the little skate, Raja erinacea

In this study we report the first estrogen receptor to be characterized in an oviparous elasmobranch. The skate receptor has high affinity for estradiol (Kd = 0.7 nM), binds both estradiol and the synthetic estrogen DES, and exists in low quantities (50-100 fmol/g oviduct). The receptor displays rapid binding kinetics with half-times of 5 min at 22 degrees and 77 min at 4 degrees. DEAE-Sepharose chromatography reveals one receptor moiety which elutes between 0.13 and 0.14 M KCl. By sucrose gradient ultracentrifugation sedimentation coefficients of 3.6 S under high-salt (0.5 M KCl) and 6.0 S under low salt (0.01 M KCl) conditions were obtained. Using Sephadex G200 gel filtration chromatography, a Stokes radius (Rs) of 2.8 nm and an estimated molecular weight of 43 kDa were calculated. DNA-cellulose elution profiles reveal that the receptor elutes as one peak between 0.34 and 0.36 M NaCl (as compared to 0.20-0.22 M NaCl in mammals and birds and 0.55 M for dogfish). Although some differences are noted between the elasmobranch ER and those of other vertebrates (e.g., dissociation kinetics, DNA affinity), in general it can be said that the skate ER is a "classical" ER in most respects. It is suggested that this steroid receptor has played a key role in the reproductive tract functions of nutrient provision, embryo protection, and as a conduit to the external environment since the earliest chordate era, approximately 400 million years ago.