Affiliation:
1. Department of Biochemistry (Division of Chemical Endocrinology), Medical Faculty, Erasmus University Rotterdam, Rotterdam, The Netherlands
Abstract
The specificity of the binding of oestradiol-17β by cytoplasmic fractions of several tissues of the male rat was investigated. 1. Agar-gel electrophoresis, Sephadex chromatography, adsorption by dextran-coated charcoal and sucrose-gradient centrifugation were used to estimate the binding capacity and specificity. The four different methods all gave similar results for the capacity of the specific oestradiol-17β-binding macromolecules in the testis. 2. The presence of a specific saturable binding protein with a sedimentation coefficient of 8S was demonstrated in liver, adrenal, pituitary, prostate, epididymis and testis interstitial tissue. The highest concentration of oestradiol-17β-binding macromolecules was found in testis interstitial tissue (0.12pmol/mg of protein) and in the pituitary (0.075pmol/mg of protein). 3. The oestradiol-17β receptor in the testis cytosol showed the characteristics of a protein with respect to Pronase treatment and temperature sensitivity. In competition experiments with different steroids the receptor showed a high affinity for oestradiol-17β, a moderate affinity for diethylstilboestrol and oestradiol-17α and a low affinity for oestrone, oestriol, testosterone and 5α-dihydrotestosterone (17β-hydroxy-5α-androstan-3-one). 4. The wide distribution of oestradiol-17β receptors in the male rat is in apparent contradiction to the current concept of the specificity of steroid-hormone action. Further research is required to investigate a possible physiological meaning of the presence of specific receptors in the different tissues.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
112 articles.
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