Estrogen receptors in human prostate: Evidence for multiple binding sites

Peter Ekman, Evelyn R. Barrack, Geoffrey L. Greene, Elwood V. Jensen, Patrick C. Walsh

Research output: Contribution to journalArticlepeer-review


The existence of estrogen receptors in the human prostate has long been a controversial issue. This may be explained partly by the apparent heterogeneity of estrogenbinding sites in prostatic tissue. We herein report on multiple binding sites for estrogens in cytosol as well as nuclear preparations of human prostatic tissues. One class of binding sites corresponds to the classical, high affinity estrogen receptor; the Kd for [3H]estradiol binding to the receptor was approximately 0.10 nM and the binding was specific for estrogens. The second class of binding sites appeared to have a Kd for [3H]estradiol in the range of 5–10 nM. This second, lower affinity class of binding sites markedly influenced studies of the classical receptor even at low ligand concentrations. Saturation analysis should be performed over a wide range of ligand concentrations (0.05–10 nM) to allow separation of the two binding components. Quantitation of estrogen receptor by a single point assay cannot be carried out accurately unless the low affinity binding component can be blocked. Multiple binding sites for estradiol were observed in the cytosol as well as in the nuclear salt extractable and saltresistant compartments of normal, benign hyperplastic, and cancerous human prostates. Normal peripheral and cancerous prostates contained significantly (P < 0.01) higher amounts of cytosol estrogen receptor compared to benign hyperplastic tissue.

Original languageEnglish (US)
Pages (from-to)166-176
Number of pages11
JournalJournal of Clinical Endocrinology and Metabolism
Issue number1
StatePublished - Jul 1983

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Endocrinology
  • Clinical Biochemistry
  • Biochemistry, medical


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