Androgen receptor in rat liver: characterization and separation from a male-specific estrogen-binding protein
| Autor: | Patricia K. Eagon, Brian J. Rogerson, Sandra M. Seguiti, Lynne E. Porter, Terence F. McGuire, Daniel H. Seeley |
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| Rok vydání: | 1989 |
| Předmět: |
Male
medicine.medical_specialty medicine.drug_class medicine.medical_treatment Ovariectomy Biophysics Biology urologic and male genital diseases Biochemistry Cytosol Reference Values Internal medicine medicine Animals Estrenes Molecular Biology Testosterone Congeners Hypophysectomy Cell Nucleus Sex Characteristics Estradiol Androgen binding Binding protein Dihydrotestosterone Rats Inbred Strains Metribolone Androgen Ligand (biochemistry) Rats Androgen receptor Steroid hormone Kinetics Endocrinology Liver Receptors Estrogen Estrogen Sex steroid Receptors Androgen Female Carrier Proteins Orchiectomy |
| Zdroj: | Archives of biochemistry and biophysics. 268(1) |
| ISSN: | 0003-9861 |
| Popis: | Many liver processes are sexually dimorphic. In particular, the microsomal content of specific enzymes and the synthesis of specific proteins are under sex steroid hormone control. Because the liver of male rats is strikingly androgen responsive, we sought evidence for an androgen receptor in this tissue. We detected and characterized both cytosolic and nuclear androgen-binding proteins. Both forms bind [3H]R1881 (methyltrienolone, 17β-hydroxy-17α-methyl-4,9,11-estratriene-3-one) with the high affinity, low capacity, and specificity for androgens and antiandrogens characteristic of androgen receptors. No high-affinity binding of [3H]DHT could be detected in unfractionated cytosol because of the rapid metabolism of this ligand; however, binding of a DHT metabolite to the high-capacity male-specific estrogen binder (MEB) of cytosol was observed. Both gel filtration and heparin-Sepharose affinity chromatography separate the cytosolic androgen receptor from MEB. Incubation of cytosol in the absence of sodium molybdate resulted in androgen-binding activity which was retained by DNA-cellulose. Castration of male rats results in a time-dependent loss of both cytosolic and nuclear androgen binding, as well as a loss in MEB activity. Androgen-binding activity is low in livers from female rats, but can be induced by testosterone treatment. An intact pituitary is necessary for maintenance of androgen-binding activity, as hypophysectomy results in complete loss of activity. |
| Databáze: | OpenAIRE |
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