Androgen Receptors and Androgen-Dependent Initiation of Protein Synthesis in the Prostate

Liao, Shutsung; Tymoczko, John L; Castañeda, Evangelina; Liang, Tehming

doi:10.1016/s0083-6729(08)60962-0

Cited by 62 publications

(16 citation statements)

References 46 publications

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“…Many reports indicated that the androgen receptor of the rat prostate showed a sedimentation coefficient of 8S in low salt solutions (Liao, 1975, Gorski and Gannon, 1976, Bradlow and Gasparini, 1979. However, 3S component has been generally observed in androgen receptors of the various androgen-target tissues of the rodent (Lea et al, 1979, Wilson andFrench, 1979).…”

Section: Sedimentation and Chromatographic Analysis Of The Bindingmentioning

confidence: 99%

“…It is well known that the human prostate contains several species of protein which show a high affinity binding to androgens (Menon et al, 1977, Shain andBoesel, 1978 (Zava et al, 1979, Asselin et al, 1979 (Liao et al, 1975 17ƒÀ-hydroxy-17ƒ¿-methyl-estra-4,9,11-trien-3-one, specific activity 87 Ci/mmol) and R 5020 ((17ƒ¿-methyl-3H) 17, 21-dimethyl-19-nor-pregna-4, 9-dien-3, 20- …”

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confidence: 99%

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Low molecular weight component of androgen receptor in cytosols from benign hypertrophic human prostate treated with high KCl solution.

1982

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Cytosol of the benign hypertrophic human prostate was prepared in a low salt medium and then the concentration of salt was increased to 0.4 M with . This preparation showed a high affinity binding to R 1881 and the binding was specific for androgens. These results suggest that the binding of the preparation to R 1881 was due mainly to the cytosolic androgen receptor. The R 1881 binding component in the 0.4 M KCl-cytosol was sedimented at 3S by sucrose density gradient centrifugation.The small sedimentation coefficient of the binder seems to be due to the high concentration of salt and not to degradation by proteolytic enzymes in the preparation. The molecular weight, Stokes radius and frictional ratio of this binding component were 32,000, 25.9 A and 1.24, respectively.

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Section: Sedimentation and Chromatographic Analysis Of The Bindingmentioning

confidence: 99%

mentioning

confidence: 99%

Low molecular weight component of androgen receptor in cytosols from benign hypertrophic human prostate treated with high KCl solution.

1982

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“…The sedimentation properties can vary, depending on pH and temperature treatment ofthe receptor preparations as well as the presence of other cellular components, such as nucleic acids or nucleoproteins (12,16), metal ions and thiols (11,17), and proteases (18). In the media containing 0.4 M KCl, the receptor complexes are dissociated from aggregated materials and sediment rather uniformly at 3.8 ± 0.3 S (17). For As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Autoimmune anti-androgen-receptor antibodies in human serum.

Liao¹,

Witte²

1985

Proc. Natl. Acad. Sci. U.S.A.

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Circulating autoantibodies to human and rat androgen receptors are present at high titers in the blood sera of some patients with prostate diseases. The antibodies from some serum samples were associated with a purified IgG fraction and interacted with the 3.8S cytosolic androgen-receptor complexes of rat ventral prostate to form 9-to 12S units. Other serum samples, however, formed 14-to 19S units, suggesting that other immunoglobulins might be involved. In the presence of an anti-human immunoglobulin as a second antibody, the androgen-receptor-antibody complexes could be immunoprecipitated. The antibodies interacted with the nuclear and the cytosolic androgen-receptor complexes, either the DNA-binding or the nonbinding form, but not with receptors for estradiol, progestin, or dexamethasone from a variety of sources. Human testosterone/estradiol-binding globulin, rat epididymal androgen-binding protein, or rat prostate a-protein (a nonreceptor steroid-binding protein) also did not interact with the antibodies to form immunoprecipitates. About 37% of male and 3% of female serum samples screened had significant antibody titer. The chance ofrinding serum with a high titer is much better in males older than 66 years than in the younger males or females at all ages. The presence of the high-titer antibodies may make it possible to prepare monoclonal antibodies to androgen receptors without purification of the receptors for immunization.Steroid receptors are usually characterized by their ability to bind radioactive ligands. The isolation of polyclonal and monoclonal antibodies to estrogen (1, 2), glucocorticoid (3-5), and progestin (6-8) receptors in recent years, however, has provided alternative means to study these hormone receptors. An antibody against androgen receptors, however, has not been produced, mainly because of the difficulty in obtaining androgen receptors in sufficiently pure form and in amounts needed for efficient immunization. In this report, we show that anti-androgen receptor antibodies are present in high titers in blood sera of some male patients having clinical prostate problems. MATERIALS AND METHODSMaterials. 5a- [1,2,3,4,5,6,16,17-3H(N)

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“…This number seems to be comparable to those reported by other investigators; Shain et al(1978) reported0.15 pmoles of dihydrotestosterone or0.29pmoles of R1881per mg DNA as the binding sites of the human hyperplastic prostate nuclei. 2,000-10,000of binding per nucleus of the rat prostate was reported by Liao et al(1975).…”

Section: Discussionmentioning

confidence: 99%

“…The acceptor site for the complex in nuclei was postulated as DNAassociated nonhistone protein (Wang1.978; Klyzsejko-Stefanowicz et al,, 1976). The mode of nuclear binding of hormone-receptor complex so far reported seems to be disputable (reviewed by Gorski and Gannon, 1976;Yamamoto and Alberts, 1976); the restricted and organ-specific binding was reported by Liao et al(1975), and nonspecific and unsaturable binding was described by Chamness et al(1974). Lack of tissue-specificity of the prostatic dihydrotestosterone-receptor complex binding to nuclei was also reported (Ichii, 1975;Ichii et al, 1977).…”

Section: Discussionmentioning

confidence: 99%

Properties of Androphilic Proteins in Cytosols of Human Benign Prostatie Hypertrophy

Kodama

Shimazaki

1979

Endocrinol Japon

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Androgen Receptors and Androgen-Dependent Initiation of Protein Synthesis in the Prostate

Cited by 62 publications

References 46 publications

Low molecular weight component of androgen receptor in cytosols from benign hypertrophic human prostate treated with high KCl solution.

Low molecular weight component of androgen receptor in cytosols from benign hypertrophic human prostate treated with high KCl solution.

Autoimmune anti-androgen-receptor antibodies in human serum.

Properties of Androphilic Proteins in Cytosols of Human Benign Prostatie Hypertrophy

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