Properties of Androphilic Proteins in Cytosols of Human Benign Prostatie Hypertrophy

Kodama, Takaomi; Shimazaki, Jun

doi:10.1507/endocrj1954.26.449

Cited by 3 publications

(1 citation statement)

References 23 publications

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“…The nuclei extract of the human prostates with high ionic KC1 showed a high affinity binding to dihydrotestosterone [8]. A previous report from this laboratory showed that 3H-dihydrotestosterone complcxed with two proteins in prostatic cytosols fractionated on Se phadex was equally bound to nuclei of the human prostate [9]. Since 'H-dihvdrotestosterone complexed with testosterone-binding globulin was not bound to nuclei in vitro, androphilic proteins in cytosols of the human prostate seem to be heterogenous.…”

Section: Discussionmentioning

confidence: 81%

Binding of Dihydrotestosterone, R 1881 and R 5020 in Cytosols from Normal, Benign Hypertrophic and Cancerous Human Prostates

Nozumi¹,

Sato²,

Itô³

et al. 1981

Urol Int

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The binding of dihydrotestosterone, R 1881 and R 5020 as examined in cytosols of normal, benign hypertrophic and cancerous tissues of the human prostates. Almost all samples obtained by open operation showed high affinity binding to these ligands. Dissociation constants of the binding to these ligands were approximately 10^––9M irrespective of the pathological state of the prostates. Maximum binding sites for dihydrotestosterone seemed to be greater in normal tissues than in the pathological ones. However, maximum binding sites for R 1881 and R 5020 were not significantly different among the normal and pathological prostates examined in the present study. Moreover, some correlation was observed between the maximum binding sites for R 1881 and those for R 5020. The samples resected by TUR seemed to be inadequate for analyses of androgen binding.

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Section: Discussionmentioning

confidence: 81%

Binding of Dihydrotestosterone, R 1881 and R 5020 in Cytosols from Normal, Benign Hypertrophic and Cancerous Human Prostates

Nozumi¹,

Sato²,

Itô³

et al. 1981

Urol Int

Self Cite

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Androphilic proteins in the human prostate

et al. 1981

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Dihydrotestosterone‐binding protein in cytosols from human prostates was different from the R1881‐and R5020‐binding proteins. The R1881‐and R5020‐binding proteins in the cytosol were very similar and most of the binding sites for R1881 were capable of binding R5020. However, nuclear extracts showed equal binding to dihydrotestosterone and R1881, but not to R5020, suggesting that there might not be a progestin receptor in the human prostate. Maximum binding sites to dihydrotestosterone, R1881, and R5020 in cytosols were very similar among “normal” and pathological prostates except that dihy‐drotestosterone binding was higher in “normal” prostates than in the pathological ones. Histochemically, R1881‐binding was observed in the epithelial cells and in malignant cells, but not in the stroma.

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Progestin-binding protein in human benign prostatic hypertrophy.

et al. 1981

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Cytosols from human benign prostatic hypertrophy contained progestin-binding components which bound to R 5020, ORG 2058 andprogesterone in a high affinity fashion.Most of the protein bound to R 5020 was recovered in the precipitate with 0-30% saturation of ammonium sulfate. The R 5020-binding protein showed sedimentation coefficients of 3.6 S and 8.4 S, and was eluted in the void volume of a Sephadex G-200 column. This protein was clearly distinguished from the dihydrotestosterone-binding protein by its precipitability by ammonium sulfate, heat stability and susceptibility to delipidization. R 5020 and ORG 2058 binding were markedly inhibited by the addition of R 1881, therefore, most ofthe binding to progestin in cytosols from the benign prostatic hypertrophy seems to be also the sites for R 1881. Although nuclear extract by 0.4 M KC1 showed R 1881 binding, the extract did not contain the R 5020-binding protein, and this suggestedthat the progestin-binding protein observed in the cytosols does not seem to be the steroid receptor.

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Properties of Androphilic Proteins in Cytosols of Human Benign Prostatie Hypertrophy

Cited by 3 publications

References 23 publications

Binding of Dihydrotestosterone, R 1881 and R 5020 in Cytosols from Normal, Benign Hypertrophic and Cancerous Human Prostates

Binding of Dihydrotestosterone, R 1881 and R 5020 in Cytosols from Normal, Benign Hypertrophic and Cancerous Human Prostates

Androphilic proteins in the human prostate

Progestin-binding protein in human benign prostatic hypertrophy.

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