Androphilic proteins in cytosols of human benign prostatic hypertrophy.

Abstract

To examine the properties of androphilic proteins in human benign prostatic hypertrophy, the binding capacity and affinity of the proteins were determined after acetone-treatment, ammonium sulfate precipitation and chromatographies of DEAE and Sephadex G-200. Androphilic proteins in the extract of acetone-dried cytosol from the hypertrophic human prostate was precipitated at 30-50% saturation of ammonium sulfate. The binding of this fraction to dihydrotestosterone and testosterone was high affinity, but the binidng to estradiol-17 beta was the one of non-specific. Androphilic proteins in the 30-50% fraction were eluted from DEAE-cellulose column by buffer containing 0.05 M KCL. On Sephadex G-200 chromatography of 30-50% fraction, the androphilic proteins were observed in three peaks; one was eluted in the void volume and other two were eluted at the sites of IgG and albumin. The amount and ratio of proteins eluted in the void volume and the site of IgG from Sephadex G-200 column were variable in individual tissue samples. The chromatographic behavior of the 30-50% fraction in Sephadex G-200 was not changed significantly by introducing 0.4 M KCl in the system. Polyacrylamide gel electrophoresis was applied for further separation of the proteins.

Inhibition by various steroids on dihydrotestosterone binding to androphilic protein in human benign prostatic hypertrophy.

“…In the present study, the acetone-dried cytosol was used for the estimation of the androphilic protein of the human prostate. A part of properties of the androphilic protein in acetone-dried preparations was already reported (Shimazaki et al, 1977 ;Kodama et al, 1977). Recently, a specific steroid binding protein (PBP; prostatic binding protein) was reported by Heyns et al(1976) and Heyns and deMoor (1977), and they stated that the PBP which was prepared from acetone-dried cytosol was different from the androgen receptor of the rodent prostate.…”

“…prostate was heterogenous, but the binding: of this protein to dihydrotestosterone showed. a high-affinity pattern in the saturation analysis (Shimazaki et al, 1977 Protein determination Protein was measured either by the biuret method (Gornall et al, 1949) or by the ultraviolet absorption at 280nm (Tombs et. al., 1959) the inhibition of these compounds were performed.…”

Binding to R 1881 (methyltrienolone) of proteins from human benign prostatic hypertrophy.

“…Previous report showed that the binding ability of cytosol to dihydrotestosterone did not change after delipidization of cytosol by acetone (Kodama et al, 1977). However, the high affinity binding component to R 1881was lost after treatment with acetone.…”

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

“…Although binding of dihydrotestosterone in cytosols from the human prostate showed a single high affinity binding in Scatchard plotting, two binding components were sepa rated on Sephadex chromatography [6]. It has been assumed that one of these binding pro teins is testosterone-binding globulin, but the nature of the other is still unclear [7].…”