QUANTIFICATION OF ANDROGEN BINDING, ANDROGEN TISSUE LEVELS, AND SEX HORMONE-BINDING GLOBULIN IN PROSTATE, MUSCLE AND PLASMA OF PATIENTS WITH BENIGN PROSTATIC HYPERTROPHY

1977 ◽  
Vol 86 (1) ◽  
pp. 200-215 ◽  
Author(s):  
M. Krieg ◽  
W. Bartsch ◽  
S. Herzer ◽  
H. Becker ◽  
K. D. Voigt
Keyword(s):  
Binding Capacity ◽  
Benign Prostatic Hypertrophy ◽  
Average Concentration ◽  
Sex Hormone ◽  
Prostatic Hypertrophy ◽  
Sex Hormone Binding Globulin ◽  
Receptor Protein ◽  
Hormone Binding ◽  
Tissue Levels

ABSTRACT The in vitro binding of 5α-dihydrotestosterone (5α-DHT) in benign prostatic hypertrophy (BPH), rectus abdominis muscle and plasma of 14 patients was characterized and quantified by agargel electrophoresis. The respective endogenous tissue and plasma levels of 5α-DHT and testosterone (T) were determined by radioimmunoassay, and the plasmatic sex hormone-binding globulin (SHBG) concentration was estimated in the 14 patients by an (NH4)2SO4 precipitation technique. Finally the in vitro conversion of 5α-DHT to the 5α-androstanediols in the BPH at 0°C after a 20–24 h incubation period was analyzed by thin-layer chromatography. The main results were as follows: (1) In 12 out of 14 BPH cytosols three charcoal resistant binding peaks were found, of which peak 1 represents SHBG, peak 2 the specific receptor protein and peak 3 a binding protein with relatively high binding capacity and low affinity for 5α-DHT. In two cases peak 2 was absent. In 11 out of 14 muscle cytosols three binding peaks are also present, resembling those of the BPH. (2) The receptor peak is reduced on average 38 % by unlabelled 5α-DHT, 23 % by cyproterone acetate (CYAC) and 29 % by oestradiol. The parallel data for the SHBG peak are: 62% by 5α-DHT, 22% by CYAC and 49% by oestradiol. (3) From displacement studies with unlabelled 5α-DHT the average concentration of receptor was calculated to be 12.3 fmol/mg cytosol protein (CP) in BPH, and 3.6 fmol/mg CP in muscle. Under identical conditions 39.9 fmol SHBG/mg CP and 24.1 fmol/mg CP were found in the BPH and muscle, respectively. The mean values are significantly different (P < 0.001). In plasma a mean value of 4.0 × 10−8 mol SHBG/1 was found. (4) In the BPH on average 4.43 ng 5α-DHT/g tissue and 0.23 ng T/g tissue are present, in muscle 0.45 ng 5α-DHT/g tissue and 0.71 ng T/g tissue, in plasma 0.47 ng 5α-DHT/ml and 3.89 ngT/ml. (5) Statistical calculations revealed (a) a significantly (P < 0.05) negative correlation between the endogenous 5α-DHT and T tissue levels and the available 5α-DHT receptor sites in BPH cytosol, (b) a positive correlation between plasmatic SHBG concentration and the available SHBG concentration in BPH cytosol. (6) Compared to the rat prostate, where 36 % of the incubated 5α-DHT was converted at 0°C within 20–24 h into the 5α-androstanediols, in the BPH conversion to 5α-androstanediols was negligible.

PLASMA SEX HORMONE-BINDING GLOBULIN BINDING CAPACITY IN BENIGN PROSTATIC HYPERTROPHY AND PROSTATIC CARCINOMA: COMPARISON WITH AN AGE DEPENDENT RISE IN NORMAL HUMAN MALES

1977 ◽  
Vol 84 (1) ◽  
pp. 207-214 ◽  
Author(s):  
M. Dennis ◽  
H.-J. Horst ◽  
M. Krieg ◽  
K. D. Voigt
Keyword(s):  
Prostatic Carcinoma ◽  
Binding Capacity ◽  
Benign Prostatic Hypertrophy ◽  
Sex Hormone ◽  
Prostatic Hypertrophy ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Age Dependent ◽  
The Mean ◽  
Age Range

ABSTRACT A method for the routine determination of plasma sex hormone-binding globulin (SHBG) binding capacity is introduced. In normal males an age dependent increase in SHBG binding capacity from 2.85 × 10−8 m in the age range 22–44 years to 4.66 × 10−8 m in the age range 45–64 years was found. A higher mean value of 6.41 × 10−8 m was obtained in normal females, 20–40 years old, and still higher values were found in females taking oral contraceptives. Although in male groups with benign prostatic hypertrophy or prostatic carcinoma the mean ages were somewhat higher than in the older normal group, a further age dependent increase in SHBG binding capacity in these diseases could not be demonstrated. In fact the mean values found were slightly although not significantly lower at 4.07 and 3.89 × 10−8 m, respectively. As expected, oestrogen treatment of males with prostatic carcinoma produced higher values.

DISTRIBUTION AND CONCENTRATIONS OF ANDROGENS IN EPITHELIAL AND STROMAL COMPARTMENTS OF THE HUMAN BENIGN HYPERTROPHIC PROSTATE

1981 ◽  
Vol 90 (1) ◽  
pp. 125-131 ◽  
Author(s):  
N. J. BOLTON ◽  
RIITTA LAHTONEN ◽  
G. L. HAMMOND ◽  
R. VIHKO
Keyword(s):  
Column Chromatography ◽  
Benign Prostatic Hypertrophy ◽  
Sex Hormone ◽  
Prostatic Hypertrophy ◽  
The Other ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Androgen Metabolism ◽  
Cell Basis ◽  
Important Site

Prostate tissues removed from patients with benign prostatic hypertrophy were separated into epithelial and stromal components and the concentrations of testosterone, 5α-dihydrotestosterone, 5α-androstane-3α,17β-diol, 4-androstene-3,17-dione, 5α-androstanedione stanedione and androsterone in these two fractions were determined by radioimmunoassays after the purification of solvent steroid extracts by Lipidex-5000 column chromatography. On a 'per cell' basis (i.e. relative to DNA), testosterone was equally distributed between the two components, while the other androgens measured were more abundant in the stroma. The observation that 5α-reduced androgens (especially 5α-dihydrotestosterone) were more concentrated in the stroma, and that significant correlations between concentrations of metabolically related androgens were more common in the stroma than in the epithelium, indicate that the stroma is an important site of androgen metabolism in benign prostatic hypertrophic tissues. The present data also support the suggestion that 5α-dihydrotestosterone produced in the prostatic stroma may be transferred to the epithelium by way of sex hormone binding globulin in the extracellular spaces of the prostate.

IN VITRO STUDIES OF TESTOSTERONE AND 5α-DIHYDROTESTOSTERONE BINDING IN BENIGN PROSTATIC HYPERTROPHY

1974 ◽  
Vol 75 (4) ◽  
pp. 773-784 ◽  
Author(s):  
P. Steins ◽  
M. Krieg ◽  
H. J. Hollmann ◽  
K. D. Voigt
Keyword(s):  
High Speed ◽  
Biological Fluids ◽  
Benign Prostatic Hypertrophy ◽  
Prostatic Hypertrophy ◽  
Sex Hormone Binding Globulin ◽  
List Type ◽  
Plasma Samples ◽  
Experimental Conditions ◽  
Displacement Experiments

ABSTRACT The cytosol fractions of prostatic adenoma and of the rectus abdominis muscle, together with the respective plasma samples were investigated in 13 patients in order to clarify whether or not there is an androgen receptor in human benign prostatic hypertrophy. The following methods were used: High speed ultracentrifugation in a sucrose gradient and agar gel electrophoresis at low temperature, of the 100 000 g supernatants after in vitro incubation with 3H-testosterone, 3H-5α-dihydrotestosterone, and 3H-oestradiol-17β. In parallel experiments the supernatants were heated to 45°C for 1 h before the steroid incubation. Displacement experiments with a 100–500-fold excess of various cold androgens. In the supernatants as well as in the plasma samples the total protein concentration was measured by the biuret reaction. The concentration of albumin and of immunoglobulin G (IgG) in the various biological fluids was determined by quantitative immuno diffusion. After charcoal stripping the binding of testosterone and of 5α-dihydrotestosterone was estimated quantitatively and correlated to the plasma contamination. By the methods used no physico-chemical differences in the androgen binding properties of plasma and of prostate cytosol were observed. However, in any individual cytosol a higher 5α-DHT binding than could be related to the plasma contamination was obtained. The question therefore remains open, as to whether the augmented 5α-dihydrotestosterone binding relates to a cellular increase of sex hormone binding globulin (SHBG) or to androgen receptors which do not show up clearly under the experimental conditions used.

Influence of sex hormone binding globulin and serum albumin on the conversion of androstenedione to testosterone by human erythrocytes

1981 ◽  
Vol 96 (1) ◽  
pp. 136-140 ◽  
Author(s):  
M. Egloff ◽  
N. Savouré ◽  
J. Tardivel-Lacombe ◽  
C. Massart ◽  
M. Nicol ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Sex Hormone ◽  
Human Erythrocytes ◽  
Sex Hormone Binding Globulin ◽  
Total Plasma ◽  
Hormone Binding ◽  
High Binding Affinity

Abstract. The influence of human serum albumin and sex hormone binding globulin (SHBG) on the enzymic conversion of androstenedione to testosterone in human erythrocytes was investigated in vitro. Total plasma and albumin delayed the conversion rate of androstenedione, while SHBG increased it markedly. The effect of SHBG was largely abolished by heating to 60°C for 1 h and by saturating its binding sites by DHT. The effect of both proteins was found to be related to their concentration. It appears that the binding sites of albumin provide a mechanism for retarding androstenedione uptake by the erythrocytes and that the high binding affinity of SHBG for testosterone facilitates the diffusion of this steroid out of the cell and thus, displaces the chemical equilibrium within the cell.

scholarly journals Protective Effect of Sex Hormone-Binding Globulin against Metabolic Syndrome: In Vitro Evidence Showing Anti-Inflammatory and Lipolytic Effects on Adipocytes and Macrophages

2018 ◽  
Vol 2018 ◽  
pp. 1-12 ◽  
Author(s):  
Hiroki Yamazaki ◽  
Akifumi Kushiyama ◽  
Hideyuki Sakoda ◽  
Midori Fujishiro ◽  
Takeshi Yamamotoya ◽  
...  
Keyword(s):  
Metabolic Syndrome ◽  
Protective Effect ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Lipid Degradation ◽  
Protein Levels ◽  
Anti Inflammatory ◽  
20 Nm

Sex hormone-binding globulin (SHBG) is a serum protein released mainly by the liver, and a low serum level correlates with a risk for metabolic syndrome including diabetes, obesity, and cardiovascular events. However, the underlying molecular mechanism(s) linking SHBG and metabolic syndrome remains unknown. In this study, using adipocytes and macrophages, we focused on the in vitro effects of SHBG on inflammation as well as lipid metabolism. Incubation with 20 nM SHBG markedly suppressed lipopolysaccharide- (LPS-) induced inflammatory cytokines, such as MCP-1, TNFα, and IL-6 in adipocytes and macrophages, along with phosphorylations of JNK and ERK. Anti-inflammatory effects were also observed in 3T3-L1 adipocytes cocultured with LPS-stimulated macrophages. In addition, SHBG treatment for 18 hrs or longer significantly induced the lipid degradation of differentiated 3T3-L1 cells, with alterations in its corresponding gene and protein levels. Notably, these effects of SHBG were not altered by coaddition of large amounts of testosterone or estradiol. In conclusion, SHBG suppresses inflammation and lipid accumulation in macrophages and adipocytes, which might be among the mechanisms underlying the protective effect of SHBG, that is, its actions which reduce the incidence of metabolic syndrome.

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