Studies on the role of sex-hormone-binding globulin (SHBG) in benign prostatic hypertrophy in men

1984 ◽  
Vol 16 (2) ◽  
pp. 141-147
Author(s):  
A. Pachman
Keyword(s):  
Benign Prostatic Hypertrophy ◽  
Sex Hormone ◽  
Prostatic Hypertrophy ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding

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.

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.

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.

Role of the Ovary in the Regulation of Sex Hormone Binding Globulin and Its Contribution to Peripheral Levels of Androstenedione

2009 ◽  
Vol 82 (04) ◽  
pp. 29-34 ◽  
Author(s):  
P. Bolufer ◽  
P. Antonio ◽  
R. Garcia ◽  
J. Munoz ◽  
A. Rodriguez ◽  
...  
Keyword(s):  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding

scholarly journals Characterization of mini-protein S, a recombinant variant of protein S that lacks the sex hormone binding globulin-like domain

1998 ◽  
Vol 330 (1) ◽  
pp. 389-396 ◽  
Author(s):  
Merel VAN WIJNEN ◽  
G. Jeanette STAM ◽  
T. G. Glenn CHANG ◽  
C. M. Joost MEIJERS ◽  
H. Pieter REITSMA ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Solid Phase ◽  
Anticoagulant Activity ◽  
Protein S ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Wild Type ◽  
Cofactor Activity

Protein S is a vitamin K-dependent glycoprotein involved in the regulation of the anticoagulant activity of activated protein C (APC). Also, an anticoagulant role for protein S, independent of APC, has been described. Protein S has a unique C-terminal sex hormone binding globulin (SHBG)-like domain that represents about half of the molecule. To define the role of this domain in APC cofactor activity and in binding to C4b-binding protein (C4BP), we have constructed a recombinant protein S molecule of N-terminal residues 1-242 that lacks the SHBG domain (mini-protein S). A panel of monoclonal antibodies directed against the N-terminal region of protein S recognized plasma-derived protein S, wild-type recombinant protein S and mini-protein S with similar affinities, whereas a monoclonal antibody that recognizes an epitope in the SHBG domain did not detect mini-protein S. Mini-protein S did not bind to C4BP in a solid-phase binding assay, and the cofactor activity of mini-protein S was not inhibited by preincubation with C4BP. In a plasma coagulation assay, the cofactor activity of mini-protein S was lower than wild-type or plasma-derived preparations. In contrast, no difference in APC cofactor activities was observed when the preparations were tested in purified systems that monitor the APC-mediated degradation of factors Va or VIIIa. In conclusion, we constructed a protein S molecule that fails to bind C4BP and still displays cofactor activity for APC. This confirms the role of the C-terminal SHBG region in C4BP binding and demonstrates that N-terminal residues 1-242 are sufficient for the expression of APC cofactor activity in a system using purified components. In plasma, however, the C-terminal SHBG region plays a role in the expression of optimal APC cofactor activity.

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