Sex-hormone-binding globulin in human follicular fluid and serum at the time of oocyte recovery

1989 ◽  
Vol 1 (4) ◽  
pp. 289 ◽  
Author(s):  
SM Campo ◽  
PA Rogers ◽  
JK Findlay

Androgen binding activity, indistinguishable from sex-hormone-binding globulin (SHBG) in serum, has been identified in human follicular fluid by binding analyses (saturation and Scatchard analyses and binding specificity), immunoradiometric assay and Con-A Sepharose chromatography. Follicular fluid was obtained at the time of oocyte recovery from either individual follicles (range 2-7) from seven patients, or as a pool obtained from follicles of several patients who had received a Clomid-human menopausal gonadotrophin treatment to stimulate follicular growth as part of an in vitro fertilization program. Concentrations of SHBG in follicular fluid varied between individual follicles (750 +/- 202 fmol mg-1 protein; mean +/- s.d.; n = 14) and ranged above and below concentrations of SHBG in serum (948 +/- 171 fmol mg-1 protein; n = 5) taken 4 h before oocyte recovery and harvest of follicular fluid. There were strong correlations (r = 0.7-0.9) between the steroid and SHBG contents in individual follicular fluids of two patients. However, the concentration of SHBG in follicular fluid was generally 100-fold lower than that of oestradiol or progesterone, suggesting that SHBG may play some role other than determining the concentration of unbound steroid in the follicle.

1995 ◽  
Vol 50 (1-2) ◽  
pp. 98-104 ◽  
Author(s):  
Dietmar Ganßer ◽  
Gerhard Spiteller

Abstract A test system is described, which allows the search for compounds interfering with human sex hormone-binding globulin (SHBG) even in complex plant extracts. The method has been evaluated and applied to Urtica dioica root extracts. The lignan secoisolariciresinol (5) as well as a mixture of isomeric (11 E)-9,10,13-trihydroxy-11-octadecenoic and (10 E)-9 ,12,13-trihydroxy-10-octadecenoic acids (3 and 4, resp.) were demonstrated to reduce binding activity of human SHBG. Methylation of the mixture of 3 and 4 increased its activity about 10-fold.


1992 ◽  
Vol 343 (1) ◽  
pp. 79-80
Author(s):  
P. Luppa ◽  
I. Schwab ◽  
D. Neumeier ◽  
D. Seidel ◽  
T. Strowitzki

1981 ◽  
Vol 96 (1) ◽  
pp. 136-140 ◽  
Author(s):  
M. Egloff ◽  
N. Savouré ◽  
J. Tardivel-Lacombe ◽  
C. Massart ◽  
M. Nicol ◽  
...  

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.


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