scholarly journals Interaction of Lignans with Human Sex Hormone Binding Globulin (SHBG)

1997 ◽  
Vol 52 (11-12) ◽  
pp. 834-843 ◽  
Author(s):  
Matthias Schöttner ◽  
Dietmar Ganßer ◽  
Gerhard Spitelle
Keyword(s):  
Binding Affinity ◽  
Binding Assay ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Protecting Groups ◽  
Hormone Binding ◽  
Substitution Pattern ◽  
Structure And Activity

Abstract Lignans bind to sex hormone-binding globulin (SHBG ). The lignan with the highest binding affinity is (±)-3,4-divanillyltetrahydrofuran. In a double Stobbe condensation - without use of protecting groups - a wide variety of lignans with different substitution pattern in the aromatic and aliphatic part of the molecule was synthesized. These lignans were tested in a SHBG -binding assay which allowed to deduce the following relationship between structure and activity: 1) (±)-diastereoisomers are more active than meso compounds 2.) the 4-hydroxy- 3-methoxy (guajacyl) substitution pattern in the aromatic part is most effective 3.) the activity increases with the decline in polarity of the aliphatic part of the molecule.

A Method for the Determination of Sex Hormone Binding Globulin Using Concanavalin A-Sepharose

1992 ◽  
Vol 29 (2) ◽  
pp. 168-171 ◽  
Author(s):  
J A Whittaker ◽  
M L Cawood ◽  
R E Oakey
Keyword(s):  
Concanavalin A ◽  
Binding Assay ◽  
Solid Phase ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Research Use ◽  
Hormone Binding

A binding assay for sex hormone binding globulin (SHBG) has been developed in which SHBG is saturated with tritiated dihydrotestosterone (DHT). Separation of bound and free DHT is achieved by using Concanavalin A-Sepharose as a solid phase matrix. The method is described and its performance, including linearity, imprecision and comparison with other methods, is assessed. The assay is simple and robust and is suitable for analysis of samples of plasma or serum for clinical or research use.

Modelling the binding affinity of steroids to zebrafish sex hormone-binding globulin

2014 ◽  
Vol 25 (5) ◽  
pp. 407-421 ◽  
Author(s):  
A.K. Saxena ◽  
J. Devillers ◽  
A.R.R. Pery ◽  
R. Beaudouin ◽  
V.M. Balaramnavar ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Binding Affinity Of Steroids

scholarly journals Evaluation of an Immunoassay for Plasma Sex Hormone-Binding Globulin: Comparison with Steroid-Binding Assay under Physiological and Pathological Conditions

1988 ◽  
Vol 25 (4) ◽  
pp. 360-366 ◽  
Author(s):  
S K Cunningham ◽  
T J McKenna
Keyword(s):  
Pregnant Women ◽  
Binding Assay ◽  
Polycystic Ovary ◽  
Binding Capacity ◽  
Binding Activity ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Obese Women ◽  
Hormone Binding ◽  
Normal Men

It is possible that alterations in sex hormone-binding globulin (SHBG) binding capacity are due to changes in binding kinetics rather than changes in concentration and, therefore, the immunoreactivity of SHBG may not reflect the binding activity. In this study an immunoradiometric (IRMA) assay was evaluated and the results compared with those of an established binding capacity assay. The correlation between the results of the IRMA ( y) and binding assay ( x) for 179 specimens was r=0·984, y=0·95 x+5·9. Irrespective of the method used, SHBG values in normal non-pregnant women were significantly ( P<0·05) higher than those in normal men, hirsute women, women with polycystic ovary syndrome, hyperprolactinaemic women and obese women, and were significantly less than those in pregnant women; SHBG levels in hirsute women rose during treatment with certain anovulants and fell in genetic males during the second decade of life independent of androgen levels or activity. While being technically simpler SHBG-IRMA provides comparable results to the classical binding assay, indicating that immunoreactivity is an excellent index of binding activity.

Rabbit sex hormone binding globulin: primary structure, tissue expression, and structure/function analyses by expression in Escherichia coli

1997 ◽  
Vol 153 (3) ◽  
pp. 373-384 ◽  
Author(s):  
W M Lee ◽  
A S T Wong ◽  
A W K Tu ◽  
C-H Cheung ◽  
J C H Li ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Binding Affinity ◽  
Reproductive Tract ◽  
Dissociation Constants ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
High Affinity ◽  
Steroid Binding

Abstract Sex hormone binding globulin (SHBG) is a homodimeric plasma protein found in mammals that binds sex steroids with high affinity and regulates their bioavailability. The protein is identical in structure and properties to the androgen binding protein (ABP) found in the male reproductive tract. We have isolated a 1245-base pair rabbit SHBG cDNA encoding a reading frame for a signal peptide followed by a protein of 367 amino acids, which shares 79·0, 68·1 and 63·2% amino acid identity with the corresponding human, rat and mouse proteins respectively. Northern blot and hot-nested PCR analyses indicated that rabbit SHBG is produced from a 1·6 kilobase mRNA in the liver of both sexes and in the testis. The rabbit SHBG cDNA was inserted into pGEX-1λT for expression of a glutathione S-transferase/SHBG fusion protein in Escherichia coli. The bacterial product bound 5α-dihydrotestosterone (DHT) in the same manner as the corresponding protein in serum. The dissociation constants (Kd) for rabbit and human SHBGs produced in E. coli were 11·1 ± 1·1 nm and 2·1 ± 0·6 nm respectively, and rabbit SHBG formed a less stable protein-steroid complex (t½=5 min) than human SHBG (t½>60 min). Unlike human SHBG, rabbit SHBG does not bind estradiol with high affinity. To aid in the identification of differences in the sequences of rabbit and human SHBG, which determine species differences in steroid-binding affinity and specificity, chimeras containing the 5′-terminal half of SHBG from one species and 3′-terminal half of SHBG from the other species were constructed and expressed. It was found that the chimeric proteins assumed similar steroid-binding affinity and specificity as the wild-type proteins when the amino (N)-terminal half of SHBG was derived from the same species. Replacement of the carboxyl (C)-terminal half of rabbit SHBG by the corresponding region of the human molecule increased the integrity of its steroid-protein complex. This supports the concept that amino acids within the N-terminal half of SHBG constitute the steroid-binding domain while the C-terminal half of the molecule may provide structural stability to the protein and its steroid-binding site. Journal of Endocrinology (1997) 153, 373–384

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