Human Sex Hormone-Binding Globulin Binding Affinities of 125 Structurally Diverse Chemicals and Comparison with Their Binding to Androgen Receptor, Estrogen Receptor, and α-Fetoprotein

2014 ◽  
Vol 143 (2) ◽  
pp. 333-348 ◽  
Author(s):  
Huixiao Hong ◽  
William S. Branham ◽  
Hui Wen Ng ◽  
Carrie L. Moland ◽  
Stacey L. Dial ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Androgen Receptor ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Binding Affinities ◽  
Hormone Binding

Binding of Phytoestrogens to Rat Uterine Estrogen Receptors and Human Sex Hormone-binding Globulins

2005 ◽  
Vol 60 (7-8) ◽  
pp. 649-656 ◽  
Author(s):  
Pablo Ibieta Hillerns ◽  
Yuangang Zu ◽  
Michael Wink
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptors ◽  
Conformational Changes ◽  
Nordihydroguaiaretic Acid ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Scatchard Analysis ◽  
Binding Affinities ◽  
Hormone Binding ◽  
17Β Estradiol

The interaction of phytoestrogens with the most important binding sites of steroid hormones, i.e. sex hormone-binding globulin and estrogen receptors, was investigated. Relative binding affinities and association constants for 21 compounds among them isoflavones, flavones, flavonols, flavanones, chalcones and lignans were determined. The lignan nordihydroguaiaretic acid weakly displaced 17β-[3H]-estradiol from estrogen receptor and Scatchard analysis suggests non-conformational changes. Compounds from Glycyrrhiza glabra, liquiritigenin and isoliquiritigenin, showed estrogenic affinities to both receptors. 18β-Glycyrrhetinic acid displaced 17β-[3H]-estradiol from sex hormone-binding globulin but not from the estrogen receptor. Phytoestrogens compete with 17β-estradiol much stronger than with 5α-dihydrotestosterone for binding to sex hormone-binding globulin.

Genetic polymorphism of the human sex hormone-binding globulin: Evidence of an isoelectric focusing variant with normal androgen-binding affinities

1990 ◽  
Vol 36 (6) ◽  
pp. 541-548 ◽  
Author(s):  
Fernando Larrea ◽  
Rosa Maria Oliart ◽  
Julio Granados ◽  
Osvaldo Mutchinick ◽  
Vicente Diaz-Sanchez ◽  
...  
Keyword(s):  
Genetic Polymorphism ◽  
Isoelectric Focusing ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Binding Affinities ◽  
Hormone Binding ◽  
Androgen Binding

scholarly journals Sex Hormone-Binding Globulin Mediates Prostate Androgen Receptor Action via a Novel Signaling Pathway

Endocrinology ◽  
1998 ◽  
Vol 139 (1) ◽  
pp. 213-218 ◽  
Author(s):  
Victor D. H. Ding ◽  
David E. Moller ◽  
William P. Feeney ◽  
Varsha Didolkar ◽  
Atif M. Nakhla ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Signaling Pathway ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Receptor Action

Sex Hormone-Binding Globulin and Estrogen Receptor in Breast Cancer: Technique and Preliminary Clinical Results*

1978 ◽  
Vol 46 (6) ◽  
pp. 998-1006 ◽  
Author(s):  
YOICHI MURAYAMA ◽  
TOMOKO SAKUMA ◽  
HIDEO UDAGAWA ◽  
JOJI UTSUNOMIYA ◽  
RYOHEI OKAMOTO ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Clinical Results ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding

scholarly journals Reduced levels of stromal sex hormone-binding globulin and androgen receptor dysfunction in the sperm storage region of the rat epididymis

Reproduction ◽  
2018 ◽  
Vol 155 (6) ◽  
pp. 467-479 ◽  
Author(s):  
Fabiane de Santi ◽  
Flávia L Beltrame ◽  
Barry T Hinton ◽  
Paulo S Cerri ◽  
Estela Sasso-Cerri
Keyword(s):  
Androgen Receptor ◽  
Epithelial Cells ◽  
Sperm Storage ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Male Rats ◽  
Hormone Binding ◽  
Storage Region ◽  
Duct Diameter ◽  
The Impact

The cauda epididymidis is the major sperm storage region whose androgenic supply, essential for the sperm viability, is provided by the vasculature and is dependent upon testosterone diffusion through the stromal tissue to reach the epithelial cells. We have focused our efforts on examining the regulation of this important epididymal region by evaluating the impact of the androgen disrupter cimetidine on the epithelial–stromal androgenic microenvironment. Male rats received 100 mg/kg cimetidine (CMTG) or saline (CG) for 50 days, serum testosterone levels were measured and the epididymal cauda region was processed for light and transmission electron microscopy. In the proximal cauda region, the duct diameter was measured and birefringent collagen in the stroma was quantified. TUNEL-labeled epithelial cells were quantified, and androgen receptor (AR), karyopherin alpha (KPNA) and sex hormone-binding globulin (SHBG) levels were analyzed by immunofluorescence and Western blot. CMTG showed reduced duct diameter and high number of apoptotic epithelial cells. In the epithelium, the total AR concentration and the KPNA immunoreactivity were reduced, and a weak/absent AR nuclear immunofluorescence was observed in contrast to the enhanced AR immunolabeling observed in the cytoplasm of the epithelial cells. A significant reduction of collagen and SHBG levels in the stroma was also observed. Cimetidine treatment impairs AR nuclear import in the epithelium, causing androgenic dysfunction and subsequent epithelial cell apoptosis and duct atrophy. The connective tissue atrophy and reduction of SHBG stromal levels associated with epithelial androgenic dysfunction indicate a possible role of stromal SHBG in the androgenic supply of the sperm storage region of the epididymis.

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