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The serum transport of steroid hormones.
Monosaccharide-induced lipogenesis regulates the human hepatic sex hormone-binding globulin gene.
- D. Selva, K. Hogeveen, S. Innis, G. Hammond
- Biology, MedicineThe Journal of clinical investigation
- 3 December 2007
Monosaccharide-induced lipogenesis reduced hepatic HNF-4alpha levels, which in turn attenuated SHBG expression, providing a biological explanation for why SHBG is a sensitive biomarker of the metabolic syndrome and the metabolic disturbances associated with increased fructose consumption.
Plasma steroid-binding proteins: primary gatekeepers of steroid hormone action
- G. Hammond
- Biology, MedicineThe Journal of endocrinology
- 1 July 2016
Understanding how the unique structures of SHBG and CBG determine their specialized functions, how changes in their plasma levels are controlled, and how they function outside the blood circulation provides insight into how they control the freedom of steroids to act in health and disease.
Genetic Determinants of Serum Testosterone Concentrations in Men
A meta-analysis of genome-wide association data in 8,938 men from seven cohorts identified genetic loci significantly associated with serum testosterone concentration in men that could influence the calculation of free testosterone using law-of-mass-action equation.
Diverse Roles for Sex Hormone-Binding Globulin in Reproduction1
- G. Hammond
- BiologyBiology of reproduction
- 1 September 2011
This review compares the production and functions of sex hormone-binding globulin in different species and evaluates the diverse effects this has on reproduction.
Hepatocyte Nuclear Factor-4 Controls Transcription from a TATA-less Human Sex Hormone-binding Globulin Gene Promoter*
Data imply that an interplay between COUP-TF and H NF-4 at a site within FP1 regulates human SHBG expression and that HNF-4 controls transcription from this TATA-less promoter by somehow substituting for Tata-binding protein in the recruitment of a transcription preinitiation complex.
Crystal structure of human sex hormone‐binding globulin: steroid transport by a laminin G‐like domain
- I. Grishkovskaya, G. Avvakumov, G. Sklenar, D. Dales, G. Hammond, Y. Muller
- Chemistry, BiologyThe EMBO journal
- 15 February 2000
The crystal structure of the N‐terminal G domain of SHBG in complex with 5α‐dihydrotestosterone at 1.55 Å resolution reveals both the architecture of the steroid‐binding site and the quaternary structure ofThe dimer, and shows that G domains have jellyroll topology and are structurally related to pentraxin.
Human Sex Hormone-binding Globulin Promoter Activity Is Influenced by a (TAAAA) n Repeat Element within an Alu Sequence*
It is found that a (TAAAA) n pentanucleotide repeat, located within an alu sequence at the 5′ boundary of the human SHBG promoter, influences its transcriptional activity in association with downstream elements, including an SP1-binding site.
Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors.
There is a remarkable similarity between the amino acid sequences of CBG and of alpha 1-antitrypsin, and this extends to other members of the serpin (serine protease inhibitor) superfamily.
A role for corticosteroid-binding globulin in delivery of cortisol to activated neutrophils.
- G. Hammond, C. Smith, N. Paterson, W. Sibbald
- Biology, MedicineThe Journal of clinical endocrinology and…
- 1 July 1990
A physiological role for CBG in the delivery of cortisol to sites of inflammation is suggested and three small molecular size fragments are detected after elastase cleavage, and carbohydrate analysis of these fragments suggests that they represent the same polypeptide fragment which has been differentially glycosylated.