Corticosteroid-binding globulin

Among the numerous corticosteroid-binding proteins that have been demonstrated to exist throughout the vertebrates, the corticosteroid-binding globulins (CBG or transcortin) of man and guinea pig have been most thoroughly investigated. Both are glycoproteins that contain one binding site for corticosteroid hormones and other steroids. The binding forces are predominantly of a hydrophilic nature, in addition to hydrophobic interaction. Human CBG forms a reversible dimer that maintains full binding affinity and capacity. The monomeric form is composed of two electrophoretic variants that appear indistinguishable in their chemical, immunological, and steroid binding properties. Thermodynamic analysis indicates different binding mechanisms for human and cavian CBG at the lower and higher temperature range. Entrance of hydroxy groups into the steroid molecule increases the affinity to CBG; the contributions to the free energy of complex formation, resulting from individual substitutions or other alterations in the steroid molecule, are additive. Determination of binding specificity leads to a conceptual image of the steroid binding site with respect to the nature of the various binding domains.     

Sex hormone-binding globulin and thyroxine-binding globulin levels in premature thelarche

Premature thelarche is defined as the isolated development of breast tissue in girls less than 8 years of age. Although breast development is an estrogen-dependent process, these girls do not have elevated serum estrogen levels, and the hormonal basis for their condition is unclear. We studied the levels of two estrogen-dependent transport proteins, sex hormone-binding globulin (SHBG) and thyroxine-binding globulin (TBG), in order to determine if there was evidence for a more subtle estrogen effect in girls with premature thelarche. SHBG levels in girls with premature thelarche were not significantly different from those of prepubertal girls of the same ages and were significantly lower than those in girls undergoing pubertal development at the appropriate age (P less than 0.05) and in normal women (P less than 0.001). There was no statistically significant difference in TBG levels between the girls with premature thelarche and prepubertal controls. There was also no significant difference in TBG levels between prepubertal girls and girls in early puberty. In contrast, women had TBG levels that were significantly lower than those in all girls studied. We conclude that the estrogen exposure (whether endogenous or exogenous) of girls with premature thelarche is less than that of girls in early true puberty and similar to that of other prepubertal girls. Further, changes in serum TBG are not as sensitive an indicator of estrogen effect as is breast development or changes in SHBG. This study also suggests that large amounts of exogenous estrogens are not an element in the development of premature thelarche.     

Plasma variation of corticosteroid-binding globulin and sex hormone-binding globulin.

Sex hormone-binding globulin (SHBG) and corticosteroid-binding globulin (CBG) circulate in plasma and bind their cognate ligands with high affinity, offering a steroid delivery system to target tissues by a variety of mechanisms. Analysis of these steroid-binding proteins is gaining importance in the clinical setting, although more information is warranted on their diurnal and biological variation. This study shows that plasma SHBG (in normal subjects) exhibits little diurnal or biological variation over the 30 day period studied, in contrast to CBG, where plasma levels peak in the early afternoon. This leads to attenuation of the diurnal free cortisol level rhythm compared to total cortisol. We also show that plasma CBG is significantly lower in male subjects with the metabolic syndrome compared to age-matched lean counterparts, and may therefore act as a surrogate marker of insulin resistance. The consequence of lower levels of CBG in these obese male subjects is reflected by higher levels of circulating free cortisol, potentially offering a more favourable environment for adipogenesis.     

Network structure and forces involved in perilla globulin gelation: comparison with sesame globulin

Scanning electron micrographs show that perilla globulin gel had a finer network structure than sesame α-globulin gel. The effects of various reagents on the gel formation and solubility of perilla and sesame gels were compared. The contribution of disulfide bonds to the formation and stability of perilla gel was greater than to sesame gel, despite having the same subunit structure.