Specific binding of human corticosteroid-binding globulin to cell membranes.

Hryb, Daniel J.; Khan, M S; Romas, Nicholas A.; Rosner, William

doi:10.1073/pnas.83.10.3253

Cited by 77 publications

(37 citation statements)

References 42 publications

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“…In addition, a CBG-like molecule has been identified on plasma membranes of liver (40) and pituitary (4 1) in the rat. Hyrb et al (42) have suggested that the presence of a CBG membrane receptor would simultaneously offer a mechanism for the internalization of CBG through receptor-mediated endocytosis and a reason for the intracellular localization of CBG. The demonstrations of specific binding of human CBG to cell membranes of the human prostate as well as several monkey tissues suggest that CBG may be involved in the transport of steroid hormones into target tissues (42).…”

Section: Discussionmentioning

confidence: 99%

“…Hyrb et al (42) have suggested that the presence of a CBG membrane receptor would simultaneously offer a mechanism for the internalization of CBG through receptor-mediated endocytosis and a reason for the intracellular localization of CBG. The demonstrations of specific binding of human CBG to cell membranes of the human prostate as well as several monkey tissues suggest that CBG may be involved in the transport of steroid hormones into target tissues (42). Such a mechanism could contribute to the shorter tm12 for total corticosterone in older animals having a greater proportion of bound corticosterone ( Fig.…”

Section: Discussionmentioning

confidence: 99%

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Kinetics of Circulating Corticosterone in Infant Rats

1988

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ABSTRACT. Corticosterone plays an important role in the regulation of postnatal development in the rat. Basal concentrations of plasma corticosterone increase markedly during the 3rd wk of life. To date, however, the physiologic bases of this increase have remained unclear. To understand the determinants of circulating concentrations of corticosterone during this period, the plasma half-life of disappearance at steady state (tlh), the apparent volume of distribution, and metabolic clearance rate were determined after injection of a tracer dose of 3H-corticosterone in rats at 12, 16, and 22 days of age. The tlh for total plasma corticosterone decreased with increasing age. The volume of distribution decreased even more steeply and, consequently, the MCR displayed a highly significant decline between 12 and 22 days of age. As plasma concentrations of corticosteroid-binding globulin are known to increase markedly during this period, the t~ of protein-bound corticosterone was measured and that of free corticosterone was computed. At all ages the tth of bound corticosterone was less than that of free corticosterone. Protein binding of the injected 3H-corticosterone increased significantly with development. Thus, increased binding of corticosterone is associated with decreased t~. The increasing association of corticosterone with corticosteroid-binding globulin during this developmental period is the most likely explanation for the steep decline of volume of distribution and thus of the metabolic clearance rate for corticosterone. The latter provides, for the first time, an understanding of the basis of the developmental increase in plasma concentrations of corticosterone. (Pediatr Res 24: 595-599,1988)

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Kinetics of Circulating Corticosterone in Infant Rats

1988

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“…Surface binding sites for CBG have been shown in liver, endometrium, placenta, prostate, spleen, and kidney (Hryb et al, 1986;Maitra et al, 1993;Singer et al, 1988;Strel'chyonok and Avvakumov, 1991). Potential receptors for DBP have been reported on macrophages, trophoblasts, and neutrophils (DiMartino et al, 2007;Gumireddy et al, 2003;Haddad, 1995).…”

Section: Receptors For Steroid Carriers -Surface Binding Sites For Stmentioning

confidence: 99%

“…Most notably, its role in transport of otherwise insoluble glucocorticoids is appreciated. However, the identification of surface binding sites for CBG in a number of steroid-target tissues including liver, endometrium, and spleen (Hryb et al, 1986;Maitra et al, 1993;Singer et al, 1988;Strel'chyonok and Avvakumov, 1991) suggested the existence of membrane receptors for cellular uptake and/or transmembrane signaling of CBG/steroid complexes. To test the relevance of CBG for glucocorticoid action and adrenocortical stress response mice genetically deficient for CBG were generated (Petersen et al, 2006).…”

Section: Mouse Models Of Cbg Deficiencymentioning

confidence: 99%

Cellular uptake of steroid carrier proteins—Mechanisms and implications

Willnow

Nykjaer

2010

Molecular and Cellular Endocrinology

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Steroid hormones are believed to enter cells solely by free diffusion through the plasma membrane. However, recent studies suggest the existence of cellular uptake pathways for carrier-bound steroids. Similar to the clearance of cholesterol via lipoproteins, these pathways involve the recognition of carrier proteins by endocytic receptors on the surface of target cells, followed by internalization and cellular delivery of the bound sterols. Here, we discuss the emerging concept that steroid hormones can selectively enter steroidogenic tissues by receptor-mediated endocytosis; and we discuss the implications of these uptake pathways for steroid hormone metabolism and action in vivo.

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“…Indeed, CBG is a substrate of the serine protease elastase that cleaves CBG in its C-terminal part resulting in the dissociation of the CBG-glucocorticoid complex and the local release of glucocorticoid at sites of inflammation (Pemberton et al 1988;Hammond et al 1990). A larger spectrum of action of CBG is suggested by several studies reporting the presence of CBG membrane receptors in extravascular sites (Hryb et al 1986;Strel'chyonok and Avvakumov 1991;Maitra et al 1993) and the fact that 68% of CBG remains in a cortisol-free state under physiological conditions (Gayrard et al 1996).…”

Section: Orticosteroid-binding Globulin (Cbg) Ismentioning

confidence: 99%

Functional Implication of an Arg307Gly Substitution in Corticosteroid-Binding Globulin, a Candidate Gene for a Quantitative Trait Locus Associated With Cortisol Variability and Obesity in Pig

Guyonnet‐Duperat¹,

Geverink²,

Plastow³

et al. 2006

Genetics

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We previously reported that corticosteroid-binding globulin gene (Cbg) may be the causal gene of a quantitative trait locus associated with cortisol levels, fat deposition, and muscle content in a pig intercross. Sequence analysis of parental animals allowed us to identify four amino-acid substitutions. Here we have examined if any of these single amino acid substitutions could be responsible for the difference in CBG binding and affinity for cortisol between the parental breeds, using in vitro assays of Cbg variants after transfection of mammalian cells. Additionally, the Cbg coding region was analyzed in samples from a synthetic pig line to study association between polymorphism and CBG biochemical properties, carcass composition, and meat quality. Both in vitro transfection assays and the association studies suggest a role of the Arg307Gly mutation in increasing CBG capacity (by .70%) and decreasing CBG affinity for cortisol (by 30%). The Ile265Val substitution may also have an effect on decreasing CBG affinity for cortisol by 25%. The mutations Ser15Ile and Thr257Met do not seem to have an effect on CBG parameters. The Arg307Gly substitution was the only mutation associated with a parameter of meat quality and no mutation was linked to carcass composition.

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Specific binding of human corticosteroid-binding globulin to cell membranes.

Abstract: Specific binding sites for corticosteroid-binding globulin were

Cited by 77 publications

References 42 publications

Kinetics of Circulating Corticosterone in Infant Rats

Kinetics of Circulating Corticosterone in Infant Rats

Cellular uptake of steroid carrier proteins—Mechanisms and implications

Functional Implication of an Arg307Gly Substitution in Corticosteroid-Binding Globulin, a Candidate Gene for a Quantitative Trait Locus Associated With Cortisol Variability and Obesity in Pig

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