Specific binding sites for corticosterone in isolated cells and plasma membrane from rat liver

Trueba, Miguel; Ibarrola, I.; Ogiza, Kepa; Marino, Aída; Macarulla, J. M.

doi:10.1007/bf01872394

Cited by 30 publications

(17 citation statements)

References 57 publications

(55 reference statements)

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“…This result is incompatible with a previous report that hydrocortisone-BSA-gold enters the hepatocyte nuclei (Nishimura and Nakano, 1999). In the rat liver cell membrane, corticosterone exhibits higher binding affinity than hydrocortisone in competition experiments (Suyemitsu and Terayama, 1975;Truebe et al, 1991). The administration of estrogen to rats results in the intranuclear accumulation of lysosomal enzymes in steroid target cells such as cells of the preputial gland (Szego et al, 1974).…”

Section: Discussioncontrasting

confidence: 70%

Immunocytochemical Localization of Bovine Serum Albumin (BSA) in the Liver and Testis of Rats injected with Testosterone-BSA, Hydrocortisone-BSA or Corticosterone-BSA.

Nishimura

Nakano

2000

Cell Struct. Funct.

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ABSTRACT. Through observations of colloidal gold with silver enhancement, we have demonstrated that 2-nm colloidal gold labeled-testosterone-bovine serum albumin (BSA) conjugate or hydrocortisone-BSA conjugate injected intravenously enters the hormone-target cell nuclei of rats (Nishimura and Ichihara, 1997; Nakano, 1997, 1999). To confirm immunocytochemically whether the nature of BSA in the steroid hormone-BSA conjugates (steroid-BSAs) remains intact in the hormone-target cell nuclei, testosterone-BSA, hydrocortisone-BSA or corticosterone-BSA was injected into the vascular system of rats, then the liver and testes of rats killed 2 h postinjection were reacted with FITC-conjugated anti-BSA antibody, and examined under fluorescence microscopy and confocal laser scanning microscopy. In the liver of rat injected with testosterone-BSA, the fluorescence was observed in the nuclei of endothelial cells, but not in the nuclei of hepatocytes, hepatic stellate cells and Kupffer cells. In the liver of rat injected with hydrocortisone-BSA, intense fluorescence was seen in the nuclei of hepatic stellate cells, but did not seem to be present in the nuclei of the other three kinds of cells. In the liver of rat injected with corticosterone-BSA, the fluorescence seemed to be in a few nuclei of hepatic stellate cells, and appeared as speckles in a few nuclei of the hepatocytes and Kupffer cells. In some seminiferous tubules of rat injected with testosterone-BSA, fluorescence was observed in the nuclei of spermatocytes and spermatids. These results suggest that BSA conjugated with steroid hormone can enter the hormone-target cell nuclei with its antigenicity kept intact, and that the fate of steroid-BSAs is decided at the cell membrane level.Key words: testosterone-BSA/hydrocortisone-BSA/corticosterone-BSA/target cell nuclei/ in vivo/immunocytochemistry Steroid hormones circulate in blood plasma in three physical states: free, albumin-bound, and bound to serum steroid binding proteins such as sex hormone-binding globulin (SHBG) and corticosteroid-binding globulin (CBG) (Kuhn,

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Section: Discussioncontrasting

confidence: 70%

Immunocytochemical Localization of Bovine Serum Albumin (BSA) in the Liver and Testis of Rats injected with Testosterone-BSA, Hydrocortisone-BSA or Corticosterone-BSA.

Nishimura

Nakano

2000

Cell Struct. Funct.

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“…Post-nuclear homogenates were collected following centrifugation at 200 ϫ g for 2 min, and the microsomal aggregates were sedimented by centrifugation at 3,000 ϫ g for 15 min. Plasma membranes from HU-VEC, rat liver, heart, and kidney were isolated by sucrose gradient centrifugation (29,31,32). Plasma membrane purity and exclusion of cytosolic fraction were assessed with measurements of alkaline phosphatase, 5Ј-nucleotidase, and lactate dehydrogenase, using commercial kits.…”

Section: Methodsmentioning

confidence: 99%

Dehydroepiandrosterone Activates Endothelial Cell Nitric-oxide Synthase by a Specific Plasma Membrane Receptor Coupled to Gαi2,3

Liu

Dillon

2002

Journal of Biological Chemistry

269

179

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The adrenal steroid dehydroepiandrosterone (DHEA) has no known cellular receptor or unifying mechanism of action, despite evidence suggesting beneficial vascular effects in humans. Based on previous data from our laboratory, we hypothesized that DHEA binds to specific cell-surface receptors to activate intracellular Gproteins and endothelial nitric-oxide synthase (eNOS). We now pharmacologically characterize a putative plasma membrane DHEA receptor and define its associated G-proteins. The physiological role of the adrenal steroid dehydroepiandrosterone (DHEA) 1 is not known. There are widespread data suggesting a beneficial effect of DHEA on vascular function. Extensive epidemiologic evidence shows an inverse correlation between circulating DHEA levels and the prevalence of atherosclerotic and cardiovascular diseases (1-5). There are few human intervention studies focused on vascular outcomes of DHEA administration, and these are not of a size or duration to define whether DHEA therapy has an effect on cardiovascular morbidity or mortality. Available studies do suggest a beneficial effect on atherosclerosis (6). Studies of the short term effect of DHEA on human vascular function, using sophisticated assays of vascular function, are beginning to emerge. Williams et al. (7) showed a significant increase in flow-mediated dilatation and systemic arterial compliance in postmenopausal women taking DHEA for 3 months. DHEA reduces atherosclerosis, decreases the accumulation of cholesterol in aortic and coronary arteries (8, 9), and inhibits platelet aggregation (10) in various animal models. DHEA also affects growth factor-induced mitogenesis and proliferation of vascular smooth muscle cells (11-13). However, the molecular mechanisms by which DHEA acts to protect from atherosclerotic and cardiovascular diseases are still unknown. Furthermore, it is unclear whether the effect on vascular tissues is related to DHEA or to its metabolites, which include estradiol.Steroid hormones are known to bind specific intracellular receptors, which function as ligand-dependent gene transcription factors (14). However, previous efforts to isolate an intracellular receptor for DHEA have failed (15-18). In contrast to this classical pathway of steroid hormone action, there are also rapid, plasma membrane-dependent, non-genomic effects of steroids in various tissues, which lead to important physiological responses (19 -24). Plasma membrane-associated receptors are postulated to mediate these non-genomic actions of steroids. Functional plasma membrane binding sites have been identified for several steroids, including estrogen, vitamin D, and progesterone (25-28). However, besides the receptor for estrogen, no plasma membrane steroid receptor has yet been unequivocally identified and characterized.We have found that DHEA stimulates nitric oxide (NO) generation within minutes from bovine aortic endothelial cells (BAEC).2 Furthermore, DHEA conjugated to bovine serum albumin (BSA) had similar effects. These cellular responses to DHEA were spe...

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“…Further analysis of the high-affinity binding site by SDS-PAGE showed two protein subunits of 52 and 57 kDa, respectively, and binding affinities distinct from those of the glucocortocoid receptor (GR) (218). In addition, the binding of corticosterone to murine and rat liver plasma membranes, to rat kidney and rat brain plasma membranes, and to calf adrenal cortex plasma membranes has been shown (219,486,487 and others).…”

Section: Glucocorticoidsmentioning

confidence: 96%

Nongenomic Steroid Action: Controversies, Questions, and Answers

Lösel

Falkenstein

Feuring

et al. 2003

Physiological Reviews

502

321

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Lösel, Ralf M., Elisabeth Falkenstein, Martin Feuring, Armin Schultz, Hanns-Christian Tillmann, Karin Rossol-Haseroth, and Martin Wehling. Nongenomic Steroid Action: Controversies, Questions, and Answers. Physiol Rev 83: 965–1016, 2003; 10.1152/physrev.00003.2003.—Steroids may exert their action in living cells by several ways: 1) the well-known genomic pathway, involving hormone binding to cytosolic (classic) receptors and subsequent modulation of gene expression followed by protein synthesis. 2) Alternatively, pathways are operating that do not act on the genome, therefore indicating nongenomic action. Although it is comparatively easy to confirm the nongenomic nature of a particular phenomenon observed, e.g., by using inhibitors of transcription or translation, considerable controversy exists about the identity of receptors that mediate these responses. Many different approaches have been employed to answer this question, including pharmacology, knock-out animals, and numerous biochemical studies. Evidence is presented for and against both the participation of classic receptors, or proteins closely related to them, as well as for the involvement of yet poorly understood, novel membrane steroid receptors. In addition, clinical implications for a wide array of nongenomic steroid actions are outlined.

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Specific binding sites for corticosterone in isolated cells and plasma membrane from rat liver

Cited by 30 publications

References 57 publications

Immunocytochemical Localization of Bovine Serum Albumin (BSA) in the Liver and Testis of Rats injected with Testosterone-BSA, Hydrocortisone-BSA or Corticosterone-BSA.

Immunocytochemical Localization of Bovine Serum Albumin (BSA) in the Liver and Testis of Rats injected with Testosterone-BSA, Hydrocortisone-BSA or Corticosterone-BSA.

Dehydroepiandrosterone Activates Endothelial Cell Nitric-oxide Synthase by a Specific Plasma Membrane Receptor Coupled to Gαi2,3

Nongenomic Steroid Action: Controversies, Questions, and Answers

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