Journal article
[3H]Dexamethasone Binding to Plasma Membrane-Enriched Fractions from Liver of Nonadrenalectomized Rats
Endocrinology (Philadelphia), Vol.123(3), pp.1642-1651
09/1988
DOI: 10.1210/endo-123-3-1642
PMID: 2841103
Abstract
Using liver from nonadrenalectomized adult male rats, binding sites for [3H]dexamethasone in particulate fractions are demonstrated. The binding is thermolabile, saturable, and specific for glucocorticoid. The apparent dissociation constant (Kdapp) for [3H]dexamethasone (0.48 ± 0.084 μM) is 60-fold greater than that for cytosolic receptor (7.9 ± 1.5 nM). The Kdapp for [3H]cortisol in particulate fractions is 2.5-fold lower than for [3H]dexamethasone (Kdapp = 0.18 μM). The binding capacities for particulate and cytosolic glucocorticoidbinding sites also differ significantly, with particulate sites at least 9.1-fold more concentrated than cytosolic sites in liver tissue. Particulate sites are determined in Percoll density gradients to have a density of 1.039 g/cc. Saturable [3H]dexamethasone radioactivity coelutes from these gradients with the plasma membrane marker enzyme 5′-nucleotidase. Adrenalectomy causes the complete loss of particulate binding sites by 6 days postadrenalectomy; however, these sites can be regenerated to two thirds of the nonadrenalectomy level by 20–30 days postadrenalectomy
Details
- Title: Subtitle
- [3H]Dexamethasone Binding to Plasma Membrane-Enriched Fractions from Liver of Nonadrenalectomized Rats
- Creators
- FREDERICK W QUELLERICHARD V SMITHCHRISTINE A HRYCYNATIMOTHY D KALIBANJOAN A CROOKSJANE M O'BRIEN
- Resource Type
- Journal article
- Publication Details
- Endocrinology (Philadelphia), Vol.123(3), pp.1642-1651
- DOI
- 10.1210/endo-123-3-1642
- PMID
- 2841103
- ISSN
- 0013-7227
- eISSN
- 1945-7170
- Language
- English
- Date published
- 09/1988
- Academic Unit
- Neuroscience and Pharmacology; Internal Medicine
- Record Identifier
- 9984040494702771
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