[3H]dexamethasone binding to plasma membrane-enriched fractions from liver of nonadrenalectomized rats.

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 microM) 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 microM). The binding capacities for particulate and cytosolic glucocorticoid-binding 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.