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  • Title: Relative binding affinity of steroids for the corticosterone receptor system in rat hippocampus.
    Author: De Kloet ER, Veldhuis HD, Wagenaars JL, Bergink EW.
    Journal: J Steroid Biochem; 1984 Aug; 21(2):173-8. PubMed ID: 6482428.
    Abstract:
    In cytosol of the hippocampus corticosterone displays highest affinity for the sites that remain available for binding in the presence of excess RU 26988, which is shown to be a "pure" glucocorticoid. A rather high affinity (greater than or equal to 25%) was found for 11 beta-hydroxyprogesterone, 21-hydroxyprogesterone, 5 alpha-corticosterone, 19-nor-deoxycorticosterone, 11-deoxycorticosterone and cortisol. A moderate affinity (greater than 5% and less than 25%) was displayed by about 14 steroids among which progesterone, aldosterone, 9 alpha-fluorocortisol and dexamethasone. Corticosterone also shows highest affinity to plasma transcortin and thymus cytosol in the presence of RU 26988. However, the rank-order in affinity by the competing steroids was distinctly different from that observed in the hippocampus; cf. aldosterone and dexamethasone displaced [3H]corticosterone from sites unoccupied by RU 26988 in the hippocampus but not from transcortin or sites in thymus cytosol. In thymus cytosol some potent glucocorticoids have higher affinity for the [3H]dexamethasone labeled sites than dexamethasone. The binding of [3H]dexamethasone in thymus cytosol is completely abolished in the presence of a 100-fold excess of RU 26988. We conclude that our data support the evidence for RU 26988 as a selective ligand for glucocorticoid receptors. RU 26988 leaves binding sites available with highest affinity for corticosterone in hippocampus cytosol that are distinct from transcortin-like sites as found in thymus cytosol or from plasma transcortin.
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