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- A J Hodgson and J W Funder.
- Am. J. Physiol. 1978 Sep 1; 235 (3): R115-20.
AbstractIn cytoplasmic fractions of liver and kidney prepared from adrenalectomized guinea pigs, tritiated dexamethasone ([3H]DM) is bound with a very low affinity (Kd 4 degrees C greater than or equal to 2 X 10(-7) M). By competition studies, the specificity of this binding was shown to be comparable with that for [3H]DM binding to glucocorticoid receptors in other species. In addition, cytoplasmic preparations from guinea pig liver and kidney appear to inhibit the binding of [3H]DM to rat glucocorticoid receptors under a variety of experimentally determined circumstances. It is proposed that such inhibitory activity may reflect a system of [3H]DM sequestration, perhaps by metabolizing enzymes with a high combining power for glucocorticoids. Both low affinity glucocorticoid receptors and avid binding to sites of metabolism may represent additive cellular bases for the apparent corticoresistance of the guinea pig.
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