Evidence for differences in the steroid binding domains of the glucocorticoid receptor versus the idiotype antibody

Abstract

Triamcinolone acetonide (TA), coupled to bovine serum albumin, was used to obtain a polyclonal anti-TA antibody in the rabbit. This idiotype differed from rat glucocorticoid receptor and transcortin in several respects. RU 38486, a synthetic antagonist with high affinity for the receptor, could neither bind the anti-TA antibody nor displace the idiotype bound 3H-TA. Similarly, corticosterone, the natural rodent ligand, had no affinity for the idiotype. These results imply differences in the conformation and topology of the corticoid binding domains, contrary to the current notion where all agonists and antagonists would saturate an identical configuration.