Biochemical similarity of rat pituitary and CNS TRH receptors.

Chemical properties of receptor binding sites for thyrotropin-releasing hormone (TRH) in rat pituitary, retina, amygdala and hypothalamus were compared by examining the influence of sulfhydryl reagents on specific binding of 3H-TRH ([3H]MeTRH). Dithiothreitol-induced reduction of disulfide bonds, alkylation of thiol residues by N-ethylmaleimide and their oxidation by 5,5-dithiobis(2-nitrobenzoic acid) (DTNB), all produced marked reduction of [3H]MeTRH binding, which could be prevented in part by preincubation with exogenous TRH. In all tissues, concentration-dependent loss of binding activity was observed following exposure to micromolar heavy metals and mono- and divalent cations, with apparent additive effects between cations and DTT and NEM. Most changes appeared to reflect only a decrease in receptor density (Bmax). The similar sensitivity of all tissues to these compounds complements existing evidence for a close resemblance of TRH receptors in the CNS and pituitary.