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Alterations in specificity of the gluco corticoid receptor with temperature in rat splenic lymphocytes



Alterations in specificity of the gluco corticoid receptor with temperature in rat splenic lymphocytes



Journal of Steroid Biochemistry 10(1): 21-30



Rat splenic lymphocytes contain specific, saturable glucocorticoid receptors. When suspensions of these cells were incubated at 0.degree. C in the presence of [3H]-triamcinolone acetonide ([3H]-TA), 80% of receptor-bound steroid was found associated with the cytoplasm, whereas at 37.degree. C, 80% of [3H]-TA binding was associated with the nucleus. The equilibrium dissociation constant for interaction of [3H]-TA with the cytoplasmic receptor at 0.degree. C is 5.6 nM while that for nuclear binding at 37.degree. C was 0.85 nM, suggesting an increase in receptor affinity for [3H]-TA at physiological temperatures. Specificity studies showed a high degree of glucocorticoid specificity at 37.degree. C in cytoplasm and nucleus, with little competition observed for either progesterone (P) or cortexolone (S). At 0.degree. C, P and S competed with [3H]-TA for receptor binding as effectively as dexamethasone. Estradiol-17.beta., testosterone, 5.alpha.-dihydrotestosterone and cortisone did not compete under any of these conditions. When cells were incubated at 0.degree. C in the presence of 0.02 .mu.M [3H]-TA and concentrations of P and S ranging from 0.04-2.56 .mu.M, [3H]-TA binding was inhibited at steroid concentrations as low as 0.1 .mu.M. If these same cells were then warmed to 37.degree. C [3H]-TA binding in cytoplasm and nucleus was inhibited only at P and S concentrations .gtoreq. 1 .mu.M. There is, concomitant with increasing temperature, an increase in affinity and specificity of the receptor for active glucocorticoids. This specificity change was regarded as evidence for a conformational change in the hormone-receptor complex coincident with activation.

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Accession: 004703926

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PMID: 513714



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