A role for glucocorticosteroids in the evolution of the rat fetal liver erythropoiesis in vivo has been proposed; accordingly suppressible binding of [3H]dexamethasone by intact liver erythroid cells at 4 °C has been described. The nature of this binding was further investigated in the present paper. Suspensions of cells of the erythroid line were prepared from liver erythropoietic tissue obtained from fetuses aged 15 or 16 days. Suppressible binding of [3H]dexamethasone was studied on these suspensions. After incubation at 4 °C, approximately 89 per cent of this binding was located in the cytosol (100 000 g supernatant fraction), was excluded from Sephadex G-50 columns and was not adsorbed on activated charcoal; 11·3 ± 2·6 (s.d.) per cent (n = 4) of the suppressible binding was present in the nucleus. When cells prelabelled with [3H]dexamethasone at 4 °C were warmed to 37 °C, 52 ± 10 per cent (n = 5) of the suppressible binding was rapidly transferred to the nucleus. The suppressible radioactivity present in the cytosols at 4 °C was eluted from diethylaminoethyl (DEAE)–cellulose columns, in the presence of molybdate, as a single peak (peak II) at phosphate concentrations between 200 and 250 mmol/l. When these cytosols were warmed at 25 °C before chromatography, the radioactivity was eluted from DEAE-cellulose as a major peak (peak I) at phosphate concentrations between 50 and 70 mmol/l, and as a smaller peak corresponding to peak II. The presence of molybdate during the incubation at 25 °C prevented the formation of peak I. The suppressible binding present in the cytosols of cells incubated at 37 °C was eluted from DEAE–cellulose columns in two equivalent peaks corresponding to peaks I and II. It was concluded that [3H]dexamethasone was bound to a macromolecular component sharing the properties generally ascribed to the receptor of glucocorticosteroids.
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Online ISSN: 1479-6805
Print ISSN: 0022-0795
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