[Characterization of dexamethasone-binding protein from the rat myocardium].
Kinetic and apparent equilibrium studies of the binding reaction steroid + receptor in equilibrium with steroid - receptor (SR) reveal a specific binding of dexamethasone and several other synthetic and natural glucocorticoids to a limited number of binding sites in the myocardium cytosol. In contrast to the binding sites of natural steroids the dexamethasone binding sites are heat sensitive. In the sucrose gradient with a low ionic strength, SR-complex sedimented at 9.5 S, heating to 25 degrees C for 20 min or increase in the ionic strength lead to a decrease in the molecular weight of the complex. A rapid temperature-dependent nuclear uptake of cytoplasmic SR-complexes was demonstrated, which was not saturable at physiologic concentrations of SR-complexes and a low ionic strength of the incubation media. All the described properties of dexamethasone-binding protein are characteristic of receptors involved in the biological effects of glucocorticoids.
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D003907:Dexamethasone / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D009206:Myocardium / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D011965:Receptors, Glucocorticoid / Q000302:isolation & purification / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*; D013696:Temperature
D011965:Receptors, Glucocorticoid; D011987:Receptors, Steroid; C028697:dexamethasone receptor; D003907:Dexamethasone
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