Stabilization of glucocorticoid-receptor interactions in vitro by removal of RNA bound to receptor complexes in vivo.
The dissociation of the steroid from glucocorticoid-receptor-RNA complexes at 5 degrees C was evaluated in cytosolic and nuclear extracts prepared from Hela cells crosslinked in vivo with glutaraldehyde. Sample treatment with catalytically active RNase A prevented the dissociation of the steroid which was induced by sample dilution with buffer. Dilution of the extracts with boiled cytosol, instead, stabilized steroid-receptor interactions. We conclude that some heat-stable factor should be also associated with glucocorticoid-receptor-RNA complexes from crosslinked cells, stabilizing steroid-receptor interactions, and we propose that it could counteract the labilizing effect of RNA.
Istituto di Chimica Biologica, Universit di Modena, Italy.
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D001685:Biological Factors / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism; D003432:Cross-Linking Reagents; D003600:Cytosol / Q000378:metabolism; D003907:Dexamethasone / Q000378:metabolism; D005938:Glucocorticoids / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D012313:RNA / Q000378:metabolism*; D011965:Receptors, Glucocorticoid / Q000378:metabolism*; D012259:Ribonuclease, Pancreatic
D001685:Biological Factors; D003432:Cross-Linking Reagents; D005938:Glucocorticoids; D011965:Receptors, Glucocorticoid; D012313:RNA; D003907:Dexamethasone; D012259:Ribonuclease, Pancreatic