Stabilization of glucocorticoid receptor association with RNA by a low molecular weight factor from rat liver cytosol.
A small (Mr less than 500) anionic, heat-stable molecule has been identified in rat liver cytosol which prevents the RNase-induced decrease in the glucocorticoid receptor sedimentation properties which we described previously. This factor, which can be removed by dialysis, molecular exclusion chromatography, or ultrafiltration, functions as a true stabilizer of the RNA-glucocorticoid receptor association, and not as a RNase inhibitor. Preliminary characterization shows that the factor is not a protein, nucleic acid, or nucleotide, is not absorbed by activated dextran-charcoal, and is unaffected by extraction with organic solvents. This factor prevents activation of the glucocorticoid receptor by dilution. The relationship of this stabilization factor to a low molecular weight activation inhibitor described by others is discussed.
Anderson
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Tymoczko
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JL
D000818:Animals; D002499:Centrifugation, Density Gradient; D002845:Chromatography / Q000379:methods; D003600:Cytosol / Q000378:metabolism; D008099:Liver / Q000378:metabolism; D008297:Male; D008970:Molecular Weight; D012313:RNA / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D011965:Receptors, Glucocorticoid / Q000378:metabolism*; D012260:Ribonucleases / Q000037:antagonists & inhibitors; D012995:Solubility
D011965:Receptors, Glucocorticoid; D012313:RNA; D012260:Ribonucleases