Transformation of glucocorticoid-receptor complexes is accompanied by dissociation of oligomers in intact cells.
The association of glucocorticoid-receptor complexes with other components in vivo has been evaluated by chemical crosslinking of hormone-treated cells. When cells were incubated with hormone at 2 degrees C, before being subjected to crosslinking, most glucocorticoid-receptor complexes were found untransformed, as judged by DEAE-cellulose chromatography, and sedimented as 11-6 S oligomers in sucrose gradients containing 0.3 M NaCl. If crosslinking was performed after cells were treated with hormone at 37 degrees C, about 60% of cytosolic glucocorticoid-receptor complexes were found transformed, and sedimented as 4 S monomers.
Rossini
G P
GP
Istituto di Chimica Biologica, Università di Modena, Italy.
Malaguti
C
C
D000447:Aldehydes / Q000494:pharmacology*; D003432:Cross-Linking Reagents; D005938:Glucocorticoids / Q000378:metabolism*; D005976:Glutaral / Q000494:pharmacology*; D006367:HeLa Cells; D006801:Humans; D046911:Macromolecular Substances; D011487:Protein Conformation; D011965:Receptors, Glucocorticoid / Q000378:metabolism*; D013329:Structure-Activity Relationship
D000447:Aldehydes; D003432:Cross-Linking Reagents; D005938:Glucocorticoids; D046911:Macromolecular Substances; D011965:Receptors, Glucocorticoid; D005976:Glutaral