Effect of cross-linking on glucocorticoid receptor activation.
Chick thymus cytosol glucocorticoid receptor complexed with [3H]-triamcinolone acetonide was heat-activated after treatment with diimidates of varying chain length. Diimidates with maximal effective reagent length shorter than 0.5 nm influenced DNA-cellulose binding only slightly, whereas sebacic diimidate (maximal effective reagent length 1.21 nm) blocked activation completely. Coupled activation - deactivation process induced in the presence of calcium was again inhibited only by the longer diimidates. Sebacic diimidate treated complex had a molecular mass similar to that of the molybdate stabilized nonactivated complex, as judged by gel permeation chromatography. It is suggested that prevention of size reduction by cross-linking blocks receptor activation as well.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002645:Chickens; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D007096:Imidoesters / Q000494:pharmacology; D011965:Receptors, Glucocorticoid / Q000187:drug effects / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013950:Thymus Gland / Q000032:analysis; D014222:Triamcinolone Acetonide / Q000378:metabolism
D003432:Cross-Linking Reagents; D007096:Imidoesters; D011965:Receptors, Glucocorticoid; D011987:Receptors, Steroid; D014222:Triamcinolone Acetonide