Abstract
Although glucocorticoid receptors have been extensively studied in a variety of tissues, the precise nature of the receptor protein still remains unknown. To further characterize this protein we assessed the effects of various lectins on [ 3H]dexamethasone binding to prepurified preparations of rat liver glucocorticoid receptor. Among the lectins tested only Ulex europeus and Lens culinaris induced a concentration-related decrease in [ 3H]dexamethasone binding. Following Ulex europeus or Lens culinaris exposure Scatchard analysis showed that these lectins led to a 3-fold reduction in receptor affinity without influencing the concentration of binding sites. These results provide new experimental evidence that rat liver glucocorticoid receptor would possess α- l-fucosyl and α- d-mannopyranoside residues in close proximity to the glucocorticoid receptor binding domain.
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