Steroid receptor domain conformations and hormone antagonism.
Receptor stabilization, activation, dimerization, and binding to cognate sequences on DNA are possible with antagonists. Tissue-, steroid-, and species-dependent differences in all these parameters, despite identical structure of the receptor from various sources for any one steroid hormone class, suggest posttranslational modifications of a primary gene product. Clinically, it is now possible to visualize receptor-specific antihormone therapy of various steroid-dependent maladies (cancer of the breast, uterus, or prostate, Cushing's disease, hypertensive disorders, etc.) where surgical resection has been hitherto most effective. Amelioration of adverse side effects, associated with currently available semispecific derivatives, should permit wider applications in a variety of other situations in the near future.
Agarwal
M K
MK
Hormone Laboratory, Centre Universitaire des Cordeliers, Paris.
D000818:Animals; D001943:Breast Neoplasms / Q000188:drug therapy; D003480:Cushing Syndrome / Q000188:drug therapy; D004268:DNA-Binding Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D005260:Female; D006727:Hormone Antagonists / Q000737:chemistry* / Q000627:therapeutic use; D006728:Hormones / Q000737:chemistry* / Q000627:therapeutic use; D006801:Humans; D006973:Hypertension / Q000188:drug therapy; D008297:Male; D011471:Prostatic Neoplasms / Q000188:drug therapy; D011987:Receptors, Steroid / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D014594:Uterine Neoplasms / Q000188:drug therapy
D004268:DNA-Binding Proteins; D006727:Hormone Antagonists; D006728:Hormones; D011987:Receptors, Steroid