Summary:The behaviour of the antifertilizing synthetic steroid RU 38486 towards human uterine progestin receptor was investigated. RU 38486 competed in the same order of magnitude äs progesterone for the [ 3 H]R 5020 binding site of progestin receptor, whereas R 5020 was unable to compete against [ 3 H]RU 38486. This apparent contradiction could be explained by means of HPLC-chroniatography. HPLC-chromatography with an anion exchange column (MonoQ, Pharmacia, Uppsala, Sweden) showed that [ 3 H]RU 38486 forms at least two stable complexes with uterine cytosol, on one hand with serum albumin, which presents almost 90% of bound radioactivity, and on the other hand with the two native progestin receptor forms, corresponding to 4 S and 8 S receptor forms in sucrose density gradient analysis.Whether reduced binding of salt-activated RU 38486 receptor complexes to DNA-cellulose is due to reduced activation is still uncertain and remains to be further investigated.
H-Markiertes RU38486: Charakterisierung der Bindungseigenschaften in Cytosol aus
Introductionprogesterone in vivo, a property that is manifested "~~ ~^ , , ^ . ,~ intheinterruptionofthelutealphaseofthemenstrual RU 38486 (structure see scheine 1) is the first cycle of ^y pregnancy in women . synthetic steroid possessmg a greater afnnity for the progestin receptor in different animal target tissues There are some indications that the potent antagonist than progesterone, but without exhibiting any agonist effect of RÜ 38486 is related to the essential bioprogestin activity (1-3). Moreover, at large doses chemical Steps following progestin receptor this steroid is capable of antagonizing the effects of occupancy which leäd to the biological response i. e.