PubMed · 13477578
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W M JACOBS, M A LEAZAR, J E LINDLEY. 1957. Functional uterine bleeding.. https://pubmed.ncbi.nlm.nih.gov/13477578/
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The aim of metroplasties is to restore a normal uterine anatomy to improve obstetrical outcomes in some uterine malformations. The hysteroscopic septoplasty cures the septate uterus. It is an effective procedure in the case of recurrent abortion losses. It probably improves the rate of live birth in women without obstetrical antecedent. For some authors, it could be considered at the time of the diagnosis, because of the simplicity of the gesture and the low complication rate. The enlarging hysteroscopic metroplasty has certainly a positive impact on the obstetrical outcome in patients presenting a uterine hypotrophy or dysmorphy, in particular in women exposed in utero to DES. However, the proofs are poor to propose this procedure as first-line treatment, apart from specific cases such as old null gravid patient or before inclusion in an Assisted Reproductive Techniques (ART) program.
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To search for endogenous estrogens that may have preferential binding affinity for human estrogen receptor (ER) alpha or beta subtype and also to gain insights into the structural determinants favoring differential subtype binding, we studied the binding affinities of 74 natural or synthetic estrogens, including more than 50 steroidal analogs of estradiol-17beta (E2) and estrone (E1) for human ER alpha and ER beta. Many of the endogenous estrogen metabolites retained varying degrees of similar binding affinity for ER alpha and ER beta, but some of them retained differential binding affinity for the two subtypes. For instance, several of the D-ring metabolites, such as 16 alpha-hydroxyestradiol (estriol), 16 beta-hydroxyestradiol-17 alpha, and 16-ketoestrone, had distinct preferential binding affinity for human ER beta over ER alpha (difference up to 18-fold). Notably, although E2 has nearly the highest and equal binding affinity for ER alpha and ER beta, E1 and 2-hydroxyestrone (two quantitatively predominant endogenous estrogens in nonpregnant woman) have preferential binding affinity for ER alpha over ER beta, whereas 16 alpha-hydroxyestradiol (estriol) and other D-ring metabolites (quantitatively predominant endogenous estrogens formed during pregnancy) have preferential binding affinity for ER beta over ER alpha. Hence, facile metabolic conversion of parent hormone E2 to various metabolites under different physiological conditions may serve unique functions by providing differential activation of the ER alpha or ER beta signaling system. Lastly, our computational three-dimensional quantitative structure-activity relationship/comparative molecular field analysis of 47 steroidal estrogen analogs for human ER alpha and ER beta yielded useful information on the structural features that determine the preferential activation of the ER alpha and ER beta subtypes, which may aid in the rational design of selective ligands for each human ER subtype.