Article révisé par les pairs
Résumé : In a previous paper, we reported that nafoxidine (UA) stimulated the synthesis of a uterine protein showing the same electrophoretic mobility as the 'estrogen-induced protein' (E2-IP) first described by Notides and Gorski. In the present work, we analyzed the IP-containing electrophoretic zone by SDS polyacrylamide-gel electrophoresis, and found that estradiol-17β (E2) and nafoxidine stimulated the synthesis of different proteins. As expected, estradiol-17β stimulated the synthesis of the E2-IP of 46,000 M(r). On the other hand, UA stimulated the synthesis of 27,000 and 30,000 M(r) proteins (UA-IP). These UA-IP were not precipitated by an antiserum raised against E2-IP. Therefore, UA-IP appear to be independent entities and not degradation or precursor products of E2-IP. Both UA-IP are constitutively present in the uterus and even in higher relative amounts in rat brain. The present finding, that an 'anti-estrogen', such as nafoxidine, stimulates the synthesis of different proteins than estrogen, provides a new approach to the study of the molecular mechanism of estrogen action.