Synthesis of placental protein 12 by human endometrium.

We have previously shown that placental protein 12 (PP12) is synthesized and secreted by human term pregnancy decidua in vitro. In the present study, fragments of proliferative and secretory phase endometrium were cultured in media in the presence and absence of progesterone (P) and 17 beta-estradiol (E2) for 96 h. The PP12 concentrations in the media and tissues were measured by RIA, and de novo synthesis was investigated by measuring the incorporation of [35S]methionine into PP12. Before culture, PP12 could not be detected in any proliferative endometria, whereas all secretory endometria contained PP12. All secretory endometria released PP12 into the medium in the presence and absence of added P and E2. Secretory endometria released significantly more PP12 than proliferative endometria. Three of seven proliferative endometria did not release PP12 in the absence of P, but all did so after P had been added. The addition of P to culture medium caused a 2.4-to over 71-fold increase in PP12 secretion over control values in proliferative endometria and up to a 3.5-fold increase in secretory endometrium. E2 had no significant effect. Cycloheximide totally inhibited the PP12 release induced by P from proliferative endometrium, and in secretory endometrium, it either totally blocked PP12 release or inhibited the stimulation due to P. [35S]Methionine was incorporated into immunoprecipitable PP12 in cultures of secretory and P-treated proliferative phase endometria. These results demonstrate de novo synthesis of PP12 by nonpregnant endometrium in tissue culture and suggest that the biosynthesis and secretion of PP12 by nonpregnant endometrium are regulated by P.