Estradiol stimulates a uterine plasma membrane protease activator.

An estrogen-regulated arginine esteropeptidase is present in the immature rat uterus. The enzymatic complex consists of a membrane-bound activator and a soluble proenzyme. The activator is under strong estrogen control; its activity increases 10-fold 3 h after a single dose of 17 beta-estradiol. The subcellular localization of the activator is determined by a radioactive assay of fractions prepared by sucrose density centrifugation. The distribution of activity parallels the distribution of two plasma membrane markers, Mg2+-ATPase and 5'-nucleotidase. Electron micrographic visualization of the gradient fractions containing the activator reveals a population of vesicles 0.2-0.5 micron in diameter.