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.
D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D002462:Cell Membrane / Q000187:drug effects; D002499:Centrifugation, Density Gradient; D004789:Enzyme Activation; D004958:Estradiol / Q000494:pharmacology*; D005260:Female; D001121:Lysine Carboxypeptidase / Q000378:metabolism; D008854:Microscopy, Electron; D010447:Peptide Hydrolases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D014599:Uterus / Q000187:drug effects / Q000201:enzymology*
D004958:Estradiol; D010447:Peptide Hydrolases; D001121:Lysine Carboxypeptidase; D017301:Ca(2+) Mg(2+)-ATPase