Peroxidases induced in rat uterus by estrogen administration. I. Synthesis, secretion and immunofluorescent demonstration of fluid enzymes.
Uterine secretions are of fundamental importance in reproductive processes. Uterine activity is related to the hormonal status of the animal, and peroxidase is a major estrogen-regulated glycoprotein in the uterine fluid. Estrogen-induced peroxidase (EIP) can be separated into several isoelectric variants. SDS-PAGE electrophoresis suggested that EIP has a molecular weight of approximately 70kd. The observed pattern of EIP isoforms appears to result from differential glycosylation of a single protein species because neuraminidase treatment resulted in a gradual shift of EIP to the more basic isoelectric variants prior to abolishing enzymatic activity. Antibody raised against one of the major isoelectric variants of EIP demonstrated uterine epithelial cells by immunofluorescence indicating an epithelial cell localization for the enzyme. Radioactive bands comigrating with major EIP isozymes were detected in uterine fluid by in vivo labeling after estrogen treatment. The results of these studies support the hypothesis that EIP is a major estrogen-regulated secretory protein of the uterine epithelium.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction; D004967:Estrogens / Q000494:pharmacology; D005260:Female; D005455:Fluorescent Antibody Technique; D008970:Molecular Weight; D010544:Peroxidases / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D014599:Uterus / Q000166:cytology / Q000187:drug effects / Q000201:enzymology*
D004967:Estrogens; D010544:Peroxidases