Developmental regulation of glycosyltransferases involved in biosynthesis of asparagine-linked glycoproteins in mouse mammary gland.

Three glycosyltransferases, namely N-acetylglucosaminyl-1-phosphotransferase, mannosyltransferase and glucosyltransferase, involved in the biosynthesis of asparagine-linked glycoproteins in the mouse mammary gland, were identified by characterization of the products formed by these enzymes. The tissue capacities of the glycosyltransferases, measured as pmol product formed g tissue-1 min-1, increase during developmental cycle of the gland until, at late lactational stage, they reach more than 34, 14 and 60 times, respectively, the basal level found in the tissue of virgin animals. Among the three enzymes at late lactational stage the specific activities of glucosyltransferase and N-acetylglucosaminyl-1-phosphotransferase increase 7-fold and 4-fold respectively, whereas mannosyltransferase shows a mere 1.4-fold increase during tissue development. All of the enzymes, both in terms of tissue capacity and specific activity, return to the basal levels of the virgin gland one month after the end of lactation. The activities of the three enzymes in the lactating gland decrease precipitously following treatment of mice with bromocriptine, a drug that interferes with the release of prolactin from the pituitary gland and thereby inhibits milk synthesis and secretion. These results indicate that the three glycosyltransferases are developmentally regulated during the growth and differentiation of the mouse mammary gland.